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Conserved domains on  [gi|2310739773|ref|WP_261710240|]
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Spy0128 family protein, partial [Streptococcus sp. HMSC074F05]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AgI_II_C2 pfam17998
Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the ...
486-635 6.13e-31

Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the C-terminal region found in antigen I/II type adhesin protein AspA from S. pyogenes. Together with C3, these two domains form an elongated structure, each domain adopts the DEv-IgG fold. Similar to the classical IgG folds, it is comprised of two major antiparallel beta-sheets, designated ABED and CFG. For the C2-domain, there are two additional strands on the CFG sheet. Furthermore, sheets ABED and CFG are interconnected by several cross-connecting loops and one alpha-helix (DH1). The side chains of D982 and N996 in the C2-domain are involved in hydrogen bonding with the side chains of R1264 and N1295 in the C3 domain. Main chain hydrogen bonding can also be observed between S992 in C2 and N1189/G1191 in C3, furthermore stabilizing the interaction between the domains. The C2 domain contains one bound metal ion, modeled as Ca2+, and both the C2- and C3-domains are stabilized by conserved isopeptide bonds, which connect the beta-sheets of the central DEv-IgG motifs.Other members of this family include Major cell-surface adhesin PAc from Streptococcus mutans and SspB from Streptococcus gordonii.


:

Pssm-ID: 465609 [Multi-domain]  Cd Length: 180  Bit Score: 119.88  E-value: 6.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 486 VDKTTNNEPENLNTKTVKRGSKLVYQVWLDTTKFTEANNI----QYVGVSDTYDAEKLDVNAADIKAYDSVTGAEVTNKF 561
Cdd:pfam17998   2 TKTVTNENGVSIDGKTVLRGDTLYYRVTLDLTQYKGIAAYdvirKGFGIVDDYDEEYLTVDAATIKVIDDATGKDVTGKF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 562 DIKVENGTITATSK--------DEFIK-----------------DKVNAPVIDTTKFEFGRYYKFDIPATVKESVKAGAD 616
Cdd:pfam17998  82 NIQVRDGVVYAFAKtvdslvpaTGEVQgdpqpadlkpygafqvfDALDPPAFDQTYLQKGQTYTLVLPMTVKKDVDGGGT 161
                         170
                  ....*....|....*....
gi 2310739773 617 IENTANQTVHVYNPVSKTV 635
Cdd:pfam17998 162 IENTAYQVDFGNGYVTNTV 180
AgI_II_C2 pfam17998
Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the ...
813-899 2.26e-18

Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the C-terminal region found in antigen I/II type adhesin protein AspA from S. pyogenes. Together with C3, these two domains form an elongated structure, each domain adopts the DEv-IgG fold. Similar to the classical IgG folds, it is comprised of two major antiparallel beta-sheets, designated ABED and CFG. For the C2-domain, there are two additional strands on the CFG sheet. Furthermore, sheets ABED and CFG are interconnected by several cross-connecting loops and one alpha-helix (DH1). The side chains of D982 and N996 in the C2-domain are involved in hydrogen bonding with the side chains of R1264 and N1295 in the C3 domain. Main chain hydrogen bonding can also be observed between S992 in C2 and N1189/G1191 in C3, furthermore stabilizing the interaction between the domains. The C2 domain contains one bound metal ion, modeled as Ca2+, and both the C2- and C3-domains are stabilized by conserved isopeptide bonds, which connect the beta-sheets of the central DEv-IgG motifs.Other members of this family include Major cell-surface adhesin PAc from Streptococcus mutans and SspB from Streptococcus gordonii.


:

Pssm-ID: 465609 [Multi-domain]  Cd Length: 180  Bit Score: 83.67  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 813 NNEAENLNTKTVERGSKLVYQVWLDTTKFDAANKDNIQ--TVGISDNYDEAKLNLNAADIKAYDSVTGAEVTDKFDIAVN 890
Cdd:pfam17998   7 NENGVSIDGKTVLRGDTLYYRVTLDLTQYKGIAAYDVIrkGFGIVDDYDEEYLTVDAATIKVIDDATGKDVTGKFNIQVR 86

                  ....*....
gi 2310739773 891 NGVITATLK 899
Cdd:pfam17998  87 DGVVYAFAK 95
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
207-308 5.74e-18

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


:

Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 80.14  E-value: 5.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 207 FKFTKKLEGKELTKDAFTFEL-LENGNVIQTKKNAADGSITFDAIEYNAVGEHTYTVREKAGNDINIDYDTMNAEVKVKV 285
Cdd:pfam12892   1 LKATKTLTGRDLKDGEFTFTLtDEDGNVIQTAKNDADGTVTFGDITYTKAGTYTYTVTEVNGGVPGVTYDTHTYTVTVTV 80
                          90       100
                  ....*....|....*....|....*
gi 2310739773 286 TkDAATGLLSTAVTMPEDTE--FNN 308
Cdd:pfam12892  81 T-DNGDGTLTATVTYDDGTEltFTN 104
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
321-420 2.89e-15

