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Conserved domains on  [gi|194244926|gb|ACF35257|]
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bile salt hydrolase [Lactiplantibacillus plantarum]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
bile_salt_hydro super family cl41894
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-311 0e+00

choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables commensal or pathogenic bacteria in the digestive tract to escape the antimicrobial activity of bile acids, which are cholesterol derivatives conjugated to glycine or taurine.


The actual alignment was detected with superfamily member NF038245:

Pssm-ID: 468428  Cd Length: 314  Bit Score: 578.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   1 MCTAITYQSYNN-YFGRNFDYEISYNEMVTITPRKYPLVFRKVENLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLN 79
Cdd:NF038245   1 MCTALTYTTKDDhYFGRNLDLEFSYGEKVVITPRNYPFKFRKEADLKTHYAIIGMATVVDNYPLYFDAMNEKGLGMAGLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  80 FAGYADYKKYDA-DKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSPLHWLVADKQE-SIVIESVKEG 157
Cdd:NF038245  81 FPGNAYYAEEVEgGKDNVAPFEFIPWILGQCETVDEVKEALKNINLVNIPFSEQLPLSPLHWIIADKTGsSIVVESTKDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 158 LKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPM 237
Cdd:NF038245 161 LHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLELTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSPSG 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194244926 238 QTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYYYRTYDNSQINSVSLNHEHLDTTELIS 311
Cdd:NF038245 241 DSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDKGIYYYKTYENSQINAVDMHKEDLDGSELIS 314
 
Name Accession Description Interval E-value
bile_salt_hydro NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-311 0e+00

choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables commensal or pathogenic bacteria in the digestive tract to escape the antimicrobial activity of bile acids, which are cholesterol derivatives conjugated to glycine or taurine.


Pssm-ID: 468428  Cd Length: 314  Bit Score: 578.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   1 MCTAITYQSYNN-YFGRNFDYEISYNEMVTITPRKYPLVFRKVENLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLN 79
Cdd:NF038245   1 MCTALTYTTKDDhYFGRNLDLEFSYGEKVVITPRNYPFKFRKEADLKTHYAIIGMATVVDNYPLYFDAMNEKGLGMAGLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  80 FAGYADYKKYDA-DKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSPLHWLVADKQE-SIVIESVKEG 157
Cdd:NF038245  81 FPGNAYYAEEVEgGKDNVAPFEFIPWILGQCETVDEVKEALKNINLVNIPFSEQLPLSPLHWIIADKTGsSIVVESTKDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 158 LKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPM 237
Cdd:NF038245 161 LHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLELTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSPSG 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194244926 238 QTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYYYRTYDNSQINSVSLNHEHLDTTELIS 311
Cdd:NF038245 241 DSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDKGIYYYKTYENSQINAVDMHKEDLDGSELIS 314
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
2-299 4.36e-152

Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), catalyzes the hydrolysis of penicillin V to yield 6-amino penicillanic acid (6-APA), an important key intermediate of semisynthetic penicillins. PVA has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which PVA belongs. This nucleophilic cysteine is exposed by post-translational prossessing of the PVA precursor. PVA forms a homotetramer.


Pssm-ID: 238303  Cd Length: 303  Bit Score: 428.56  E-value: 4.36e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   2 CTAITYQSYNN--YFGRNFDYEISYNEMVTITPRKYPLVFRKV-ENLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGL 78
Cdd:cd00542    1 CTSLTLSTKDGdhVFGRTMDFAFDLGSQIIIIPRGYEWTSRSQgKSYTTKYAFIGMGAVGDDYPLLFDGVNEKGLAIAGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  79 NFAGYADYKKYDA-DKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSPLHWLVADKQ-ESIVIESVKE 156
Cdd:cd00542   81 YFPGYASYSKETKeGKTNIAPFEFITWVLGNFASVEEVKEALKNINVVDDPINLLGPVPPLHWIISDKSgRSIVVEPTKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 157 GLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLP 236
Cdd:cd00542  161 GLKVYDNPVGVLTNSPDFDWHLTNLRNYINLSPEPPKNVKLGGVNLTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194244926 237 MQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYYYRTYDNSQINSVSL 299
Cdd:cd00542  241 PKDEEEAVNNAFHILNSVDIPKGAVITENGSSDYTQYTSVMDLETGTYYYKTYDNNQIRAVDL 303
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
2-312 1.24e-149

Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and acid ceramidase EC:3.5.1.23. This domain forms the alpha-subunit for members from vertebral species, see family NAAA-beta, pfam15508.


