|
Name |
Accession |
Description |
Interval |
E-value |
| RecQ |
COG0514 |
Superfamily II DNA helicase RecQ [Replication, recombination and repair]; |
2-476 |
0e+00 |
|
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
Pssm-ID: 440280 [Multi-domain] Cd Length: 489 Bit Score: 716.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 2 DAREVLKTYFGYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIMPGITIVISPLISLMQDQVKSLNDAGIH 81
Cdd:COG0514 4 DALEVLKRVFGYDSFRPGQEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLLPGLTLVVSPLIALMKDQVDALRAAGIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 82 AGFINSSLTDRQIQLVYSRASEGAYIILYVAPERLESSDFIEFASKTKISMVTVDEAHCISQWGQDFRPSYLGIVNFIDR 161
Cdd:COG0514 84 AAFLNSSLSAEERREVLRALRAGELKLLYVAPERLLNPRFLELLRRLKISLFAIDEAHCISQWGHDFRPDYRRLGELRER 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 162 LPKRPVVsAFTATATMEVKEDISCILKLQDPKTVITGFDRENLYFDVE--ITKQKDDYVLDYIKKHPDESGIIYCATRNS 239
Cdd:COG0514 164 LPNVPVL-ALTATATPRVRADIAEQLGLEDPRVFVGSFDRPNLRLEVVpkPPDDKLAQLLDFLKEHPGGSGIVYCLSRKK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 240 VDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAG 319
Cdd:COG0514 243 VEELAEWLREAGIRAAAYHAGLDAEEREANQDRFLRDEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 320 RDGESSRCILLFSPKDIIINKFLLEHKDftdiPSEDViliKERDMRRLNVMEGYCKTTGCLRNYILEYFGEKNTEPCDNC 399
Cdd:COG0514 323 RDGLPAEALLLYGPEDVAIQRFFIEQSP----PDEER---KRVERAKLDAMLAYAETTGCRRQFLLRYFGEELAEPCGNC 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 652962033 400 GNCHKHFIEEDRTEDAKKVINCVFETRGRYGLNIILGTLLGANRARLKELGIVNYRTYGTLKDRSEADLRILINQLI 476
Cdd:COG0514 396 DNCLGPPETFDGTEAAQKALSCVYRTGQRFGAGHVIDVLRGSKNEKIRQFGHDKLSTYGIGKDLSDKEWRSVIRQLL 472
|
|
| recQ |
TIGR01389 |
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 ... |
3-605 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273594 [Multi-domain] Cd Length: 591 Bit Score: 692.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 3 AREVLKTYFGYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIMPGITIVISPLISLMQDQVKSLNDAGIHA 82
Cdd:TIGR01389 1 AQQVLKRTFGYDDFRPGQEEIISHVLDGRDVLVVMPTGGGKSLCYQVPALLLKGLTVVISPLISLMKDQVDQLRAAGVAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 83 GFINSSLTDRQIQLVYSRASEGAYIILYVAPERLESSDFIEFASKTKISMVTVDEAHCISQWGQDFRPSYLGIVNFIDRL 162
Cdd:TIGR01389 81 AYLNSTLSAKEQQDIEKALVNGELKLLYVAPERLEQDYFLNMLQRIPIALVAVDEAHCVSQWGHDFRPEYQRLGSLAERF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 163 PKRPVVsAFTATATMEVKEDISCILKLQDPKTVITGFDRENLYFDVEITKQKDDYVLDYIKKHPDESGIIYCATRNSVDT 242
Cdd:TIGR01389 161 PQVPRI-ALTATADAETRQDIRELLRLADANEFITSFDRPNLRFSVVKKNNKQKFLLDYLKKHRGQSGIIYASSRKKVEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 243 LYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAGRDG 322
Cdd:TIGR01389 240 LAERLESQGISALAYHAGLSNKVRAENQEDFLYDDVKVMVATNAFGMGIDKPNVRFVIHYDMPGNLESYYQEAGRAGRDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 323 ESSRCILLFSPKDIIINKFLLEhkdfTDIPSEDViliKERDMRRLNVMEGYCKTTGCLRNYILEYFGEKNTEPCDNCGNC 402
Cdd:TIGR01389 320 LPAEAILLYSPADIALLKRRIE----QSEADDDY---KQIEREKLRAMIAYCETQTCRRAYILRYFGENEVEPCGNCDNC 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 403 HKHFIEEDRTEDAKKVINCVFETRGRYGLNIILGTLLGANRARLKELGIVNYRTYGTLKDRSEADLRILINQLILDGYLC 482
Cdd:TIGR01389 393 LDPPKSYDATVEAQKALSCVYRMGQRFGVGYIIEVLRGSKNDKILQKGHDQLSTYGIGKDYTQKEWRSLIDQLIAEGLLT 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 483 QTADKYSVIQLGD-ITPLKDPATRVIVRTTQakepdsnKVRQIKKKTDSLTKAGYD--LFDILKALRTQIAREEGMPPYI 559
Cdd:TIGR01389 473 ENDEIYIGLQLTEaARKVLKNEVEVLLRPFK-------VVAKEKTRVQKNLSVGVDnaLFEALRELRKEQADEQNVPPYV 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 652962033 560 VFSDKTLIDMSAKAPLDRAAMLNVSGVGEMKYDKYGQRFINAISSY 605
Cdd:TIGR01389 546 IFSDSTLREMAEKRPATLNALLKIKGVGQNKLDRYGEAFLEVIREY 591
|
|
| PRK11057 |
PRK11057 |
ATP-dependent DNA helicase RecQ; Provisional |
1-610 |
0e+00 |
|
ATP-dependent DNA helicase RecQ; Provisional
Pssm-ID: 182933 [Multi-domain] Cd Length: 607 Bit Score: 534.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 1 MDAREVLKTYFGYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIMPGITIVISPLISLMQDQVKSLNDAGI 80
Cdd:PRK11057 11 SLAKQVLQETFGYQQFRPGQQEIIDAVLSGRDCLVVMPTGGGKSLCYQIPALVLDGLTLVVSPLISLMKDQVDQLLANGV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 81 HAGFINSSLTDRQIQLVYSRASEGAYIILYVAPERLESSDFIEFASKTKISMVTVDEAHCISQWGQDFRPSYLGIVNFID 160
Cdd:PRK11057 91 AAACLNSTQTREQQLEVMAGCRTGQIKLLYIAPERLMMDNFLEHLAHWNPALLAVDEAHCISQWGHDFRPEYAALGQLRQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 161 RLPKRPVVsAFTATATMEVKEDISCILKLQDPKTVITGFDRENLYFDVeITKQKD-DYVLDYIKKHPDESGIIYCATRNS 239
Cdd:PRK11057 171 RFPTLPFM-ALTATADDTTRQDIVRLLGLNDPLIQISSFDRPNIRYTL-VEKFKPlDQLMRYVQEQRGKSGIIYCNSRAK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 240 VDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAG 319
Cdd:PRK11057 249 VEDTAARLQSRGISAAAYHAGLDNDVRADVQEAFQRDDLQIVVATVAFGMGINKPNVRFVVHFDIPRNIESYYQETGRAG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 320 RDGESSRCILLFSPKDIIINKFLLEHKDftDIPSEDVilikERdmRRLNVMEGYCKTTGCLRNYILEYFGEKNTEPCDNC 399
Cdd:PRK11057 329 RDGLPAEAMLFYDPADMAWLRRCLEEKP--AGQQQDI----ER--HKLNAMGAFAEAQTCRRLVLLNYFGEGRQEPCGNC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 400 GNC---HKHFieeDRTEDAKKVINCVFETRGRYGLNIILGTLLGANRARLKELGIVNYRTYGTLKDRSEADLRILINQLI 476
Cdd:PRK11057 401 DICldpPKQY---DGLEDAQKALSCIYRVNQRFGMGYVVEVLRGANNQRIRDYGHDKLKVYGIGRDKSHEHWVSVIRQLI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 477 LDGYLCQTADKYSVIQLGDitplkdpATRVIVR---TTQAKEPDSNKVRqiKKKTDSLTKAGYD--LFDILKALRTQIAR 551
Cdd:PRK11057 478 HLGLVTQNIAQHSALQLTE-------AARPVLRgevSLQLAVPRIVALK--PRAMQKSFGGNYDrkLFAKLRKLRKSIAD 548
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 652962033 552 EEGMPPYIVFSDKTLIDMSAKAPLDRAAMLNVSGVGEMKYDKYGQRFINAISSYLDEHE 610
Cdd:PRK11057 549 EENIPPYVVFNDATLIEMAEQMPITASEMLSVNGVGQRKLERFGKPFMALIRAHVDGDD 607
|
|
| recQ_fam |
TIGR00614 |