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


:

Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 72.43  E-value: 2.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 321 TKKLAGRELKDGEFKFILKDANGREVETVTNKADGTVTFSELSFDntKVGTHTYTVEEVIPANKefGMTYDQMKATVTVE 400
Cdd:pfam12892   4 TKTLTGRDLKDGEFTFTLTDEDGNVIQTAKNDADGTVTFGDITYT--KAGTYTYTVTEVNGGVP--GVTYDTHTYTVTVT 79
                          90       100
                  ....*....|....*....|
gi 2310739773 401 VAKNGHSLTTVTNVTSTGGK 420
Cdd:pfam12892  80 VTDNGDGTLTATVTYDDGTE 99
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
95-199 8.10e-15

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


:

Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 71.28  E-value: 8.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  95 SKALAGRELKEGEFSFVLKDSNGKTLQTKTNTKQGVVAFDDLTFDntQVGTHKYTVEEVIPEnkETGMTYDPMKAEVTIT 174
Cdd:pfam12892   4 TKTLTGRDLKDGEFTFTLTDEDGNVIQTAKNDADGTVTFGDITYT--KAGTYTYTVTEVNGG--VPGVTYDTHTYTVTVT 79
                          90       100
                  ....*....|....*....|....*...
gi 2310739773 175 VTKEGH-VLKATNTLPADTE--FNNTFT 199
Cdd:pfam12892  80 VTDNGDgTLTATVTYDDGTEltFTNTYK 107
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
656-760 1.20e-11

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


:

Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 62.03  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 656 NFTKRLEGRELQAKEFEFVLK-KDGVEVERVKNDAAGKIVFKTLEFGRDdlgKTYNYTVEETPGTDATVKYDTMVATVKV 734
Cdd:pfam12892   2 KATKTLTGRDLKDGEFTFTLTdEDGNVIQTAKNDADGTVTFGDITYTKA---GTYTYTVTEVNGGVPGVTYDTHTYTVTV 78
                          90       100
                  ....*....|....*....|....*..
gi 2310739773 735 VVSHDGTAK-AIVANVTDAADKEFNNR 760
Cdd:pfam12892  79 TVTDNGDGTlTATVTYDDGTELTFTNT 105
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
3-82 1.50e-11

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


:

Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 61.65  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773   3 ENGNVIQTKQNAADGTIQFDAISYAAAGTHTYTVREKAGTDTNIDYDPMNAVVTVNVTkDAQTGLLNAAVTMPADTE--F 80
Cdd:pfam12892  24 EDGNVIQTAKNDADGTVTFGDITYTKAGTYTYTVTEVNGGVPGVTYDTHTYTVTVTVT-DNGDGTLTATVTYDDGTEltF 102

                  ..
gi 2310739773  81 NN 82
Cdd:pfam12892 103 TN 104
 
Name Accession Description Interval E-value
AgI_II_C2 pfam17998
Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the ...
486-635 6.13e-31

Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the C-terminal region found in antigen I/II type adhesin protein AspA from S. pyogenes. Together with C3, these two domains form an elongated structure, each domain adopts the DEv-IgG fold. Similar to the classical IgG folds, it is comprised of two major antiparallel beta-sheets, designated ABED and CFG. For the C2-domain, there are two additional strands on the CFG sheet. Furthermore, sheets ABED and CFG are interconnected by several cross-connecting loops and one alpha-helix (DH1). The side chains of D982 and N996 in the C2-domain are involved in hydrogen bonding with the side chains of R1264 and N1295 in the C3 domain. Main chain hydrogen bonding can also be observed between S992 in C2 and N1189/G1191 in C3, furthermore stabilizing the interaction between the domains. The C2 domain contains one bound metal ion, modeled as Ca2+, and both the C2- and C3-domains are stabilized by conserved isopeptide bonds, which connect the beta-sheets of the central DEv-IgG motifs.Other members of this family include Major cell-surface adhesin PAc from Streptococcus mutans and SspB from Streptococcus gordonii.


