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Conserved domains on  [gi|671871400|gb|AIJ00812|]
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truncated muramidase-released protein [Streptococcus suis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YSIRK_signal pfam04650
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and ...
 14-38 8.84e-08

YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.


:

Pssm-ID: 428049 [Multi-domain]  Cd Length: 26  Bit Score: 46.22  E-value: 8.84e-08
                          10        20
                  ....*....|....*....|....*
gi 671871400   14 TKQQFSIRKYHFGAASVLLGVSLVL 38
Cdd:pfam04650   2 KKQRYSIRKLSVGVASVLIGTLLFL 26
AlphaC_N super family cl07437
Alpha C protein N terminal; The alpha C protein (ACP) is found in Streptococcus and acts as an ...
 1-66 1.26e-05

Alpha C protein N terminal; The alpha C protein (ACP) is found in Streptococcus and acts as an invasin which plays a role in the internalization and translocation of the organizm across human epithelial surfaces. Group B Streptococcus is the leading cause of diseases including bacterial pneumonia, sepsis and meningitis. The N terminal of ACP is associated with virulence and forms a beta sandwich and a three helix bundle. ACP consists of an N-terminal domain (170 amino acids) followed by a variable number of tandem repeats (82 amino acids each) and a C-terminal domain (45 amino acids) containing an LPXTG peptidoglycan-anchoring motif. This entry is the N-terminal domain of ACP (NtACP). NtACP can be further divided into two structurally distinct domains, D1 and D2. D1, the more distal (amino-terminal) portion, consists of a beta sandwich with strong structural homology to fibronectin's integrin-binding region (FnIII10). D2 consists of three antiparallel alpha helix coils containing a portion of the glycosaminoglycan (GAG)-binding domain adjacent to the repeat region. NtACP binds to heparin and GAGs only when it is covalently associated with the adjacent repeat region. NtACP's D1 region contains a K144- T145-D146 (KTD) motif, located within a loop region that is structurally analogous to the loop containing the RGD integrin-binding motif in FnIII10. Single mutation within the KTD motif (D146A), present in the D1 domain, reduces NtACP binding to a1b integrion. The a1b1-integrin is one of four collagen-binding I-domain-containing integrins. Structural analysis of the D1 domain, in particular the region containing the putative integrin-binding loop and KTD motif, shares a strong structural homology with the FnIII10's integrin-binding region. Amino acid sequence alignment of Alps indicates that KTD is highly conserved.


The actual alignment was detected with superfamily member pfam08829:

Pssm-ID: 462613  Cd Length: 106  Bit Score: 42.42  E-value: 1.26e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 671871400    1 MRRSNKKSFDWYGTKQQFSIRKYHFGAASVLLGVSLVLG-------AGAQVVKADETVASSEPTIASSVAPAS 66
Cdd:pfam08829   2 FIRGKANSLDTLMTKNRFNGKAFIDGAASKLGGIDFLGGftlgqfdIKADTVFAAEGISFSAPSELTNMGAAS 74
PRK11907 super family cl36084
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
21-124 7.67e-04

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


The actual alignment was detected with superfamily member PRK11907:

Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 39.45  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671871400  21 RKYHFGAASVLLGVSLVLGAGAQVVKADETVASSE--PTIASSVAPASTEAVAEEAEKTNAENTSAVATTSTEVEKAKAV 98
Cdd:PRK11907   2 MKHYFSKSAVALTLALLTASNPKLAQAEEIVTTTPatSTEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETAETS 81

                         90       100
                 ....*....|....*....|....*.
gi 671871400  99 LEQVTSESPLLAGLGQKELAKTEDAT 124
Cdd:PRK11907  82 DPTSEATDTTTSEARTVTPAATETSK 107
 
Name Accession Description Interval E-value
YSIRK_signal pfam04650
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and ...
 14-38 8.84e-08

YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.