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are ... |
6-463 |
3.78e-156 |
|
ATP-dependent DNA helicase, RecQ family; All proteins in this family for which functions are known are 3'-5' DNA-DNA helicases. These proteins are used for recombination, recombinational repair, and possibly maintenance of chromosome stability. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129701 [Multi-domain] Cd Length: 470 Bit Score: 461.93 E-value: 3.78e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 6 VLKTYFGYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIMPGITIVISPLISLMQDQVKSLNDAGIHAGFI 85
Cdd:TIGR00614 2 ILKKYFGLSSFRPVQLEVINAVLLGRDCFVVMPTGGGKSLCYQLPALYSDGITLVISPLISLMEDQVLQLQALGIPATFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 86 NSSLTDRQIQLVYSRASEGAYIILYVAPERL-ESSDFIE-FASKTKISMVTVDEAHCISQWGQDFRPSY--LGIVNfiDR 161
Cdd:TIGR00614 82 NSAQTKEQQLNVLTDLKDGKIKLLYVTPEKIsASNRLLQtLEERKGITLIAVDEAHCISQWGHDFRPDYkaLGSLK--QK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 162 LPKRPVVsAFTATATMEVKEDISCILKLQDPKTVITGFDRENLYFDVEITKQK--DDYVLDYIKKHPDESGIIYCATRNS 239
Cdd:TIGR00614 160 FPNVPVM-ALTATASPSVREDILRQLNLLNPQIFCTSFDRPNLYYEVRRKTPKilEDLLRFIRKEFEGKSGIIYCPSRKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 240 VDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAG 319
Cdd:TIGR00614 239 VEQVAAELQKLGLAAGAYHAGLEDSARDDVQHKFQRDEIQVVVATVAFGMGINKPDVRFVIHYSLPKSMESYYQESGRAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 320 RDGESSRCILLFSPKDIIINKFLLEhkdftDIPSEDVILIKerdMRRLNVMEGYCKTTGCLRNYILEYFGEKNT------ 393
Cdd:TIGR00614 319 RDGLPSECHLFYAPADMNRLRRLLM-----EEPDGNFRTYK---LKLYEMMEYCLNSSTCRRLILLSYFGEKGFnksfci 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 394 ----EPCDNCGNCHKHFIEE------DRTEDAKKVINCVFETRGRYGLNIILGTLLGANRARLKELGIVNYRTYGTLKDR 463
Cdd:TIGR00614 391 mgteKCCDNCCKRLDYKTKDvtdkvyDFGPQAQKALSAVGRLNQKFGMGYPVDFLRGSNSQKIRDGGFRKHSLYGRGKDE 470
|
|
| PLN03137 |
PLN03137 |
ATP-dependent DNA helicase; Q4-like; Provisional |
8-628 |
1.36e-105 |
|
ATP-dependent DNA helicase; Q4-like; Provisional
Pssm-ID: 215597 [Multi-domain] Cd Length: 1195 Bit Score: 349.96 E-value: 1.36e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 8 KTYFGYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIMPGITIVISPLISLMQDQVKSLNDAGIHAGFINS 87
Cdd:PLN03137 453 KKVFGNHSFRPNQREIINATMSGYDVFVLMPTGGGKSLTYQLPALICPGITLVISPLVSLIQDQIMNLLQANIPAASLSA 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 88 SLT-DRQIQLVYSRASEGA-YIILYVAPERLESSDFI-----EFASKTKISMVTVDEAHCISQWGQDFRPSYLGIVNFID 160
Cdd:PLN03137 533 GMEwAEQLEILQELSSEYSkYKLLYVTPEKVAKSDSLlrhleNLNSRGLLARFVIDEAHCVSQWGHDFRPDYQGLGILKQ 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 161 RLPKRPVVsAFTATATMEVKEDISCILKLQDPKTVITGFDRENLYFDV-EITKQKDDYVLDYIKK-HPDESGIIYCATRN 238
Cdd:PLN03137 613 KFPNIPVL-ALTATATASVKEDVVQALGLVNCVVFRQSFNRPNLWYSVvPKTKKCLEDIDKFIKEnHFDECGIIYCLSRM 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 239 SVDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRA 318
Cdd:PLN03137 692 DCEKVAERLQEFGHKAAFYHGSMDPAQRAFVQKQWSKDEINIICATVAFGMGINKPDVRFVIHHSLPKSIEGYHQECGRA 771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 319 GRDGESSRCILLFSPKDIIINKFLLEHKDFTDIP---------SEDVILikERDMRRLNVMEGYCKT-TGCLRNYILEYF 388
Cdd:PLN03137 772 GRDGQRSSCVLYYSYSDYIRVKHMISQGGVEQSPmamgynrmaSSGRIL--ETNTENLLRMVSYCENeVDCRRFLQLVHF 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 389 GEK-NTEPCDN-CGNCH--KHFIEEDRTEDAKKVINCVFETRGRYGLNIILGTLLGANRARLKELGIVNYRTYGTLKDRS 464
Cdd:PLN03137 850 GEKfDSTNCKKtCDNCSssKSLIDKDVTEIARQLVELVKLTGERFSSAHILEVYRGSLNQYVKKHRHETLSLHGAGKHLS 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 465 EADLRILINQLILDGYLCQTADK------------------YSVIQLGDITPLKDPAT-RVIVRTTQAKEPDSNKVRQIK 525
Cdd:PLN03137 930 KGEASRILHYLVTEDILAEDVKKsdlygsvssllkvneskaYKLFSGGQTIIMRFPSSvKASKPSKFEATPAKGPLTSGK 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 526 KKTDSLTKAGY---------DLFDILKALRTQIARE--EGMPPYIVFSDKTLIDMSAKAPLDRAAMLNVSGVGEMKYDKY 594
Cdd:PLN03137 1010 QSTLPMATPAQppvdlnlsaILYTALRKLRTALVKEagDGVMAYHIFGNATLQQISKRIPRTKEELLEINGLGKAKVSKY 1089
|
650 660 670
....*....|....*....|....*....|....
gi 652962033 595 GQRFINAISSYLDEHEGvVTAITDSQNEAADNIK 628
Cdd:PLN03137 1090 GDRLLETIESTINEYYK-TDKNSSSSNDSPDSGK 1122
|
|
| DEXHc_RecQ |
cd17920 |
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ... |
4-200 |
2.65e-96 |
|
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.
Pssm-ID: 350678 [Multi-domain] Cd Length: 200 Bit Score: 297.14 E-value: 2.65e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 4 REVLKTYFGYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIMPGITIVISPLISLMQDQVKSLNDAGIHAG 83
Cdd:cd17920 1 EQILKEVFGYDEFRPGQLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALLLDGVTLVVSPLISLMQDQVDRLQQLGIRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 84 FINSSLTDRQIQLVYSRASEGAYIILYVAPERLESSDFIEFASK----TKISMVTVDEAHCISQWGQDFRPSYLGIVNFI 159
Cdd:cd17920 81 ALNSTLSPEEKREVLLRIKNGQYKLLYVTPERLLSPDFLELLQRlperKRLALIVVDEAHCVSQWGHDFRPDYLRLGRLR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 652962033 160 DRLPKRPVVsAFTATATMEVKEDISCILKLQDPKTVITGFD 200
Cdd:cd17920 161 RALPGVPIL-ALTATATPEVREDILKRLGLRNPVIFRASFD 200
|
|
| DEXHc_RecQ4-like |
cd18018 |
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ... |
5-191 |
1.96e-72 |
|
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.
Pssm-ID: 350776 [Multi-domain] Cd Length: 201 Bit Score: 234.46 E-value: 1.96e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 5 EVLKTYFGYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIM----PGITIVISPLISLMQDQVKSLNDAgI 80
Cdd:cd18018 2 KLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLrrrgPGLTLVVSPLIALMKDQVDALPRA-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 81 HAGFINSSLTDRQIQLVYSRASEGAYIILYVAPERLESSDFIEFASKTK-ISMVTVDEAHCISQWGQDFRPSYLGIVNFI 159
Cdd:cd18018 81 KAAALNSSLTREERRRILEKLRAGEVKILYVSPERLVNESFRELLRQTPpISLLVVDEAHCISEWSHNFRPDYLRLCRVL 160
|
170 180 190
....*....|....*....|....*....|..