Pssm-ID: 465609 [Multi-domain]  Cd Length: 180  Bit Score: 119.88  E-value: 6.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 486 VDKTTNNEPENLNTKTVKRGSKLVYQVWLDTTKFTEANNI----QYVGVSDTYDAEKLDVNAADIKAYDSVTGAEVTNKF 561
Cdd:pfam17998   2 TKTVTNENGVSIDGKTVLRGDTLYYRVTLDLTQYKGIAAYdvirKGFGIVDDYDEEYLTVDAATIKVIDDATGKDVTGKF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 562 DIKVENGTITATSK--------DEFIK-----------------DKVNAPVIDTTKFEFGRYYKFDIPATVKESVKAGAD 616
Cdd:pfam17998  82 NIQVRDGVVYAFAKtvdslvpaTGEVQgdpqpadlkpygafqvfDALDPPAFDQTYLQKGQTYTLVLPMTVKKDVDGGGT 161
                         170
                  ....*....|....*....
gi 2310739773 617 IENTANQTVHVYNPVSKTV 635
Cdd:pfam17998 162 IENTAYQVDFGNGYVTNTV 180
AgI_II_C2 pfam17998
Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the ...
813-899 2.26e-18

Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the C-terminal region found in antigen I/II type adhesin protein AspA from S. pyogenes. Together with C3, these two domains form an elongated structure, each domain adopts the DEv-IgG fold. Similar to the classical IgG folds, it is comprised of two major antiparallel beta-sheets, designated ABED and CFG. For the C2-domain, there are two additional strands on the CFG sheet. Furthermore, sheets ABED and CFG are interconnected by several cross-connecting loops and one alpha-helix (DH1). The side chains of D982 and N996 in the C2-domain are involved in hydrogen bonding with the side chains of R1264 and N1295 in the C3 domain. Main chain hydrogen bonding can also be observed between S992 in C2 and N1189/G1191 in C3, furthermore stabilizing the interaction between the domains. The C2 domain contains one bound metal ion, modeled as Ca2+, and both the C2- and C3-domains are stabilized by conserved isopeptide bonds, which connect the beta-sheets of the central DEv-IgG motifs.Other members of this family include Major cell-surface adhesin PAc from Streptococcus mutans and SspB from Streptococcus gordonii.


Pssm-ID: 465609 [Multi-domain]  Cd Length: 180  Bit Score: 83.67  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 813 NNEAENLNTKTVERGSKLVYQVWLDTTKFDAANKDNIQ--TVGISDNYDEAKLNLNAADIKAYDSVTGAEVTDKFDIAVN 890
Cdd:pfam17998   7 NENGVSIDGKTVLRGDTLYYRVTLDLTQYKGIAAYDVIrkGFGIVDDYDEEYLTVDAATIKVIDDATGKDVTGKFNIQVR 86

                  ....*....
gi 2310739773 891 NGVITATLK 899
Cdd:pfam17998  87 DGVVYAFAK 95
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
207-308 5.74e-18

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 80.14  E-value: 5.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 207 FKFTKKLEGKELTKDAFTFEL-LENGNVIQTKKNAADGSITFDAIEYNAVGEHTYTVREKAGNDINIDYDTMNAEVKVKV 285
Cdd:pfam12892   1 LKATKTLTGRDLKDGEFTFTLtDEDGNVIQTAKNDADGTVTFGDITYTKAGTYTYTVTEVNGGVPGVTYDTHTYTVTVTV 80
                          90       100
                  ....*....|....*....|....*
gi 2310739773 286 TkDAATGLLSTAVTMPEDTE--FNN 308
Cdd:pfam12892  81 T-DNGDGTLTATVTYDDGTEltFTN 104
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
321-420 2.89e-15

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 72.43  E-value: 2.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 321 TKKLAGRELKDGEFKFILKDANGREVETVTNKADGTVTFSELSFDntKVGTHTYTVEEVIPANKefGMTYDQMKATVTVE 400
Cdd:pfam12892   4 TKTLTGRDLKDGEFTFTLTDEDGNVIQTAKNDADGTVTFGDITYT--KAGTYTYTVTEVNGGVP--GVTYDTHTYTVTVT 79
                          90       100
                  ....*....|....*....|
gi 2310739773 401 VAKNGHSLTTVTNVTSTGGK 420
Cdd:pfam12892  80 VTDNGDGTLTATVTYDDGTE 99
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
95-199 8.10e-15

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 71.28  E-value: 8.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  95 SKALAGRELKEGEFSFVLKDSNGKTLQTKTNTKQGVVAFDDLTFDntQVGTHKYTVEEVIPEnkETGMTYDPMKAEVTIT 174
Cdd:pfam12892   4 TKTLTGRDLKDGEFTFTLTDEDGNVIQTAKNDADGTVTFGDITYT--KAGTYTYTVTEVNGG--VPGVTYDTHTYTVTVT 79
                          90       100
                  ....*....|....*....|....*...
gi 2310739773 175 VTKEGH-VLKATNTLPADTE--FNNTFT 199
Cdd:pfam12892  80 VTDNGDgTLTATVTYDDGTEltFTNTYK 107
isopep_sspB_C2 TIGR04228
adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 ...
488-623 3.57e-14

adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 in seed alignment) and Asn at 177 that form an intramolecular isopeptide bond. The Asp (or Glu) at position 59