Pssm-ID: 396726  Cd Length: 316  Bit Score: 423.08  E-value: 1.24e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926    2 CTAITY--QSYNNYFGRNFDYEISYNEMVTITPRKYPLVFRKVEN-LDHHYAIIGITADVESYPLYYDAMNEKGLCIAGL 78
Cdd:pfam02275   1 CTSITLetKKGNLLFGRNMDFGISYGEEVIITPRNYKLVFEKLGNmLVTKYAVIGMGTDVGSYPLFYDGLNEKGLGIAGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   79 NFAGYADYKKY-DADKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSPLHWLVADK-QESIVIESVKE 156
Cdd:pfam02275  81 YFPGYAFYSKGpKKDKVNIQPGELILWVLGNFTSVEEVKELLTKLNIVNEALDILGGKAPLHWIISDAsGESIVIEPRKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  157 GLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLP 236
Cdd:pfam02275 161 GLKVYDNEVGVMTNSPTFDWHLTNLNNYTGLRPNQPQNFFMGDLDLTPFGQGTGGLGLPGDFTPASRFVRAAYLKMNLPK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194244926  237 MQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYYYRTYDNSQINSVSLNHEHLDTTELISY 312
Cdd:pfam02275 241 AKTETESVATFFHILSNVAIPKGAVLNIEGKLEYTVYTSCMDLTKGNYYFETYDNSQINAVNLDHENLDCTELVTY 316
YxeI COG3049
Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope ...
1-320 7.77e-140

Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 442283  Cd Length: 337  Bit Score: 398.87  E-value: 7.77e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   1 MCTAITYQSYNN--YFGRNFDYEISYNEMVTITPRKYPLVFRKVEN---LDHHYAIIGITAdVESYPLYYDAMNEKGLCI 75
Cdd:COG3049    3 MCTRIVYKTKDGtvITGRTMDWGFDLGSNLVVFPRGYERDGEVGPNslkWTSKYGSVGMGA-YDGYPLTADGMNEKGLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  76 AGLNFAGYADYKKYD-ADKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSPLHWLVADKQ-ESIVIES 153
Cdd:COG3049   82 ALLYFPGYADYPKRDkEGKPNLAPSEFVQWVLDNFATVEEVKEALKKINFVNDPVPGLGRVAPLHLSISDATgDSAVIEY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 154 VKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLN 233
Cdd:COG3049  162 IDGKLVIHDNPVGVMTNSPTFDWQLANLRNYINLSPKQPEPVKLGGLTLTPFGQGSGTLGLPGDYTSPSRFVRAAFLKNA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 234 SLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYYYRTYDNSQINSVSLNHEHLD-TTELISY 312
Cdd:COG3049  242 LPKPADEEEAVASVFHILRNVSIPKGIVRPDEPNISYTQWTSVADLKNKTYYFETYDNPNIFWVDLKKLDFSkGAEVKKL 321

                 ....*...
gi 194244926 313 PLRSEAQY 320
Cdd:COG3049  322 DLDPNEQL 329
 
Name Accession Description Interval E-value
bile_salt_hydro NF038245
choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables ...
1-311 0e+00

choloylglycine hydrolase; Bile salt hydrolase, also known as choloylglycine hydrolase, enables commensal or pathogenic bacteria in the digestive tract to escape the antimicrobial activity of bile acids, which are cholesterol derivatives conjugated to glycine or taurine.