gi 652962033 160 DRLPKRPVVSAFTATATMEVKEDISCILKLQD 191
Cdd:cd18018 161 RELLGAPPVLALTATATKRVVEDIASHLGIPE 192
|
|
| DEXHc_RecQ1 |
cd18015 |
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ... |
3-200 |
2.83e-55 |
|
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350773 [Multi-domain] Cd Length: 209 Bit Score: 188.73 E-value: 2.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 3 AREVLKTYFGYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIMPGITIVISPLISLMQDQVKSLNDAGIHA 82
Cdd:cd18015 6 VKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCSDGFTLVVSPLISLMEDQLMALKKLGISA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 83 GFINSSLTDRQIQLVYSRASEG--AYIILYVAPERLESSDfiEFASKT-------KISMVTVDEAHCISQWGQDFRPSY- 152
Cdd:cd18015 86 TMLNASSSKEHVKWVHAALTDKnsELKLLYVTPEKIAKSK--RFMSKLekaynagRLARIAIDEVHCCSQWGHDFRPDYk 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 652962033 153 -LGIvnFIDRLPKRPVVsAFTATATMEVKEDISCILKLQDPKTVITGFD 200
Cdd:cd18015 164 kLGI--LKRQFPNVPIL-GLTATATSKVLKDVQKILCIQKCLTFTASFN 209
|
|
| SF2_C_RecQ |
cd18794 |
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ... |
201-331 |
2.92e-55 |
|
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350181 [Multi-domain] Cd Length: 134 Bit Score: 185.88 E-value: 2.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 201 RENLYFDVEI---TKQKDDYVLDYIKKHPDESGIIYCATRNSVDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDR 277
Cdd:cd18794 1 RPNLFYSVRPkdkKDEKLDLLKRIKVEHLGGSGIIYCLSRKECEQVAARLQSKGISAAAYHAGLEPSDRRDVQRKWLRDK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 652962033 278 CPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAGRDGESSRCILLF 331
Cdd:cd18794 81 IQVIVATVAFGMGIDKPDVRFVIHYSLPKSMESYYQESGRAGRDGLPSECILFY 134
|
|
| DEXHc_RecQ3 |
cd18017 |
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ... |
7-200 |
8.91e-54 |
|
DEAH-box helicase domain of RecQ3; DEAD-like helicase RecQ3 (also called Werner syndrome ATP-dependent helicase or WRN) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Werner's syndrome.
Pssm-ID: 350775 [Multi-domain] Cd Length: 193 Bit Score: 184.21 E-value: 8.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 7 LKTYFGYDSFKKGQDEIIEAIL-SGRDVLSIMPTGAGKSICYQVPALIMPGITIVISPLISLMQDQVKSLNDAGIHAGFI 85
Cdd:cd18017 4 LNEYFGHSSFRPVQWKVIRSVLeERRDNLVVMATGYGKSLCYQYPSVLLNSLTLVISPLISLMEDQVLQLVMSNIPACFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 86 NSSltdrQIQLVYSRASEGAYIILYVAPERLESSDFIEFASKTKISMVTVDEAHCISQWGQDFRPSYLGIVNFIDRLPKR 165
Cdd:cd18017 84 GSA----QSQNVLDDIKMGKIRVIYVTPEFVSKGLELLQQLRNGITLIAIDEAHCVSQWGHDFRSSYRHLGSIRNRLPNV 159
|
170 180 190
....*....|....*....|....*....|....*
gi 652962033 166 PVVsAFTATATMEVKEDISCILKLQDPKTVITGFD 200
Cdd:cd18017 160 PIV-ALTATATPSVRDDIIKNLNLRNPQITCTSFD 193
|
|
| DEXHc_RecQ5 |
cd18014 |
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ... |
4-192 |
1.20e-50 |
|
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350772 [Multi-domain] Cd Length: 205 Bit Score: 175.74 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 4 REVLKTYFGYDSFKKG-QDEIIEAILSGR-DVLSIMPTGAGKSICYQVPALIMPGITIVISPLISLMQDQVKSLNDAGIH 81
Cdd:cd18014 1 RSTLKKVFGHSDFKSPlQEKATMAVVKGNkDVFVCMPTGAGKSLCYQLPALLAKGITIVISPLIALIQDQVDHLKTLKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 82 AGFINSSLT-DRQIQLVYSRASEGAYI-ILYVAPERLESSDFIE----FASKTKISMVTVDEAHCISQWGQDFRPSYLGI 155
Cdd:cd18014 81 VDSLNSKLSaQERKRIIADLESEKPQTkFLYITPEMAATSSFQPllssLVSRNLLSYLVVDEAHCVSQWGHDFRPDYLRL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 652962033 156 VNFIDRLPKRPVVsAFTATATMEVKEDISCILKLQDP 192
Cdd:cd18014 161 GALRSRYGHVPWV-ALTATATPQVQEDIFAQLRLKKP 196
|
|
| DEXHc_RecQ2_BLM |
cd18016 |
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ... |
5-200 |
6.46e-49 |
|
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.
Pssm-ID: 350774 [Multi-domain] Cd Length: 208 Bit Score: 171.16 E-value: 6.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 5 EVLKTYFGYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIMPGITIVISPLISLMQDQVKSLNDAGIHAGF 84
Cdd:cd18016 7 KIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 85 INSSLTDRQIQLVYSRASEGAYII--LYVAPERLESSD-----FIEFASKTKISMVTVDEAHCISQWGQDFRPSYLGIVN 157
Cdd:cd18016 87 LTGDKTDAEATKIYLQLSKKDPIIklLYVTPEKISASNrlistLENLYERKLLARFVIDEAHCVSQWGHDFRPDYKRLNM 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 652962033 158 FIDRLPKRPVVsAFTATATMEVKEDISCILKLQDPKTVITGFD 200
Cdd:cd18016 167 LRQKFPSVPMM-ALTATATPRVQKDILNQLKMLRPQVFTMSFN 208
|
|
| DpdF |
NF041063 |
protein DpdF; |
6-336 |
3.10e-40 |
|
protein DpdF;
Pssm-ID: 468990 [Multi-domain] Cd Length: 813 Bit Score: 158.92 E-value: 3.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 6 VLKTYFGYDSFK-KGQDEIIEAILS---GRDVLSIMPTGAGKSICYQVPALIMP---GITIVISPLISLMQDQ----VKS 74
Cdd:NF041063 130 FLAEALGFTHYRsPGQREAVRAALLappGSTLIVNLPTGSGKSLVAQAPALLASrqgGLTLVVVPTVALAIDQerraREL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 75 LNDAGIHAGFIN---SSLTDRQIQLVYSRASEGAYIILYVAPERLESSDF---IEFASKTKISMVTVDEAHCISQWGQDF 148
Cdd:NF041063 210 LRRAGPDLGGPLawhGGLSAEERAAIRQRIRDGTQRILFTSPESLTGSLRpalFDAAEAGLLRYLVVDEAHLVDQWGDGF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 149 RPSY--LG--IVNFIDRLPK--RPVVSAFTATATMEVKEDISCILKLQDPKTVITG-FDR-ENLYF--DVEITKQKDDYV 218
Cdd:NF041063 290 RPEFqlLAglRRSLLRLAPSgrPFRTLLLSATLTESTLDTLETLFGPPGPFIVVSAvQLRpEPAYWvaKCDSEEERRERV 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 219 LDYIKKHPDESgIIYCATRNSVDTLYELLSKEGVP-VARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVR 297
Cdd:NF041063 370 LEALRHLPRPL-ILYVTKVEDAEAWLQRLRAAGFRrVALFHGDTPDAERERLIEQWRENELDIVVATSAFGLGMDKSDVR 448
|
330 340 350
....*....|....*....|....*....|....*....
gi 652962033 298 FVIHYNMPQSMENYYQEAGRAGRDGESSRCILLFSPKDI 336
Cdd:NF041063 449 TVIHACVPETLDRFYQEVGRGGRDGKASLSLLIYTPDDL 487
|
|
| DEAD |
pfam00270 |
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ... |
20-181 |
4.38e-29 |
|
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
Pssm-ID: 425570 [Multi-domain] Cd Length: 165 Bit Score: 113.88 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIM------PGITIVISPLISLMQDQVKSLNDAGIHAGF-INSSLTDR 92
Cdd:pfam00270 4 QAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEAldkldnGPQALVLAPTRELAEQIYEELKKLGKGLGLkVASLLGGD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 93 QIQLVYSRASEgaYIILYVAPERLEssDFIEFASKTK-ISMVTVDEAHCISQWGqdFRPSYLGIvnfIDRLPKRPVVSAF 171
Cdd:pfam00270 84 SRKEQLEKLKG--PDILVGTPGRLL--DLLQERKLLKnLKLLVLDEAHRLLDMG--FGPDLEEI---LRRLPKKRQILLL 154
|
170
....*....|
gi 652962033 172 TATATMEVKE 181
Cdd:pfam00270 155 SATLPRNLED 164
|
|
| Helicase_C |
pfam00271 |
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ... |
213-322 |
1.30e-27 |
|
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
Pssm-ID: 459740 [Multi-domain] Cd Length: 109 Bit Score: 107.30 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 213 QKDDYVLDYIKKHPDESGIIYCATRNSVDTLYeLLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGID 292
Cdd:pfam00271 1 EKLEALLELLKKERGGKVLIFSQTKKTLEAEL-LLEKEGIKVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLD 79
|
90 100 110
....*....|....*....|....*....|
gi 652962033 293 KSNVRFVIHYNMPQSMENYYQEAGRAGRDG 322
Cdd:pfam00271 80 LPDVDLVINYDLPWNPASYIQRIGRAGRAG 109
|
|
| SrmB |
COG0513 |
Superfamily II DNA and RNA helicase [Replication, recombination and repair]; |
20-366 |
2.50e-25 |
|
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
Pssm-ID: 440279 [Multi-domain] Cd Length: 420 Bit Score: 109.47 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAILSGRDVLSIMPTGAGKSICYQVPAL--IMPGI-----TIVISP---LIslmqDQV-KSLNDAGIHAGFinSS 88
Cdd:COG0513 29 QAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLqrLDPSRprapqALILAPtreLA----LQVaEELRKLAKYLGL--RV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 89 LT-------DRQIQlvysRASEGAYIIlyVA-PERLEssDFIEfaSKT----KISMVTVDEAhcisqwgqD------FRP 150
Cdd:COG0513 103 ATvyggvsiGRQIR----ALKRGVDIV--VAtPGRLL--DLIE--RGAldlsGVETLVLDEA--------DrmldmgFIE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 151 SylgIVNFIDRLPKRPVVSAFTATATMEVKEdiscILK--LQDPKTVITgfDRENL--------YFDVEiTKQKDDYVLD 220
Cdd:COG0513 165 D---IERILKLLPKERQTLLFSATMPPEIRK----LAKryLKNPVRIEV--APENAtaetieqrYYLVD-KRDKLELLRR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 221 YIKKHPDESGIIYCATRNSVDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVI 300
Cdd:COG0513 235 LLRDEDPERAIVFCNTKRGADRLAEKLQKRGISAAALHGDLSQGQRERALDAFRNGKIRVLVATDVAARGIDIDDVSHVI 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 301 HYNMPQSMENYYQEAGRAGRDGESSRCILLFSPKDII----INKFLLEHKDFTDIPSEDVILIKERDMRR 366
Cdd:COG0513 315 NYDLPEDPEDYVHRIGRTGRAGAEGTAISLVTPDERRllraIEKLIGQKIEEEELPGFEPVEEKRLERLK 384
|
|
| HELICc |
smart00490 |
helicase superfamily c-terminal domain; |
241-322 |
3.25e-24 |
|
helicase superfamily c-terminal domain;
Pssm-ID: 197757 [Multi-domain] Cd Length: 82 Bit Score: 96.90 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 241 DTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAGR 320
Cdd:smart00490 1 EELAELLKELGIKVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGR 80
|
..