Pssm-ID: 275068 [Multi-domain]  Cd Length: 173  Bit Score: 71.56  E-value: 3.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 488 KTTNNEPENLNTKTVKRGSKLVYQVWLDTTKF-----TEANNIQYVGVSDTYDAEKLDVNAADIKAYDSvTGAEVTNKFD 562
Cdd:TIGR04228   4 KNTNDAGVNIDGKTVLPGSTNYYRLTWDLSQYkgikaSKEAIAKGFGYVDDYDEEALTVDQDKITITDS-NGKDVTGLFT 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310739773 563 IKVENGTITATSK-DEFIKDKVNAPV-------------IDTTKFEFGRYYKFDIPATVKEsVKAGADIENTANQ 623
Cdd:TIGR04228  83 MYHVLSVKEAPAKvQAILKAAGITPKgefqvwvakdpqaFYKNYVQTGQNITIVLPMTVKK-DKTGGKVENTAYQ 156
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
656-760 1.20e-11

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 62.03  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 656 NFTKRLEGRELQAKEFEFVLK-KDGVEVERVKNDAAGKIVFKTLEFGRDdlgKTYNYTVEETPGTDATVKYDTMVATVKV 734
Cdd:pfam12892   2 KATKTLTGRDLKDGEFTFTLTdEDGNVIQTAKNDADGTVTFGDITYTKA---GTYTYTVTEVNGGVPGVTYDTHTYTVTV 78
                          90       100
                  ....*....|....*....|....*..
gi 2310739773 735 VVSHDGTAK-AIVANVTDAADKEFNNR 760
Cdd:pfam12892  79 TVTDNGDGTlTATVTYDDGTELTFTNT 105
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
3-82 1.50e-11

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 61.65  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773   3 ENGNVIQTKQNAADGTIQFDAISYAAAGTHTYTVREKAGTDTNIDYDPMNAVVTVNVTkDAQTGLLNAAVTMPADTE--F 80
Cdd:pfam12892  24 EDGNVIQTAKNDADGTVTFGDITYTKAGTYTYTVTEVNGGVPGVTYDTHTYTVTVTVT-DNGDGTLTATVTYDDGTEltF 102

                  ..
gi 2310739773  81 NN 82
Cdd:pfam12892 103 TN 104
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
152-900 7.60e-10

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 63.19  E-value: 7.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  152 EVIPENKETGMTYDPMKAEVTITVTKEGHVLKATN-TLPADTEFNNTFTPVA--TQAQF----KFTKKLEGKelTKDAFT 224
Cdd:NF033875   236 EIAAKNKAEKERYEKEVAEYNKHKNENGYVNEAISkNLVFDQSVVTKDTKISsiKGGKFikatDFNKVNAGD--SKDIFT 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  225 -FELLENGNVIQTKKNAadgsiTFDAIEYNAVGehTYTVREKAGNDINIDYDTMNAEVKVKvtKDAATGLLSTAVTMPED 303
Cdd:NF033875   314 kLSKDMGGKATGNFQNS-----FVKEANLGSNG--GYAVLLEKNKPVTVTYTGLNASYLGR--KITKAEFVYELQSSPSQ 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  304 TEFNNYVVS--PVVTKFDFTKKLAGRELKDgEFKFILKDANGREVetvTNKADGTVTFSeLSFDNTKVGTHTYTVEEVip 381
Cdd:NF033875   385 SGTLNAVFSndPIITAFVGTNNVNGKDVKT-RLTIKFFDASGKEV---LPDKDSPFAYA-LSSLNSSLTNKGGHAEFV-- 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  382 anKEFGMTyDQMKATVTVEVAKN---------------GHSLTTVTNVTSTGGKDANGKATDG---TPDK---EFNNKVT 440
Cdd:NF033875   458 --SDFGAN-NAFKYINGSYVKKQadgkfyspedidygtGPSGLKNSDWDAVGHKNAYFGSGVGlanTPGRisfSFGMTTK 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  441 PPETPEFQPEKFVVSKE-------KYDITGNKLMDDDDELTNEYTETNADPYV--DKTTNNEPENLNTKTVKRGSKLVYQ 511
Cdd:NF033875   535 GKNVPVSSAQWFAFSTNlnaksikPYQNKGNPKEPEKATIEFNRYKANVVPVLvpNKEVTDGQKNINDLNVKRGDSLQYI 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  512 VWLDTTKFTEAN--NIQYVGVSDTYDAEKLDVNAADIKAY------------------DSVTGAEVTNKFDIKVENGTIT 571
Cdd:NF033875   615 VTGDTTELAKVDpkTVTKQGIRDTFDAEKVTIDLSKVKVYqadaslnekdlkavaaaiNSGKAKDVTASYDLHLDQNTVT 694
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  572 ATSkdefikdKVNAPviDTTKFEFGRYYKFDIPATVKesvKAGADIENTANQTVHVYNPVSKTVekpekptqkrVNSVPV 651
Cdd:NF033875   695 AMM-------KTNAD--GSVVLAMGYKYLLVLPFVVK---NVEGDFENTAVQLTNDGETVTNTV----------INHVPG 752
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  652 P-----VEMNFTKRLEGRELQAKEFEFVLKkdgVEVERVKNDAAGKIVFKTLEFGRDDL---------GKTYNYTVEETP 717
Cdd:NF033875   753 SnpskdVKADKNGTVGSVSLHDKDIPLQTK---IYYEVKSSERPANYGGITEEWGMNDVldtthdrftGKWHAITNYDLK 829
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  718 GTDATVKYDTMVATVKVVVSHDGTAKAIVAN-VTDAADKEFNNRVTPPEEPKFQPEKYVVSKekyDITGDKLVDDDRELA 796
Cdd:NF033875   830 VGDKTLKAGTDISAYILLENKDNKDLTFTMNqALLAALNEGSNKVGKQAWSVYLEVERIKTG---DVENTQTENYNKELV 906
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  797 DKYADTNANPyaDDAS------NNEAENLNTKTVERGSKLVYQVWLDTTKFD---AANKDNIQT-VGISDNYDEAKLNLN 866
Cdd:NF033875   907 RSNTVVTHTP--DDPKptkavhNKKGEDINHGKVARGDVLSYEMTWDLKGYDkdfAFDTVDLATgVSFFDDYDETKVTPI 984
                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 2310739773  867 AADIKAYDSvTGAEVTDKFDIAVNN--GVITATLKD 900
Cdd:NF033875   985 KDLLRVKDS-KGVDITNQFTISWDDakGTVTISAKD 1019
isopep_sspB_C2 TIGR04228
adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 ...
813-899 1.89e-09

adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 in seed alignment) and Asn at 177 that form an intramolecular isopeptide bond. The Asp (or Glu) at position 59


Pssm-ID: 275068 [Multi-domain]  Cd Length: 173  Bit Score: 57.69  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 813 NNEAENLNTKTVERGSKLVYQVWLDTTKF---DAANKDNIQTVGISDNYDEAKLNLNAADIKAYDSvTGAEVTDKFDIAV 889
Cdd:TIGR04228   7 NDAGVNIDGKTVLPGSTNYYRLTWDLSQYkgiKASKEAIAKGFGYVDDYDEEALTVDQDKITITDS-NGKDVTGLFTMYH 85
                          90
                  ....*....|
gi 2310739773 890 NNGVITATLK 899
Cdd:TIGR04228  86 VLSVKEAPAK 95
strep_pil_rpt TIGR03786
streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once ...
247-303 3.60e-07

streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation.


Pssm-ID: 274781 [Multi-domain]  Cd Length: 63  Bit Score: 48.07  E-value: 3.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2310739773 247 FDAIEYNAVGEHTYTVREKAGNDINIDYDTMNAEVKVKVTKDAATGLLSTAVTMPED 303
Cdd:TIGR03786   1 FSPLTFTKVGTYTYTVTEVKGKEPGVTYDTTVHTVTVTVTDDEQGKLVATVIYDKEK 57
strep_pil_rpt TIGR03786
streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once ...
21-83 3.93e-07

streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation.


Pssm-ID: 274781 [Multi-domain]  Cd Length: 63  Bit Score: 47.68  E-value: 3.93e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310739773  21 FDAISYAAAGTHTYTVREKAGTDTNIDYDPMNAVVTVNVTKDAQtGLLNAAVTMPADTEFNNF 83
Cdd:TIGR03786   1 FSPLTFTKVGTYTYTVTEVKGKEPGVTYDTTVHTVTVTVTDDEQ-GKLVATVIYDKEKNPITF 62
strep_pil_rpt TIGR03786
streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once ...
359-406 5.73e-04

streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation.


Pssm-ID: 274781 [Multi-domain]  Cd Length: 63  Bit Score: 38.82  E-value: 5.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2310739773 359 FSELSFdnTKVGTHTYTVEEVipANKEFGMTYDQMKATVTVEVAKNGH 406
Cdd:TIGR03786   1 FSPLTF--TKVGTYTYTVTEV--KGKEPGVTYDTTVHTVTVTVTDDEQ 44
strep_pil_rpt TIGR03786
streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once ...
133-199 1.26e-03

streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation.