Pssm-ID: 428049 [Multi-domain]  Cd Length: 26  Bit Score: 46.22  E-value: 8.84e-08
                          10        20
                  ....*....|....*....|....*
gi 671871400   14 TKQQFSIRKYHFGAASVLLGVSLVL 38
Cdd:pfam04650   2 KKQRYSIRKLSVGVASVLIGTLLFL 26
AlphaC_N pfam08829
Alpha C protein N terminal; The alpha C protein (ACP) is found in Streptococcus and acts as an ...
 1-66 1.26e-05

Alpha C protein N terminal; The alpha C protein (ACP) is found in Streptococcus and acts as an invasin which plays a role in the internalization and translocation of the organizm across human epithelial surfaces. Group B Streptococcus is the leading cause of diseases including bacterial pneumonia, sepsis and meningitis. The N terminal of ACP is associated with virulence and forms a beta sandwich and a three helix bundle. ACP consists of an N-terminal domain (170 amino acids) followed by a variable number of tandem repeats (82 amino acids each) and a C-terminal domain (45 amino acids) containing an LPXTG peptidoglycan-anchoring motif. This entry is the N-terminal domain of ACP (NtACP). NtACP can be further divided into two structurally distinct domains, D1 and D2. D1, the more distal (amino-terminal) portion, consists of a beta sandwich with strong structural homology to fibronectin's integrin-binding region (FnIII10). D2 consists of three antiparallel alpha helix coils containing a portion of the glycosaminoglycan (GAG)-binding domain adjacent to the repeat region. NtACP binds to heparin and GAGs only when it is covalently associated with the adjacent repeat region. NtACP's D1 region contains a K144- T145-D146 (KTD) motif, located within a loop region that is structurally analogous to the loop containing the RGD integrin-binding motif in FnIII10. Single mutation within the KTD motif (D146A), present in the D1 domain, reduces NtACP binding to a1b integrion. The a1b1-integrin is one of four collagen-binding I-domain-containing integrins. Structural analysis of the D1 domain, in particular the region containing the putative integrin-binding loop and KTD motif, shares a strong structural homology with the FnIII10's integrin-binding region. Amino acid sequence alignment of Alps indicates that KTD is highly conserved.


Pssm-ID: 462613  Cd Length: 106  Bit Score: 42.42  E-value: 1.26e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 671871400    1 MRRSNKKSFDWYGTKQQFSIRKYHFGAASVLLGVSLVLG-------AGAQVVKADETVASSEPTIASSVAPAS 66
Cdd:pfam08829   2 FIRGKANSLDTLMTKNRFNGKAFIDGAASKLGGIDFLGGftlgqfdIKADTVFAAEGISFSAPSELTNMGAAS 74
YSIRK_signal TIGR01168
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, ...
 15-43 1.85e-04

Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.


Pssm-ID: 273479 [Multi-domain]  Cd Length: 39  Bit Score: 37.46  E-value: 1.85e-04
                          10        20
                  ....*....|....*....|....*....
gi 671871400   15 KQQFSIRKYHFGAASVLLGvSLVLGAGAQ 43
Cdd:TIGR01168   8 QQKYSIRKLSVGVASVLVA-SLFFGGGVA 35
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
21-124 7.67e-04

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 39.45  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671871400  21 RKYHFGAASVLLGVSLVLGAGAQVVKADETVASSE--PTIASSVAPASTEAVAEEAEKTNAENTSAVATTSTEVEKAKAV 98
Cdd:PRK11907   2 MKHYFSKSAVALTLALLTASNPKLAQAEEIVTTTPatSTEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETAETS 81

                         90       100
                 ....*....|....*....|....*.
gi 671871400  99 LEQVTSESPLLAGLGQKELAKTEDAT 124
Cdd:PRK11907  82 DPTSEATDTTTSEARTVTPAATETSK 107
 
Name Accession Description Interval E-value
YSIRK_signal pfam04650
YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and ...
 14-38 8.84e-08

YSIRK type signal peptide; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.