gi 652962033 321 DG 322
Cdd:smart00490 81 AG 82
|
|
| SF2_C_DEAD |
cd18787 |
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse ... |
202-331 |
4.82e-24 |
|
C-terminal helicase domain of the DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis, and RNA degradation. They are superfamily (SF)2 helicases that, similar to SF1, do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350174 [Multi-domain] Cd Length: 131 Bit Score: 97.96 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 202 ENLYFDVEITKQKDDYVLDYIKKHPDESGIIYCATRNSVDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVI 281
Cdd:cd18787 2 KQLYVVVEEEEKKLLLLLLLLEKLKPGKAIIFVNTKKRVDRLAELLEELGIKVAALHGDLSQEERERALKKFRSGKVRVL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 652962033 282 IATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAGRDGESSRCILLF 331
Cdd:cd18787 82 VATDVAARGLDIPGVDHVINYDLPRDAEDYVHRIGRTGRAGRKGTAITFV 131
|
|
| DEXDc |
smart00487 |
DEAD-like helicases superfamily; |
10-199 |
7.68e-23 |
|
DEAD-like helicases superfamily;
Pssm-ID: 214692 [Multi-domain] Cd Length: 201 Bit Score: 97.18 E-value: 7.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 10 YFGYDSFKKGQDEIIEAILSG-RDVLSIMPTGAGKSICYQVPALI-----MPGITIVISPLISLMQDQVKSLNDAGIHAG 83
Cdd:smart00487 3 KFGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEalkrgKGGRVLVLVPTRELAEQWAEELKKLGPSLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 84 FINSSLTDR-QIQLVYSRASEGAYIILYVAPERLESSDFIEFASKTKISMVTVDEAHCISQWGqdFRPSYLGIVNfidRL 162
Cdd:smart00487 83 LKVVGLYGGdSKREQLRKLESGKTDILVTTPGRLLDLLENDKLSLSNVDLVILDEAHRLLDGG--FGDQLEKLLK---LL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 652962033 163 PKRPVVSAFTATATMEVKEDISciLKLQDPKTVITGF 199
Cdd:smart00487 158 PKNVQLLLLSATPPEEIENLLE--LFLNDPVFIDVGF 192
|
|
| HRDC |
pfam00570 |
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic ... |
537-602 |
1.20e-21 |
|
HRDC domain; The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains.
Pssm-ID: 425755 [Multi-domain] Cd Length: 68 Bit Score: 89.13 E-value: 1.20e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 652962033 537 DLFDILKALRTQIAREEGMPPYIVFSDKTLIDMSAKAPLDRAAMLNVSGVGEMKYDKYGQRFINAI 602
Cdd:pfam00570 3 ALLKALREWRDELAREEDVPPYVIFPDKTLLEIAEKLPRTLEELLAIPGVGPRKVERYGEEILAAI 68
|
|
| RQC |
pfam09382 |
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a ... |
406-495 |
1.54e-19 |
|
RQC domain; This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure. The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 462780 [Multi-domain] Cd Length: 108 Bit Score: 84.51 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 406 FIEEDRTEDAKKVINCVFETRGRYGLNIILGTLLGANRARLKELGIVNYRTYGTLKDRSEADLRILINQLILDGYLCQTA 485
Cdd:pfam09382 2 PETVDVTEEAQKILSCVYRTGQRFGAGHLIDVLRGSKNKKIRQLGHDKLSTFGIGKDLSKKEWRRIIRQLIAEGYLEVDI 81
|
90
....*....|
gi 652962033 486 DKYSVIQLGD 495
Cdd:pfam09382 82 EFYSVLKLTP 91
|
|
| PLN00206 |
PLN00206 |
DEAD-box ATP-dependent RNA helicase; Provisional |
12-329 |
1.83e-19 |
|
DEAD-box ATP-dependent RNA helicase; Provisional
Pssm-ID: 215103 [Multi-domain] Cd Length: 518 Bit Score: 92.54 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 12 GYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVP-----ALIMPG--------ITIVISP---LISLMQDQVKSL 75
Cdd:PLN00206 140 GYEFPTPIQMQAIPAALSGRSLLVSADTGSGKTASFLVPiisrcCTIRSGhpseqrnpLAMVLTPtreLCVQVEDQAKVL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 76 ------NDAGIHAGfinssltDRQIQLVYsRASEGAYIILYvAPERLessdfIEFASK-----TKISMVTVDEAHCISQW 144
Cdd:PLN00206 220 gkglpfKTALVVGG-------DAMPQQLY-RIQQGVELIVG-TPGRL-----IDLLSKhdielDNVSVLVLDEVDCMLER 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 145 GqdFRPSYLGIVnfidRLPKRPVVSAFTATATMEVKEDISCILKlqDPKTVITGFDR------ENLYFDVEiTKQKDDYV 218
Cdd:PLN00206 286 G--FRDQVMQIF----QALSQPQVLLFSATVSPEVEKFASSLAK--DIILISIGNPNrpnkavKQLAIWVE-TKQKKQKL 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 219 LDYI--KKHPDESGIIYCATRNSVDTLYELLSK-EGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSN 295
Cdd:PLN00206 357 FDILksKQHFKPPAVVFVSSRLGADLLANAITVvTGLKALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLR 436
|
330 340 350
....*....|....*....|....*....|....
gi 652962033 296 VRFVIHYNMPQSMENYYQEAGRAGRDGESSRCIL 329
Cdd:PLN00206 437 VRQVIIFDMPNTIKEYIHQIGRASRMGEKGTAIV 470
|
|
| RQC |
smart00956 |
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix ... |
410-495 |
1.45e-18 |
|
This DNA-binding domain is found in the RecQ helicase among others and has a helix-turn-helix structure; The RQC domain, found only in RecQ family enzymes, is a high affinity G4 DNA binding domain.
Pssm-ID: 214936 [Multi-domain] Cd Length: 92 Bit Score: 80.98 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 410 DRTEDAKKVINCVFETRGRYGLNIILGTLLGANRARLKELGIVNYRTYGTLKDRSEADLRILINQLILDGYLCQTADKYS 489
Cdd:smart00956 1 DVTEEAQKLLSCVYRTGQRFGAGHVIDVLRGSKNKKIRQKGHDRLSTFGIGKDLSKKEWRRLIRQLIAEGYLREDGGRYP 80
|
....*.
gi 652962033 490 VIQLGD 495
Cdd:smart00956 81 YLKLTE 86
|
|
| RecQ_Zn_bind |
pfam16124 |
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ. |
333-402 |
9.69e-17 |
|
RecQ zinc-binding; This domain is the zinc-binding domain of ATP-dependent DNA helicase RecQ.