Pssm-ID: 468428  Cd Length: 314  Bit Score: 578.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   1 MCTAITYQSYNN-YFGRNFDYEISYNEMVTITPRKYPLVFRKVENLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLN 79
Cdd:NF038245   1 MCTALTYTTKDDhYFGRNLDLEFSYGEKVVITPRNYPFKFRKEADLKTHYAIIGMATVVDNYPLYFDAMNEKGLGMAGLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  80 FAGYADYKKYDA-DKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSPLHWLVADKQE-SIVIESVKEG 157
Cdd:NF038245  81 FPGNAYYAEEVEgGKDNVAPFEFIPWILGQCETVDEVKEALKNINLVNIPFSEQLPLSPLHWIIADKTGsSIVVESTKDG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 158 LKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLPM 237
Cdd:NF038245 161 LHVYDNPVGVLTNNPTFDWQLFNLNNYMNLSPKQPENTFWGDLELTPYSRGMGGIGLPGDLSSPSRFVRAAFTKANSPSG 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194244926 238 QTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYYYRTYDNSQINSVSLNHEHLDTTELIS 311
Cdd:NF038245 241 DSEEENVSQFFHILGSVEQQKGCCEVGNGKYEYTIYSSCMNLDKGIYYYKTYENSQINAVDMHKEDLDGSELIS 314
Ntn_PVA cd00542
Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), ...
2-299 4.36e-152

Penicillin V acylase (PVA), also known as conjugated bile salt acid hydrolase (CBAH), catalyzes the hydrolysis of penicillin V to yield 6-amino penicillanic acid (6-APA), an important key intermediate of semisynthetic penicillins. PVA has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which PVA belongs. This nucleophilic cysteine is exposed by post-translational prossessing of the PVA precursor. PVA forms a homotetramer.


Pssm-ID: 238303  Cd Length: 303  Bit Score: 428.56  E-value: 4.36e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   2 CTAITYQSYNN--YFGRNFDYEISYNEMVTITPRKYPLVFRKV-ENLDHHYAIIGITADVESYPLYYDAMNEKGLCIAGL 78
Cdd:cd00542    1 CTSLTLSTKDGdhVFGRTMDFAFDLGSQIIIIPRGYEWTSRSQgKSYTTKYAFIGMGAVGDDYPLLFDGVNEKGLAIAGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  79 NFAGYADYKKYDA-DKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSPLHWLVADKQ-ESIVIESVKE 156
Cdd:cd00542   81 YFPGYASYSKETKeGKTNIAPFEFITWVLGNFASVEEVKEALKNINVVDDPINLLGPVPPLHWIISDKSgRSIVVEPTKG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 157 GLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLP 236
Cdd:cd00542  161 GLKVYDNPVGVLTNSPDFDWHLTNLRNYINLSPEPPKNVKLGGVNLTAFGQGSGTLGLPGDYTPPSRFVRAAYLKNYAPQ 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194244926 237 MQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYYYRTYDNSQINSVSL 299
Cdd:cd00542  241 PKDEEEAVNNAFHILNSVDIPKGAVITENGSSDYTQYTSVMDLETGTYYYKTYDNNQIRAVDL 303
CBAH pfam02275
Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several ...
2-312 1.24e-149

Linear amide C-N hydrolases, choloylglycine hydrolase family; This family includes several hydrolases which cleave carbon-nitrogen bonds, other than peptide bonds, in linear amides. These include choloylglycine hydrolase (conjugated bile acid hydrolase, CBAH) EC:3.5.1.24, penicillin acylase EC:3.5.1.11 and acid ceramidase EC:3.5.1.23. This domain forms the alpha-subunit for members from vertebral species, see family NAAA-beta, pfam15508.


Pssm-ID: 396726  Cd Length: 316  Bit Score: 423.08  E-value: 1.24e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926    2 CTAITY--QSYNNYFGRNFDYEISYNEMVTITPRKYPLVFRKVEN-LDHHYAIIGITADVESYPLYYDAMNEKGLCIAGL 78
Cdd:pfam02275   1 CTSITLetKKGNLLFGRNMDFGISYGEEVIITPRNYKLVFEKLGNmLVTKYAVIGMGTDVGSYPLFYDGLNEKGLGIAGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   79 NFAGYADYKKY-DADKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSPLHWLVADK-QESIVIESVKE 156
Cdd:pfam02275  81 YFPGYAFYSKGpKKDKVNIQPGELILWVLGNFTSVEEVKELLTKLNIVNEALDILGGKAPLHWIISDAsGESIVIEPRKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  157 GLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLNSLP 236
Cdd:pfam02275 161 GLKVYDNEVGVMTNSPTFDWHLTNLNNYTGLRPNQPQNFFMGDLDLTPFGQGTGGLGLPGDFTPASRFVRAAYLKMNLPK 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194244926  237 MQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYYYRTYDNSQINSVSLNHEHLDTTELISY 312
Cdd:pfam02275 241 AKTETESVATFFHILSNVAIPKGAVLNIEGKLEYTVYTSCMDLTKGNYYFETYDNSQINAVNLDHENLDCTELVTY 316
YxeI COG3049
Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope ...
1-320 7.77e-140