Pssm-ID: 428049 [Multi-domain]  Cd Length: 26  Bit Score: 46.22  E-value: 8.84e-08
                          10        20
                  ....*....|....*....|....*
gi 671871400   14 TKQQFSIRKYHFGAASVLLGVSLVL 38
Cdd:pfam04650   2 KKQRYSIRKLSVGVASVLIGTLLFL 26
AlphaC_N pfam08829
Alpha C protein N terminal; The alpha C protein (ACP) is found in Streptococcus and acts as an ...
 1-66 1.26e-05

Alpha C protein N terminal; The alpha C protein (ACP) is found in Streptococcus and acts as an invasin which plays a role in the internalization and translocation of the organizm across human epithelial surfaces. Group B Streptococcus is the leading cause of diseases including bacterial pneumonia, sepsis and meningitis. The N terminal of ACP is associated with virulence and forms a beta sandwich and a three helix bundle. ACP consists of an N-terminal domain (170 amino acids) followed by a variable number of tandem repeats (82 amino acids each) and a C-terminal domain (45 amino acids) containing an LPXTG peptidoglycan-anchoring motif. This entry is the N-terminal domain of ACP (NtACP). NtACP can be further divided into two structurally distinct domains, D1 and D2. D1, the more distal (amino-terminal) portion, consists of a beta sandwich with strong structural homology to fibronectin's integrin-binding region (FnIII10). D2 consists of three antiparallel alpha helix coils containing a portion of the glycosaminoglycan (GAG)-binding domain adjacent to the repeat region. NtACP binds to heparin and GAGs only when it is covalently associated with the adjacent repeat region. NtACP's D1 region contains a K144- T145-D146 (KTD) motif, located within a loop region that is structurally analogous to the loop containing the RGD integrin-binding motif in FnIII10. Single mutation within the KTD motif (D146A), present in the D1 domain, reduces NtACP binding to a1b integrion. The a1b1-integrin is one of four collagen-binding I-domain-containing integrins. Structural analysis of the D1 domain, in particular the region containing the putative integrin-binding loop and KTD motif, shares a strong structural homology with the FnIII10's integrin-binding region. Amino acid sequence alignment of Alps indicates that KTD is highly conserved.


Pssm-ID: 462613  Cd Length: 106  Bit Score: 42.42  E-value: 1.26e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 671871400    1 MRRSNKKSFDWYGTKQQFSIRKYHFGAASVLLGVSLVLG-------AGAQVVKADETVASSEPTIASSVAPAS 66
Cdd:pfam08829   2 FIRGKANSLDTLMTKNRFNGKAFIDGAASKLGGIDFLGGftlgqfdIKADTVFAAEGISFSAPSELTNMGAAS 74
YSIRK_signal TIGR01168
Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, ...
 15-43 1.85e-04

Gram-positive signal peptide, YSIRK family; Many surface proteins found in Streptococcus, Staphylococcus, and related lineages share apparently homologous signal sequences. A motif resembling [YF]SIRKxxxGxxS[VIA] appears at the start of the transmembrane domain. The GxxS motif appears perfectly conserved, suggesting a specific function and not just homology. There is a strong correlation between proteins carrying this region at the N-terminus and those carrying the Gram-positive anchor domain with the LPXTG sortase processing site at the C-terminus.


Pssm-ID: 273479 [Multi-domain]  Cd Length: 39  Bit Score: 37.46  E-value: 1.85e-04
                          10        20
                  ....*....|....*....|....*....
gi 671871400   15 KQQFSIRKYHFGAASVLLGvSLVLGAGAQ 43
Cdd:TIGR01168   8 QQKYSIRKLSVGVASVLVA-SLFFGGGVA 35
PRK11907 PRK11907
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
21-124 7.67e-04

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 237019 [Multi-domain]  Cd Length: 814  Bit Score: 39.45  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 671871400  21 RKYHFGAASVLLGVSLVLGAGAQVVKADETVASSE--PTIASSVAPASTEAVAEEAEKTNAENTSAVATTSTEVEKAKAV 98
Cdd:PRK11907   2 MKHYFSKSAVALTLALLTASNPKLAQAEEIVTTTPatSTEAEQTTPVESDATEEADNTETPVAATTAAEAPSSSETAETS 81

                         90       100
                 ....*....|....*....|....*.
gi 671871400  99 LEQVTSESPLLAGLGQKELAKTEDAT 124
Cdd:PRK11907  82 DPTSEATDTTTSEARTVTPAATETSK 107
 
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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