Pssm-ID: 465031 [Multi-domain] Cd Length: 66 Bit Score: 75.02 E-value: 9.69e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 652962033 333 PKDIIINKFLLEHKDFTDIpsedvilIKERDMRRLNVMEGYCKTTG-CLRNYILEYFGEK-NTEPCDNCGNC 402
Cdd:pfam16124 1 YQDVVRLRFLIEQSEADEE-------RKEVELQKLQAMVAYCENTTdCRRKQLLRYFGEEfDSEPCGNCDNC 65
|
|
| PTZ00110 |
PTZ00110 |
helicase; Provisional |
28-333 |
8.22e-16 |
|
helicase; Provisional
Pssm-ID: 240273 [Multi-domain] Cd Length: 545 Bit Score: 80.97 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 28 LSGRDVLSIMPTGAGKSICYQVPA--------LIMPG---ITIVISPLISLM----QDQVKSLNDAGIHAGFINSSLTDR 92
Cdd:PTZ00110 165 LSGRDMIGIAETGSGKTLAFLLPAivhinaqpLLRYGdgpIVLVLAPTRELAeqirEQCNKFGASSKIRNTVAYGGVPKR 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 93 QIQLVYSRASEgayiILYVAPERLesSDFIEfASKTKISMVT---VDEAHCISQWGqdFRPSYLGIVNFIDrlPKRPVVs 169
Cdd:PTZ00110 245 GQIYALRRGVE----ILIACPGRL--IDFLE-SNVTNLRRVTylvLDEADRMLDMG--FEPQIRKIVSQIR--PDRQTL- 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 170 AFTATATMEVKEDISCILKlQDPKTVITGfdrenlyfDVEIT-----KQKDDYVLDYIKK-----------HPDESGIIY 233
Cdd:PTZ00110 313 MWSATWPKEVQSLARDLCK-EEPVHVNVG--------SLDLTachniKQEVFVVEEHEKRgklkmllqrimRDGDKILIF 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 234 CATRNSVDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQ 313
Cdd:PTZ00110 384 VETKKGADFLTKELRLDGWPALCIHGDKKQEERTWVLNEFKTGKSPIMIATDVASRGLDVKDVKYVINFDFPNQIEDYVH 463
|
330 340
....*....|....*....|
gi 652962033 314 EAGRAGRDGESSRCILLFSP 333
Cdd:PTZ00110 464 RIGRTGRAGAKGASYTFLTP 483
|
|
| SSL2 |
COG1061 |
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair]; |
20-477 |
8.91e-15 |
|
Superfamily II DNA or RNA helicase [Transcription, Replication, recombination, and repair];
Pssm-ID: 440681 [Multi-domain] Cd Length: 566 Bit Score: 78.14 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAILS-----GRDVLSIMPTGAGKSIcyqVPALIM-----PGITIVISPLISLMqDQ-----VKSLNDAGIHAGF 84
Cdd:COG1061 85 QQEALEALLAalergGGRGLVVAPTGTGKTV---LALALAaellrGKRVLVLVPRRELL-EQwaeelRRFLGDPLAGGGK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 85 INSsltDRQIqLVYSRASegayiiLYVAPERLESSDFIefasktkiSMVTVDEAHCISqwgqdfRPSYLGIvnfIDRLPK 164
Cdd:COG1061 161 KDS---DAPI-TVATYQS------LARRAHLDELGDRF--------GLVIIDEAHHAG------APSYRRI---LEAFPA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 165 RPVVsAFTAT------ATMEVKEDISCI--LKLQD--------P---KTVITGFDRENLYFD----------VEITKQKD 215
Cdd:COG1061 214 AYRL-GLTATpfrsdgREILLFLFDGIVyeYSLKEaiedgylaPpeyYGIRVDLTDERAEYDalserlrealAADAERKD 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 216 DYVLDYIKKHPDES-GIIYCATRNSVDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKS 294
Cdd:COG1061 293 KILRELLREHPDDRkTLVFCSSVDHAEALAELLNEAGIRAAVVTGDTPKKEREEILEAFRDGELRILVTVDVLNEGVDVP 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 295 NVRFVIhYNMP-QSMENYYQEAGRAGRDGESSRCILLFspkDIIINKFLLEHKDFTDIPSEDVILIKERDmRRLNVMEGY 373
Cdd:COG1061 373 RLDVAI-LLRPtGSPREFIQRLGRGLRPAPGKEDALVY---DFVGNDVPVLEELAKDLRDLAGYRVEFLD-EEESEELAL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 374 CKTTGCLRNYILEYFGEKNTEPCDNCGNCHKHFIEEDRTEDAKKVINCVFETRGRYGLNIILGTLLGANRARLKELGIVN 453
Cdd:COG1061 448 LIAVKPALEVKGELEEELLEELELLEDALLLVLAELLLLELLALALELLELAKAEGKAEEEEEEKELLLLLALAKLLKLL 527
|
490 500
....*....|....*....|....
gi 652962033 454 YRTYGTLKDRSEADLRILINQLIL 477
Cdd:COG1061 528 LLLLLLLLLELLELLAALLRLEEL 551
|
|
| PTZ00424 |
PTZ00424 |
helicase 45; Provisional |
155-336 |
1.09e-14 |
|
helicase 45; Provisional
Pssm-ID: 185609 [Multi-domain] Cd Length: 401 Bit Score: 76.79 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 155 IVNFIDRLPKRPVVSAFTATATMEVKEDISCILKlqDPKTVITGFDRENL------YFDVEITKQKDDYVLDYIKKHPDE 228
Cdd:PTZ00424 191 IYDVFKKLPPDVQVALFSATMPNEILELTTKFMR--DPKRILVKKDELTLegirqfYVAVEKEEWKFDTLCDLYETLTIT 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 229 SGIIYCATRNSVDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSM 308
Cdd:PTZ00424 269 QAIIYCNTRRKVDYLTKKMHERDFTVSCMHGDMDQKDRDLIMREFRSGSTRVLITTDLLARGIDVQQVSLVINYDLPASP 348
|
170 180
....*....|....*....|....*...
gi 652962033 309 ENYYQEAGRAGRDGESSRCILLFSPKDI 336
Cdd:PTZ00424 349 ENYIHRIGRSGRFGRKGVAINFVTPDDI 376
|
|
| HRDC |
smart00341 |
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the ... |
542-608 |
1.35e-14 |
|
Helicase and RNase D C-terminal; Hypothetical role in nucleic acid binding. Mutations in the HRDC domain cause human disease.
Pssm-ID: 128635 [Multi-domain] Cd Length: 81 Bit Score: 69.25 E-value: 1.35e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 652962033 542 LKALRTQIAREEGMPPYIVFSDKTLIDMSAKAPLDRAAMLNVSGVGEMKYDKYGQRFINAISSYLDE 608
Cdd:smart00341 11 LRQWRDEIARREDVPPYFVLPDETLIKMAAALPTNVSELLAIDGVGEEKARRYGKDLLAVIQEASDS 77
|
|
| PRK11634 |
PRK11634 |
ATP-dependent RNA helicase DeaD; Provisional |
12-329 |
1.33e-13 |
|
ATP-dependent RNA helicase DeaD; Provisional
Pssm-ID: 236941 [Multi-domain] Cd Length: 629 Bit Score: 74.50 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 12 GYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPAL--IMPGI----TIVISPLISLMQDQVKSLNDAGIHAGFI 85
Cdd:PRK11634 25 GYEKPSPIQAECIPHLLNGRDVLGMAQTGSGKTAAFSLPLLhnLDPELkapqILVLAPTRELAVQVAEAMTDFSKHMRGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 86 NS-SLTDRQIQLVYSRASEGAYIILYVAPERLesSDFIEFASK--TKISMVTVDEAHCISQWG--QDfrpsylgIVNFID 160
Cdd:PRK11634 105 NVvALYGGQRYDVQLRALRQGPQIVVGTPGRL--LDHLKRGTLdlSKLSGLVLDEADEMLRMGfiED-------VETIMA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 161 RLPKRPVVSAFTATatmeVKEDISCILK--LQDPK------TVITGFDRENLYFDVEiTKQKDDYVLDYIKKHPDESGII 232
Cdd:PRK11634 176 QIPEGHQTALFSAT----MPEAIRRITRrfMKEPQevriqsSVTTRPDISQSYWTVW-GMRKNEALVRFLEAEDFDAAII 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 233 YCATRNSVDTLYELLSKEGVPVARYHAGMtNQSRKESQDDFIYD-RCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENY 311
Cdd:PRK11634 251 FVRTKNATLEVAEALERNGYNSAALNGDM-NQALREQTLERLKDgRLDILIATDVAARGLDVERISLVVNYDIPMDSESY 329
|
330
....*....|....*...
gi 652962033 312 YQEAGRAGRDGESSRCIL 329
Cdd:PRK11634 330 VHRIGRTGRAGRAGRALL 347
|
|
| SF2_C_Hrq |
cd18797 |
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ... |
231-330 |
5.64e-13 |
|
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350184 [Multi-domain] Cd Length: 146 Bit Score: 66.90 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 231 IIYCATRNSVDTLY----ELLSKEGVPVAR---YHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYN 303
Cdd:cd18797 39 IVFCRSRKLAELLLrylkARLVEEGPLASKvasYRAGYLAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAG 118
|
90 100
....*....|....*....|....*..