Pssm-ID: 274781 [Multi-domain]  Cd Length: 63  Bit Score: 38.05  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310739773 133 FDDLTFdnTQVGTHKYTVEEVipENKETGMTYDPMKAEVTITVTKEGHVLKATNTLPADTEFNNTFT 199
Cdd:TIGR03786   1 FSPLTF--TKVGTYTYTVTEV--KGKEPGVTYDTTVHTVTVTVTDDEQGKLVATVIYDKEKNPITFT 63
strep_pil_rpt TIGR03786
streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once ...
695-750 1.92e-03

streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation.


Pssm-ID: 274781 [Multi-domain]  Cd Length: 63  Bit Score: 37.28  E-value: 1.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310739773 695 FKTLEFgrdDLGKTYNYTVEETPGTDATVKYDTMVATVKVVVSHDGTAKaIVANVT 750
Cdd:TIGR03786   1 FSPLTF---TKVGTYTYTVTEVKGKEPGVTYDTTVHTVTVTVTDDEQGK-LVATVI 52
 
Name Accession Description Interval E-value
AgI_II_C2 pfam17998
Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the ...
486-635 6.13e-31

Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the C-terminal region found in antigen I/II type adhesin protein AspA from S. pyogenes. Together with C3, these two domains form an elongated structure, each domain adopts the DEv-IgG fold. Similar to the classical IgG folds, it is comprised of two major antiparallel beta-sheets, designated ABED and CFG. For the C2-domain, there are two additional strands on the CFG sheet. Furthermore, sheets ABED and CFG are interconnected by several cross-connecting loops and one alpha-helix (DH1). The side chains of D982 and N996 in the C2-domain are involved in hydrogen bonding with the side chains of R1264 and N1295 in the C3 domain. Main chain hydrogen bonding can also be observed between S992 in C2 and N1189/G1191 in C3, furthermore stabilizing the interaction between the domains. The C2 domain contains one bound metal ion, modeled as Ca2+, and both the C2- and C3-domains are stabilized by conserved isopeptide bonds, which connect the beta-sheets of the central DEv-IgG motifs.Other members of this family include Major cell-surface adhesin PAc from Streptococcus mutans and SspB from Streptococcus gordonii.


Pssm-ID: 465609 [Multi-domain]  Cd Length: 180  Bit Score: 119.88  E-value: 6.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 486 VDKTTNNEPENLNTKTVKRGSKLVYQVWLDTTKFTEANNI----QYVGVSDTYDAEKLDVNAADIKAYDSVTGAEVTNKF 561
Cdd:pfam17998   2 TKTVTNENGVSIDGKTVLRGDTLYYRVTLDLTQYKGIAAYdvirKGFGIVDDYDEEYLTVDAATIKVIDDATGKDVTGKF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 562 DIKVENGTITATSK--------DEFIK-----------------DKVNAPVIDTTKFEFGRYYKFDIPATVKESVKAGAD 616
Cdd:pfam17998  82 NIQVRDGVVYAFAKtvdslvpaTGEVQgdpqpadlkpygafqvfDALDPPAFDQTYLQKGQTYTLVLPMTVKKDVDGGGT 161
                         170
                  ....*....|....*....
gi 2310739773 617 IENTANQTVHVYNPVSKTV 635
Cdd:pfam17998 162 IENTAYQVDFGNGYVTNTV 180
AgI_II_C2 pfam17998
Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the ...
813-899 2.26e-18

Cell surface antigen I/II C2 terminal domain; This is the second domain (C2) located in the C-terminal region found in antigen I/II type adhesin protein AspA from S. pyogenes. Together with C3, these two domains form an elongated structure, each domain adopts the DEv-IgG fold. Similar to the classical IgG folds, it is comprised of two major antiparallel beta-sheets, designated ABED and CFG. For the C2-domain, there are two additional strands on the CFG sheet. Furthermore, sheets ABED and CFG are interconnected by several cross-connecting loops and one alpha-helix (DH1). The side chains of D982 and N996 in the C2-domain are involved in hydrogen bonding with the side chains of R1264 and N1295 in the C3 domain. Main chain hydrogen bonding can also be observed between S992 in C2 and N1189/G1191 in C3, furthermore stabilizing the interaction between the domains. The C2 domain contains one bound metal ion, modeled as Ca2+, and both the C2- and C3-domains are stabilized by conserved isopeptide bonds, which connect the beta-sheets of the central DEv-IgG motifs.Other members of this family include Major cell-surface adhesin PAc from Streptococcus mutans and SspB from Streptococcus gordonii.