Penicillin V acylase or related amidase, Ntn superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 442283  Cd Length: 337  Bit Score: 398.87  E-value: 7.77e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   1 MCTAITYQSYNN--YFGRNFDYEISYNEMVTITPRKYPLVFRKVEN---LDHHYAIIGITAdVESYPLYYDAMNEKGLCI 75
Cdd:COG3049    3 MCTRIVYKTKDGtvITGRTMDWGFDLGSNLVVFPRGYERDGEVGPNslkWTSKYGSVGMGA-YDGYPLTADGMNEKGLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  76 AGLNFAGYADYKKYD-ADKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSPLHWLVADKQ-ESIVIES 153
Cdd:COG3049   82 ALLYFPGYADYPKRDkEGKPNLAPSEFVQWVLDNFATVEEVKEALKKINFVNDPVPGLGRVAPLHLSISDATgDSAVIEY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 154 VKEGLKIYDNPVGVLTNNPNFDYQLFNLNNYRALSNSTPQNSFSEKVDLDSYSRGMGGLGLPGDLSSMSRFVRAAFTKLN 233
Cdd:COG3049  162 IDGKLVIHDNPVGVMTNSPTFDWQLANLRNYINLSPKQPEPVKLGGLTLTPFGQGSGTLGLPGDYTSPSRFVRAAFLKNA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 234 SLPMQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYYYRTYDNSQINSVSLNHEHLD-TTELISY 312
Cdd:COG3049  242 LPKPADEEEAVASVFHILRNVSIPKGIVRPDEPNISYTQWTSVADLKNKTYYFETYDNPNIFWVDLKKLDFSkGAEVKKL 321

                 ....*...
gi 194244926 313 PLRSEAQY 320
Cdd:COG3049  322 DLDPNEQL 329
Ntn_CGH_like cd01935
Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins ...
2-264 4.54e-64

Choloylglycine hydrolase (CGH)_like. This family of choloylglycine hydrolase-like proteins includes conjugated bile acid hydrolase (CBAH), penicillin V acylase (PVA), acid ceramidase (AC), and N-acylethanolamine-hydrolyzing acid amidase (NAAA) which cleave non-peptide carbon-nitrogen bonds in bile salt constituents. These enzymes have an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which they belong. This nucleophilic cysteine is exposed by post-translational prossessing of the precursor protein.


Pssm-ID: 238910  Cd Length: 229  Bit Score: 202.20  E-value: 4.54e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   2 CTAITYQSYNN--YFGRNFDYEISYNEMVTITPRKYPLVFRKVENlDHHYAIIGITADVESYPLYYDAMNEKGLCIAGLN 79
Cdd:cd01935    1 CTSIVAQTKDGgvYLGRNMDFSFDYELRLLVFPRGYQRNGQTGDK-SKWYAKYGSGGTSAGYIGLVDGMNEKGLSVSLLY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  80 FAGYADYKKY-DADKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSPLHWLVADKQ-ESIVIESVKEG 157
Cdd:cd01935   80 FPGYAYYPAGiKEGKDGLPAFELIRWVLENCDSVEEVKEALKKIPIVDFPIPLGGPAAPLHYILSDKSgDSAVIEPIDGG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 158 LKIYDNP-VGVLTNNPNFDYQLfnlnnyralsnstpqnsfsekvdldsysrgmgglglpgdlssMSRFVRAAFTKLNSLP 236
Cdd:cd01935  160 LKIYDNPwFGVMTNHPTFDWHL------------------------------------------PRRFVRVAYLKNTAQK 197
                        250       260
                 ....*....|....*....|....*...
gi 194244926 237 MQTESGSVSQFFHILGSVEQQKGLCEVT 264
Cdd:cd01935  198 NKETVEDVKNLFHILESVPIPNGLTVYT 225
Ntn_CGH cd01902
Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide ...
1-309 2.50e-19

Choloylglycine hydrolase (CGH) is a bile salt-modifying enzyme that hydrolyzes non-peptide carbon-nitrogen bonds in choloylglycine and choloyltaurine, both of which are present in bile. CGH is present in a number of probiotic microbial organisms that inhabit the gut. CGH has an N-terminal nucleophilic cysteine, as do other members of the Ntn hydrolase family to which CGH belongs.