gi 652962033 304 MPQSMENYYQEAGRAGRDGESSRCILL 330
Cdd:cd18797 119 YPGSLASLWQQAGRAGRRGKDSLVILV 145
|
|
| YprA |
COG1205 |
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ... |
20-358 |
7.36e-13 |
|
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];
Pssm-ID: 440818 [Multi-domain] Cd Length: 758 Bit Score: 72.18 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAILSGRDVLSIMPTGAGKSICYQVPAL--IM--PGIT-IVISPLISLMQDQVKSLND------AGIHAGFIN-- 86
Cdd:COG1205 61 QAEAIEAARAGKNVVIATPTASGKSLAYLLPVLeaLLedPGATaLYLYPTKALARDQLRRLRElaealgLGVRVATYDgd 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 87 SSLTDRqiQLVYSRASegayIILyVAPERLESS------DFIEFASKTKIsmVTVDEAHcisqwgqdfrpSYLGI----V 156
Cdd:COG1205 141 TPPEER--RWIREHPD----IVL-TNPDMLHYGllphhtRWARFFRNLRY--VVIDEAH-----------TYRGVfgshV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 157 -NFIDRLpKR--------PVVSAftATATM----------------EVKEDISC-----ILkLQDPKTVITGFDRENLYF 206
Cdd:COG1205 201 aNVLRRL-RRicrhygsdPQFIL--ASATIgnpaehaerltgrpvtVVDEDGSPrgertFV-LWNPPLVDDGIRRSALAE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 207 DVEITKqkdDYVLDYIKkhpdesGIIYCATRNSVDTLYELLSKE------GVPVARYHAGMTNQSRKESQDDFIYDRCPV 280
Cdd:COG1205 277 AARLLA---DLVREGLR------TLVFTRSRRGAELLARYARRAlrepdlADRVAAYRAGYLPEERREIERGLRSGELLG 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 281 IIATNAFGMGIDKSNVRFVI--HYnmPQSMENYYQEAGRAGRDGESSRCILLFS--PKDiiinKFLLEH-KDFTDIPSED 355
Cdd:COG1205 348 VVSTNALELGIDIGGLDAVVlaGY--PGTRASFWQQAGRAGRRGQDSLVVLVAGddPLD----QYYVRHpEELFERPPEA 421
|
...
gi 652962033 356 VIL 358
Cdd:COG1205 422 AVI 424
|
|
| SF2-N |
cd00046 |
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ... |
30-176 |
5.80e-12 |
|
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.
Pssm-ID: 350668 [Multi-domain] Cd Length: 146 Bit Score: 63.96 E-value: 5.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 30 GRDVLSIMPTGAGKSICYQVPAL----IMPGITIVISPLISLMQDQ---VKSLNDAGIHAGFINSSLTDRQIqlvySRAS 102
Cdd:cd00046 1 GENVLITAPTGSGKTLAALLAALllllKKGKKVLVLVPTKALALQTaerLRELFGPGIRVAVLVGGSSAEER----EKNK 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 652962033 103 EGAYIILYVAPERLESSDFIEFASKTK-ISMVTVDEAHCISQWGQDFRPSYLGIVNFIdrlpkRPVVSAFTATAT 176
Cdd:cd00046 77 LGDADIIIATPDMLLNLLLREDRLFLKdLKLIIVDEAHALLIDSRGALILDLAVRKAG-----LKNAQVILLSAT 146
|
|
| DEXHc_Hrq1-like |
cd17923 |
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ... |
20-139 |
5.90e-10 |
|
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350681 [Multi-domain] Cd Length: 182 Bit Score: 59.14 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAILSGRDVLSIMPTGAGKSICYQVPAL--IM--PGIT-IVISPLISLMQDQVKSLND--AGIHAGFINSSLT-D 91
Cdd:cd17923 5 QAEAIEAARAGRSVVVTTGTASGKSLCYQLPILeaLLrdPGSRaLYLYPTKALAQDQLRSLREllEQLGLGIRVATYDgD 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 652962033 92 RQIQLVYSRASEGAYIILyVAPERLE------SSDFIEFASKTKisMVTVDEAH 139
Cdd:cd17923 85 TPREERRAIIRNPPRILL-TNPDMLHyallphHDRWARFLRNLR--YVVLDEAH 135
|
|
| PRK01297 |
PRK01297 |
ATP-dependent RNA helicase RhlB; Provisional |
20-335 |
1.54e-09 |
|
ATP-dependent RNA helicase RhlB; Provisional
Pssm-ID: 234938 [Multi-domain] Cd Length: 475 Bit Score: 61.08 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAILSGRDVLSIMPTGAGKSICY---------QVP-----------ALImpgitivISP----LISLMQDQVKSL 75
Cdd:PRK01297 114 QAQVLGYTLAGHDAIGRAQTGTGKTAAFlisiinqllQTPppkerymgeprALI-------IAPtrelVVQIAKDAAALT 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 76 NDAGIHA-GFINSSLTDRQIQLVYSRASEgayiILYVAPERLesSDFIEfASKTKISMVTV---DEAHCISQWGqdFRPS 151
Cdd:PRK01297 187 KYTGLNVmTFVGGMDFDKQLKQLEARFCD----ILVATPGRL--LDFNQ-RGEVHLDMVEVmvlDEADRMLDMG--FIPQ 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 152 YLGIVNFIDRLPKRPVVsAFTATATmevkEDISCILK--LQDPKTVitGFDRENLYFD-----VEITKQKDDYVLDY--I 222
Cdd:PRK01297 258 VRQIIRQTPRKEERQTL-LFSATFT----DDVMNLAKqwTTDPAIV--EIEPENVASDtveqhVYAVAGSDKYKLLYnlV 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 223 KKHPDESGIIYCATRNSVDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHY 302
Cdd:PRK01297 331 TQNPWERVMVFANRKDEVRRIEERLVKDGINAAQLSGDVPQHKRIKTLEGFREGKIRVLVATDVAGRGIHIDGISHVINF 410
|
330 340 350
....*....|....*....|....*....|...
gi 652962033 303 NMPQSMENYYQEAGRAGRDGESSRCILLFSPKD 335
Cdd:PRK01297 411 TLPEDPDDYVHRIGRTGRAGASGVSISFAGEDD 443
|
|
| BRR2 |
COG1204 |
Replicative superfamily II helicase [Replication, recombination and repair]; |
1-320 |
2.07e-09 |
|
Replicative superfamily II helicase [Replication, recombination and repair];
Pssm-ID: 440817 [Multi-domain] Cd Length: 529 Bit Score: 60.68 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 1 MDAREVLKTyFGYDSFKKGQDEIIEA-ILSGRDVLSIMPTGAGKS------ICYqvpALIMPGITIVISPLISL----MQ 69
Cdd:COG1204 9 EKVIEFLKE-RGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTliaelaILK---ALLNGGKALYIVPLRALasekYR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 70 DQVKSLNDAGIHAGfINSSLTDRQIQLVYSrasegaYIILYVAPERLES-----SDFIEfasktKISMVTVDEAHCIsqw 144
Cdd:COG1204 85 EFKRDFEELGIKVG-VSTGDYDSDDEWLGR------YDILVATPEKLDSllrngPSWLR-----DVDLVVVDEAHLI--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 145 GQDFR-PSY-LGIVNFIDRLPKRPVVSaftATATMEVKEDISCILklqDPKTVITG----------FDRENLYFDvEITK 212
Cdd:COG1204 150 DDESRgPTLeVLLARLRRLNPEAQIVA---LSATIGNAEEIAEWL---DAELVKSDwrpvplnegvLYDGVLRFD-DGSR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 213 QKDDYVLDYIKKHPDESG--IIYCATRNSV----------------------------------------DTLYELLSKE 250
Cdd:COG1204 223 RSKDPTLALALDLLEEGGqvLVFVSSRRDAeslakkladelkrrltpeereeleelaeellevseethtnEKLADCLEKG 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 652962033 251 gvpVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIdksN--VRFVI------HYNMPQSMENYYQEAGRAGR 320
Cdd:COG1204 303 ---VAFHHAGLPSELRRLVEDAFREGLIKVLVATPTLAAGV---NlpARRVIirdtkrGGMVPIPVLEFKQMAGRAGR 374
|
|
| SF2_C |
cd18785 |
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ... |
264-330 |
4.11e-09 |
|
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350172 [Multi-domain] Cd Length: 77 Bit Score: 53.86 E-value: 4.11e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 652962033 264 QSRKESQDdfIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAGRDG-ESSRCILL 330
Cdd:cd18785 11 NSIEHAEE--IASSLEILVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGkDEGEVILF 76
|
|
| SF2_C_dicer |
cd18802 |
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave ... |
219-330 |
8.87e-08 |
|