Pssm-ID: 465609 [Multi-domain]  Cd Length: 180  Bit Score: 83.67  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 813 NNEAENLNTKTVERGSKLVYQVWLDTTKFDAANKDNIQ--TVGISDNYDEAKLNLNAADIKAYDSVTGAEVTDKFDIAVN 890
Cdd:pfam17998   7 NENGVSIDGKTVLRGDTLYYRVTLDLTQYKGIAAYDVIrkGFGIVDDYDEEYLTVDAATIKVIDDATGKDVTGKFNIQVR 86

                  ....*....
gi 2310739773 891 NGVITATLK 899
Cdd:pfam17998  87 DGVVYAFAK 95
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
207-308 5.74e-18

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 80.14  E-value: 5.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 207 FKFTKKLEGKELTKDAFTFEL-LENGNVIQTKKNAADGSITFDAIEYNAVGEHTYTVREKAGNDINIDYDTMNAEVKVKV 285
Cdd:pfam12892   1 LKATKTLTGRDLKDGEFTFTLtDEDGNVIQTAKNDADGTVTFGDITYTKAGTYTYTVTEVNGGVPGVTYDTHTYTVTVTV 80
                          90       100
                  ....*....|....*....|....*
gi 2310739773 286 TkDAATGLLSTAVTMPEDTE--FNN 308
Cdd:pfam12892  81 T-DNGDGTLTATVTYDDGTEltFTN 104
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
321-420 2.89e-15

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 72.43  E-value: 2.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 321 TKKLAGRELKDGEFKFILKDANGREVETVTNKADGTVTFSELSFDntKVGTHTYTVEEVIPANKefGMTYDQMKATVTVE 400
Cdd:pfam12892   4 TKTLTGRDLKDGEFTFTLTDEDGNVIQTAKNDADGTVTFGDITYT--KAGTYTYTVTEVNGGVP--GVTYDTHTYTVTVT 79
                          90       100
                  ....*....|....*....|
gi 2310739773 401 VAKNGHSLTTVTNVTSTGGK 420
Cdd:pfam12892  80 VTDNGDGTLTATVTYDDGTE 99
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
95-199 8.10e-15

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 71.28  E-value: 8.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  95 SKALAGRELKEGEFSFVLKDSNGKTLQTKTNTKQGVVAFDDLTFDntQVGTHKYTVEEVIPEnkETGMTYDPMKAEVTIT 174
Cdd:pfam12892   4 TKTLTGRDLKDGEFTFTLTDEDGNVIQTAKNDADGTVTFGDITYT--KAGTYTYTVTEVNGG--VPGVTYDTHTYTVTVT 79
                          90       100
                  ....*....|....*....|....*...
gi 2310739773 175 VTKEGH-VLKATNTLPADTE--FNNTFT 199
Cdd:pfam12892  80 VTDNGDgTLTATVTYDDGTEltFTNTYK 107
isopep_sspB_C2 TIGR04228
adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 ...
488-623 3.57e-14

adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 in seed alignment) and Asn at 177 that form an intramolecular isopeptide bond. The Asp (or Glu) at position 59


Pssm-ID: 275068 [Multi-domain]  Cd Length: 173  Bit Score: 71.56  E-value: 3.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 488 KTTNNEPENLNTKTVKRGSKLVYQVWLDTTKF-----TEANNIQYVGVSDTYDAEKLDVNAADIKAYDSvTGAEVTNKFD 562
Cdd:TIGR04228   4 KNTNDAGVNIDGKTVLPGSTNYYRLTWDLSQYkgikaSKEAIAKGFGYVDDYDEEALTVDQDKITITDS-NGKDVTGLFT 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310739773 563 IKVENGTITATSK-DEFIKDKVNAPV-------------IDTTKFEFGRYYKFDIPATVKEsVKAGADIENTANQ 623
Cdd:TIGR04228  83 MYHVLSVKEAPAKvQAILKAAGITPKgefqvwvakdpqaFYKNYVQTGQNITIVLPMTVKK-DKTGGKVENTAYQ 156
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
656-760 1.20e-11

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 62.03  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 656 NFTKRLEGRELQAKEFEFVLK-KDGVEVERVKNDAAGKIVFKTLEFGRDdlgKTYNYTVEETPGTDATVKYDTMVATVKV 734
Cdd:pfam12892   2 KATKTLTGRDLKDGEFTFTLTdEDGNVIQTAKNDADGTVTFGDITYTKA---GTYTYTVTEVNGGVPGVTYDTHTYTVTV 78
                          90       100
                  ....*....|....*....|....*..
gi 2310739773 735 VVSHDGTAK-AIVANVTDAADKEFNNR 760
Cdd:pfam12892  79 TVTDNGDGTlTATVTYDDGTELTFTNT 105
FctA pfam12892
Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of ...
3-82 1.50e-11

Spy0128-like isopeptide containing domain; The FCT and equivalent region genes of Streptococcus pyogenes and other related bacteria encode surface proteins that include fibronectin- and collagen-binding proteins and the serological markers known as T antigens. Some of these proteins give rise to pilus-like appendages. The FctA family is found in many Firmicutes and related bacteria. In S. pyogenes, the pili have a role in bacterial adherence and colonization of human tissues. Members of this family have a conserved N-terminal lysine and C-terminal asparagine that can form a covalent isopeptide bond.