Pssm-ID: 238885  Cd Length: 291  Bit Score: 86.24  E-value: 2.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   1 MCTAITYQSYNNYF--GRNFDYEISYNEMVTITPR---KYPLVFRKVENLDHHYAIIGITAdvesyplYY----DAMNEK 71
Cdd:cd01902    1 ACTRILWNTNNQGVitGRSMDWKEDTGPNLWVFPRgmeRDGGTGDNSAKWTSKYGSVVASM-------YDigtvDGMNEK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  72 GLcIAGLNFAGYADYKKYDADKVNITPFELIPWLLGQFSSVREVKKNIQKLNLVNINFSEQLPLSP-LHWLVADKQ-ESI 149
Cdd:cd01902   74 GL-VANLLYLTESDYGPADPNKPTLSAGAWGQYLLDNYATVEEAVKALAKEPFVIVASVPGDGREAtLHLSISDATgDSA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 150 VIESVKEGLKIYDNP-VGVLTNNPNFDYQLFNLNNYRALSNSTpqnsfsekvdldsysrgmGGLGLPGDLSSMSRFVRAA 228
Cdd:cd01902  153 IIEYIDGKLVIHHGKqYQVMTNSPTYDQQLALNKYWKQEKDIG------------------GTTGLPGNNNPADRFVRAS 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926 229 FTkLNSLP-MQTESGSVSQFFHILGSVEQQKGLCEVTDGKYEYTIYSSCCDMDKGVYYYrtydnsqINSVSLNHEHLDTT 307
Cdd:cd01902  215 YY-ISALPkTADEREAVASVLSVIRNVSVPFGIPTPAPPNISDTRWRTVADHKMKRYFF-------ESTLTPNLFWVDLK 286

                 ..
gi 194244926 308 EL 309
Cdd:cd01902  287 KL 288
COG4927 COG4927
Predicted choloylglycine hydrolase [General function prediction only];
2-170 4.91e-06

Predicted choloylglycine hydrolase [General function prediction only];


Pssm-ID: 443955 [Multi-domain]  Cd Length: 242  Bit Score: 46.87  E-value: 4.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   2 CTAITYQSYNN-YFGRNFDYeisynemvtiTPRKYPLVFRKVENLDHHYAIIGITAdveSYPLYYDAMNEKGLCIaGLNF 80
Cdd:COG4927   88 CSQFAVAPEGEpLLARNYDF----------HPDLYEGRLLLTVQPDGGYAFIGVTD---GLIGRLDGMNEKGLAV-GLNF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926  81 AGYADYKkydaDKVNItPFeLIPWLLGQFSSVREVkkniqklnlvnINFSEQLPL-SPLHWLVADKQESI-VIESVKEGL 158
Cdd:COG4927  154 VGRKVAG----PGFPI-PL-LIRYILETCSTVDEA-----------IALLKEIPHaSSYNLTLADASGNAaVVEVSPRGV 216
                        170
                 ....*....|...
gi 194244926 159 KIYD-NPVGVLTN 170
Cdd:COG4927  217 EVREpNGFLVCTN 229
AAT pfam03417
Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;
13-122 3.94e-03

Acyl-coenzyme A:6-aminopenicillanic acid acyl-transferase;


Pssm-ID: 397472  Cd Length: 223  Bit Score: 38.08  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194244926   13 YFGRNFDYeisynemvtiTPRKYPLVFRKVENLDHHYAIIGITAdveSYPLYYDAMNEKGLcIAGLNFAGyadYKKYDAD 92
Cdd:pfam03417   8 LLGRNEDY----------DPETYSHRYLLTAPEDPGFATIGYAG---RLPGRTDGINEKGL-AMGINFVH---LRKLRGD 70
                          90       100       110
                  ....*....|....*....|....*....|
gi 194244926   93 KVNItpFELIPWLLGQFSSVREVKKNIQKL 122
Cdd:pfam03417  71 GFPR--HFITRLLLETCSSVEEAVKLLKEI 98
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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