C-terminal helicase domain of the endoribonuclease Dicer; Dicer ribonucleases cleave double-stranded RNA (dsRNA) precursors to generate microRNAs (miRNAs) and small interfering RNAs (siRNAs). In concert with Argonautes, these small RNAs bind complementary mRNAs to down-regulate their expression. miRNAs are processed by Dicer from small hairpins, while siRNAs are typically processed from longer dsRNA, from endogenous sources, or exogenous sources such as viral replication intermediates. Some organisms, such as Homo sapiens and Caenorhabditis elegans, encode one Dicer that generates miRNAs and siRNAs, but other organisms have multiple dicers with specialized functions. Dicer exists throughout eukaryotes, and a subset has an N-terminal helicase domain of the RIG-I-like receptor (RLR) subgroup. RLRs often function in innate immunity and Dicer helicase domains sometimes show differences in activity that correlate with roles in immunity. Dicer helicase domains are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350189 [Multi-domain] Cd Length: 142 Bit Score: 51.82 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 219 LDYIKKHPDESGIIYCATRNSVDTLYELLSKEGVPVARYHAG---------------MTNQSRKESQDDFIYDRCPVIIA 283
Cdd:cd18802 17 REYFPKTPDFRGIIFVERRATAVVLSRLLKEHPSTLAFIRCGfligrgnssqrkrslMTQRKQKETLDKFRDGELNLLIA 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 652962033 284 TNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAGRDGesSRCILL 330
Cdd:cd18802 97 TSVLEEGIDVPACNLVIRFDLPKTLRSYIQSRGRARAPN--SKYILM 141
|
|
| SF2_C_Ski2 |
cd18795 |
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ... |
206-322 |
2.29e-07 |
|
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350182 [Multi-domain] Cd Length: 154 Bit Score: 51.01 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 206 FDVEITKQKDDYVLDYIKKHPDESG-IIYCATRNSVDTLYELLSKegvpVARYHAGMTNQSRKESQDDFIYDRCPVIIAT 284
Cdd:cd18795 21 VDVMNKFDSDIIVLLKIETVSEGKPvLVFCSSRKECEKTAKDLAG----IAFHHAGLTREDRELVEELFREGLIKVLVAT 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 652962033 285 NAFGMGID--------KSNVRFVIHYNMPQSMENYYQEAGRAGRDG 322
Cdd:cd18795 97 STLAAGVNlpartviiKGTQRYDGKGYRELSPLEYLQMIGRAGRPG 142
|
|
| DEADc |
cd00268 |
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ... |
20-195 |
3.82e-07 |
|
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350669 [Multi-domain] Cd Length: 196 Bit Score: 51.29 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAILSGRDVLSIMPTGAGKSICYQVPAL--IMPGITIVISPLISL---------MQ--DQVKSLNDA-GIHAG-F 84
Cdd:cd00268 17 QAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILekLLPEPKKKGRGPQALvlaptrelaMQiaEVARKLGKGtGLKVAaI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 85 INSSLTDRQIQlvysRASEGAYIIlyVA-PERLesSDFIE--FASKTKISMVTVDEAhcisqwgqD------FRPSylgI 155
Cdd:cd00268 97 YGGAPIKKQIE----ALKKGPDIV--VGtPGRL--LDLIErgKLDLSNVKYLVLDEA--------DrmldmgFEED---V 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 652962033 156 VNFIDRLPKRPVVSAFTATATMEVKEDISciLKLQDPKTV 195
Cdd:cd00268 158 EKILSALPKDRQTLLFSATLPEEVKELAK--KFLKNPVRI 195
|
|
| PRK10590 |
PRK10590 |
ATP-dependent RNA helicase RhlE; Provisional |
12-320 |
9.13e-07 |
|
ATP-dependent RNA helicase RhlE; Provisional
Pssm-ID: 236722 [Multi-domain] Cd Length: 456 Bit Score: 52.12 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 12 GYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIM------------PGITIVISPLISL-------MQDQV 72
Cdd:PRK10590 20 GYREPTPIQQQAIPAVLEGRDLMASAQTGTGKTAGFTLPLLQHlitrqphakgrrPVRALILTPTRELaaqigenVRDYS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 73 KSLNDAGIHAgFINSSLTDRQIQLvysrasEGAYIILYVAPERLESSDFIEFASKTKISMVTVDEAHcisqwgqdfRPSY 152
Cdd:PRK10590 100 KYLNIRSLVV-FGGVSINPQMMKL------RGGVDVLVATPGRLLDLEHQNAVKLDQVEILVLDEAD---------RMLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 153 LGIVNFIDR----LPKRPVVSAFTATATMEVKEDISCILklQDPKTVITGfdRENLYFDvEIT--------KQKDDYVLD 220
Cdd:PRK10590 164 MGFIHDIRRvlakLPAKRQNLLFSATFSDDIKALAEKLL--HNPLEIEVA--RRNTASE-QVTqhvhfvdkKRKRELLSQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 221 YIKKHPDESGIIYCATRNSVDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVI 300
Cdd:PRK10590 239 MIGKGNWQQVLVFTRTKHGANHLAEQLNKDGIRSAAIHGNKSQGARTRALADFKSGDIRVLVATDIAARGLDIEELPHVV 318
|
330 340
....*....|....*....|
gi 652962033 301 HYNMPQSMENYYQEAGRAGR 320
Cdd:PRK10590 319 NYELPNVPEDYVHRIGRTGR 338
|
|
| Rnd |
COG0349 |
Ribonuclease D [Translation, ribosomal structure and biogenesis]; |
541-602 |
7.65e-06 |
|
Ribonuclease D [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440118 [Multi-domain] Cd Length: 365 Bit Score: 48.71 E-value: 7.65e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 652962033 541 ILKAL---RTQIAREEGMPPYIVFSDKTLIDMSAKAPLDRAAMLNVSGVGEMKYDKYGQRFINAI 602
Cdd:COG0349 212 VLRELaawREREARKRDVPRNRVLKDEALLELARRQPKSLEELARLRGLSPGEIRRHGEELLAAV 276
|
|
| DEADc_DDX52 |
cd17957 |
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ... |
20-198 |
3.87e-05 |
|
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350715 [Multi-domain] Cd Length: 198 Bit Score: 45.27 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAILSGRDVLSIMPTGAGKSICYQVPALIM-------PGI-TIVISP---LISLMQDQVKSLNDA-GIHAGFINS 87
Cdd:cd17957 17 QMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKlgkprkkKGLrALILAPtreLASQIYRELLKLSKGtGLRIVLLSK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 88 SLTDRQiqlVYSRASEGAYIILYVAPERLesSDFIEFASKT--KISMVTVDEAHCIsqWGQDFRPSYLGIVNFIDRLPKR 165
Cdd:cd17957 97 SLEAKA---KDGPKSITKYDILVSTPLRL--VFLLKQGPIDlsSVEYLVLDEADKL--FEPGFREQTDEILAACTNPNLQ 169
|
170 180 190
....*....|....*....|....*....|...
gi 652962033 166 pvVSAFTATATMEVKEdiSCILKLQDPKTVITG 198
Cdd:cd17957 170 --RSLFSATIPSEVEE--LARSVMKDPIRIIVG 198
|
|
| SF2_C_SNF |
cd18793 |
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) ... |
216-322 |
5.33e-05 |
|
C-terminal helicase domain of the SNF family helicases; The Sucrose Non-Fermenting (SNF) family includes chromatin-remodeling factors, such as CHD proteins and SMARCA proteins, recombination proteins Rad54, and many others. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350180 [Multi-domain] Cd Length: 135 Bit Score: 43.62 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 216 DYVLDYIKKHPDESG--IIYCATRNSVDTLYELLSKEGVPVARYHAGMTNQSRKESQDDFIYD-RCPV-IIATNAFGMGI 291
Cdd:cd18793 14 EALLELLEELREPGEkvLIFSQFTDTLDILEEALRERGIKYLRLDGSTSSKERQKLVDRFNEDpDIRVfLLSTKAGGVGL 93
|
90 100 110
....*....|....*....|....*....|...
gi 652962033 292 DKSNVRFVIHYNMPQ--SMENyyQEAGRAGRDG 322
Cdd:cd18793 94 NLTAANRVILYDPWWnpAVEE--QAIDRAHRIG 124
|
|
| SF2_C_LHR |
cd18796 |
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ... |
191-331 |
7.65e-05 |
|
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350183 [Multi-domain] Cd Length: 150 Bit Score: 43.41 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 191 DPKTVITGFDRENLYfDVEITKQKDDYVLDYIKKHpdESGIIYCATRNSVDTLYELL------SKEGVPVARYHAGMTNQ 264
Cdd:cd18796 5 DIKVILPVAPEIFPW-AGESGADAYAEVIFLLERH--KSTLVFTNTRSQAERLAQRLrelcpdRVPPDFIALHHGSLSRE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 652962033 265 SRKESQDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAG-RDGESSRCILLF 331
Cdd:cd18796 82 LREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKSVARLLQRLGRSGhRPGAASKGRLVP 149
|
|
| DEADc_DDX5_DDX17 |
cd17966 |
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are ... |
28-180 |
9.92e-05 |
|
DEAD-box helicase domain of ATP-dependent RNA helicases DDX5 and DDX17; DDX5 and DDX17 are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350724 [Multi-domain] Cd Length: 197 Bit Score: 43.90 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 28 LSGRDVLSIMPTGAGKSICYQVPALI--------MPG---ITIVISPLISLMQdQVKSLNDAGIHAGFINSSltdrqiqL 96
Cdd:cd17966 25 LSGRDMVGIAQTGSGKTLAFLLPAIVhinaqpplERGdgpIVLVLAPTRELAQ-QIQQEANKFGGSSRLRNT-------C 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 97 VYSRASEGAYI--------ILYVAPERLesSDFIEfASKTKISMVT---VDEAHCISQWGqdFRPSYLGIVNFIDrlPKR 165
Cdd:cd17966 97 VYGGAPKGPQIrdlrrgveICIATPGRL--IDFLD-QGKTNLRRVTylvLDEADRMLDMG--FEPQIRKIVDQIR--PDR 169
|
170
....*....|....*
gi 652962033 166 PVVsAFTATATMEVK 180
Cdd:cd17966 170 QTL-MWSATWPKEVR 183
|
|
| DEADc_DDX10 |
cd17941 |
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin ... |
20-195 |
1.10e-04 |
|
DEAD-box helicase domain of DEAD box protein 10; Fusion of the DDX10 gene and the nucleoporin gene, NUP98, by inversion 11 (p15q22) chromosome translocation is found in the patients with de novo or therapy-related myeloid malignancies. Diseases associated with DDX10 (also known as DDX10-NUP98 Fusion Protein Type 2) include myelodysplastic syndrome and leukemia, acute myeloid. DDX10 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350699 [Multi-domain] Cd Length: 198 Bit Score: 43.82 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAILSGRDVLSIMPTGAGKSICYQVPAL---------IMPGI-TIVISPLISLMQDQVKSLNDAGIH----AGFI 85
Cdd:cd17941 17 QRDSIPHALQGRDILGAAKTGSGKTLAFLVPLLeklyrerwtPEDGLgALIISPTRELAMQIFEVLRKVGKYhsfsAGLI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 86 NSSLTDRQIQLVYSRASegayiILYVAPERL-----ESSDFiefaSKTKISMVTVDEAHCISQWGqdFRPSYLGIVNfid 160
Cdd:cd17941 97 IGGKDVKEEKERINRMN-----ILVCTPGRLlqhmdETPGF----DTSNLQMLVLDEADRILDMG--FKETLDAIVE--- 162
|
170 180 190
....*....|....*....|....*....|....*
gi 652962033 161 RLPKRPVVSAFTATATMEVKEdiSCILKLQDPKTV 195
Cdd:cd17941 163 NLPKSRQTLLFSATQTKSVKD--LARLSLKNPEYI 195
|
|
| DEADc_DDX17 |
cd18050 |
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or ... |
28-181 |
3.82e-04 |
|
DEAD-box helicase domain of DEAD box protein 17; DDX17 (also called DEAD Box Protein P72 or DEAD Box Protein P82) has a wide variety of functions including regulating the alternative splicing of exons exhibiting specific features such as the inclusion of AC-rich alternative exons in CD44 transcripts, playing a role in innate immunity, and promoting mRNA degradation mediated by the antiviral zinc-finger protein ZC3HAV1 in an ATPase-dependent manner. DDX17 synergizes with DDX5 and SRA1 RNA to activate MYOD1 transcriptional activity and is involved in skeletal muscle differentiation. DDX17 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350808 [Multi-domain] Cd Length: 271 Bit Score: 43.08 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 28 LSGRDVLSIMPTGAGKSICYQVPALIMPG-----------ITIVISPLISLMQdQVKSLNDAGIHAGFINSSltdrqiqL 96
Cdd:cd18050 97 LSGRDMVGIAQTGSGKTLAYLLPAIVHINhqpylergdgpICLVLAPTRELAQ-QVQQVADDYGKSSRLKST-------C 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 97 VYSRASEGAYI--------ILYVAPERLesSDFIEfASKTKISMVT---VDEAHCISQWGqdFRPSYLGIVNFIDrlPKR 165
Cdd:cd18050 169 IYGGAPKGPQIrdlergveICIATPGRL--IDFLE-AGKTNLRRCTylvLDEADRMLDMG--FEPQIRKIVDQIR--PDR 241
|
170
....*....|....*.
gi 652962033 166 PVVsAFTATATMEVKE 181
Cdd:cd18050 242 QTL-MWSATWPKEVRQ 256
|
|
| DEXHc_RE |
cd17926 |
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ... |
20-174 |
4.17e-04 |
|
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350684 [Multi-domain] Cd Length: 146 Bit Score: 41.14 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAIL----SGRDVLSiMPTGAGKSIC-YQVPALIMPGITIVISPLISLMQDQVKSLNDAGIHAgfinsslTDRQI 94
Cdd:cd17926 5 QEEALEAWLahknNRRGILV-LPTGSGKTLTaLALIAYLKELRTLIVVPTDALLDQWKERFEDFLGDS-------SIGLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 95 QLVYSRASEGAYIILYVaPERLESSDFIEFASKTKISMVTVDEAHCIS--QWGQdfrpsylgivnFIDRLPKRPVVsAFT 172
Cdd:cd17926 77 GGGKKKDFDDANVVVAT-YQSLSNLAEEEKDLFDQFGLLIVDEAHHLPakTFSE-----------ILKELNAKYRL-GLT 143
|
..
gi 652962033 173 AT 174
Cdd:cd17926 144 AT 145
|
|
| DEXHc_Ski2 |
cd17921 |
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ... |
20-143 |
9.89e-04 |
|
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350679 [Multi-domain] Cd Length: 181 Bit Score: 40.71 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 20 QDEIIEAI-LSGRDVLSIMPTGAGKSICYQ---VPALIMPGITIV-ISPLISLMQDQVKSLNDAGIHAGFINSSLTDrqi 94
Cdd:cd17921 6 QREALRALyLSGDSVLVSAPTSSGKTLIAElaiLRALATSGGKAVyIAPTRALVNQKEADLRERFGPLGKNVGLLTG--- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 652962033 95 QLVYSRASEGAYIILYVAPERLES------SDFIEfasktKISMVTVDEAHCISQ 143
Cdd:cd17921 83 DPSVNKLLLAEADILVATPEKLDLllrnggERLIQ-----DVRLVVVDEAHLIGD 132
|
|
| DEADc_DDX46 |
cd17953 |
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) ... |
11-52 |
2.77e-03 |
|
DEAD-box helicase domain of DEAD box protein 46; DDX46 (also called Prp5-like DEAD-box protein) is a component of the 17S U2 snRNP complex. It plays an important role in pre-mRNA splicing and has a role in antiviral innate immunity. DDX46 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.
Pssm-ID: 350711 [Multi-domain] Cd Length: 222 Bit Score: 40.05 E-value: 2.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 652962033 11 FGYDSFKKGQDEIIEAILSGRDVLSIMPTGAGKSICYQVPAL 52
Cdd:cd17953 30 LGYEKPTPIQAQALPAIMSGRDVIGIAKTGSGKTLAFLLPMF 71
|
|
| SF2_C_FANCM_Hef |
cd18801 |
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M ... |
207-331 |
3.56e-03 |
|
C-terminal helicase domain of Fanconi anemia group M family helicases; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. Hef (helicase-associated endonuclease fork-structure) belongs to the XPF/MUS81/FANCM family of endonucleases and is involved in stalled replication fork repair. FANCM and Hef are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.
Pssm-ID: 350188 [Multi-domain] Cd Length: 143 Bit Score: 38.49 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 652962033 207 DVEITKQKDDYVLDYIKKH-------PDESGIIYCATRNSVDTLYELLSKEGVPV----------ARYHAGMTNQSRKES 269
Cdd:cd18801 3 KVEKIHPKLEKLEEIVKEHfkkkqegSDTRVIIFSEFRDSAEEIVNFLSKIRPGIratrfigqasGKSSKGMSQKEQKEV 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 652962033 270 QDDFIYDRCPVIIATNAFGMGIDKSNVRFVIHYNMPQSMENYYQEAGRAGRdGESSRCILLF 331
Cdd:cd18801 83 IEQFRKGGYNVLVATSIGEEGLDIGEVDLIICYDASPSPIRMIQRMGRTGR-KRQGRVVVLL 143
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| DEXHc_LHR-like |
cd17922 |
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ... |
30-78 |
5.13e-03 |
|
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350680 [Multi-domain] Cd Length: 166 Bit Score: 38.33 E-value: 5.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 652962033 30 GRDVLSIMPTGAGK------SICYQVPALIMPGITIV-ISPLISLMQDQVKSLNDA 78
Cdd:cd17922 1 GRNVLIAAPTGSGKteaaflPALSSLADEPEKGVQVLyISPLKALINDQERRLEEP 56
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