Pssm-ID: 463742 [Multi-domain]  Cd Length: 107  Bit Score: 61.65  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773   3 ENGNVIQTKQNAADGTIQFDAISYAAAGTHTYTVREKAGTDTNIDYDPMNAVVTVNVTkDAQTGLLNAAVTMPADTE--F 80
Cdd:pfam12892  24 EDGNVIQTAKNDADGTVTFGDITYTKAGTYTYTVTEVNGGVPGVTYDTHTYTVTVTVT-DNGDGTLTATVTYDDGTEltF 102

                  ..
gi 2310739773  81 NN 82
Cdd:pfam12892 103 TN 104
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
152-900 7.60e-10

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 63.19  E-value: 7.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  152 EVIPENKETGMTYDPMKAEVTITVTKEGHVLKATN-TLPADTEFNNTFTPVA--TQAQF----KFTKKLEGKelTKDAFT 224
Cdd:NF033875   236 EIAAKNKAEKERYEKEVAEYNKHKNENGYVNEAISkNLVFDQSVVTKDTKISsiKGGKFikatDFNKVNAGD--SKDIFT 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  225 -FELLENGNVIQTKKNAadgsiTFDAIEYNAVGehTYTVREKAGNDINIDYDTMNAEVKVKvtKDAATGLLSTAVTMPED 303
Cdd:NF033875   314 kLSKDMGGKATGNFQNS-----FVKEANLGSNG--GYAVLLEKNKPVTVTYTGLNASYLGR--KITKAEFVYELQSSPSQ 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  304 TEFNNYVVS--PVVTKFDFTKKLAGRELKDgEFKFILKDANGREVetvTNKADGTVTFSeLSFDNTKVGTHTYTVEEVip 381
Cdd:NF033875   385 SGTLNAVFSndPIITAFVGTNNVNGKDVKT-RLTIKFFDASGKEV---LPDKDSPFAYA-LSSLNSSLTNKGGHAEFV-- 457
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  382 anKEFGMTyDQMKATVTVEVAKN---------------GHSLTTVTNVTSTGGKDANGKATDG---TPDK---EFNNKVT 440
Cdd:NF033875   458 --SDFGAN-NAFKYINGSYVKKQadgkfyspedidygtGPSGLKNSDWDAVGHKNAYFGSGVGlanTPGRisfSFGMTTK 534
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  441 PPETPEFQPEKFVVSKE-------KYDITGNKLMDDDDELTNEYTETNADPYV--DKTTNNEPENLNTKTVKRGSKLVYQ 511
Cdd:NF033875   535 GKNVPVSSAQWFAFSTNlnaksikPYQNKGNPKEPEKATIEFNRYKANVVPVLvpNKEVTDGQKNINDLNVKRGDSLQYI 614
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  512 VWLDTTKFTEAN--NIQYVGVSDTYDAEKLDVNAADIKAY------------------DSVTGAEVTNKFDIKVENGTIT 571
Cdd:NF033875   615 VTGDTTELAKVDpkTVTKQGIRDTFDAEKVTIDLSKVKVYqadaslnekdlkavaaaiNSGKAKDVTASYDLHLDQNTVT 694
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  572 ATSkdefikdKVNAPviDTTKFEFGRYYKFDIPATVKesvKAGADIENTANQTVHVYNPVSKTVekpekptqkrVNSVPV 651
Cdd:NF033875   695 AMM-------KTNAD--GSVVLAMGYKYLLVLPFVVK---NVEGDFENTAVQLTNDGETVTNTV----------INHVPG 752
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  652 P-----VEMNFTKRLEGRELQAKEFEFVLKkdgVEVERVKNDAAGKIVFKTLEFGRDDL---------GKTYNYTVEETP 717
Cdd:NF033875   753 SnpskdVKADKNGTVGSVSLHDKDIPLQTK---IYYEVKSSERPANYGGITEEWGMNDVldtthdrftGKWHAITNYDLK 829
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  718 GTDATVKYDTMVATVKVVVSHDGTAKAIVAN-VTDAADKEFNNRVTPPEEPKFQPEKYVVSKekyDITGDKLVDDDRELA 796
Cdd:NF033875   830 VGDKTLKAGTDISAYILLENKDNKDLTFTMNqALLAALNEGSNKVGKQAWSVYLEVERIKTG---DVENTQTENYNKELV 906
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773  797 DKYADTNANPyaDDAS------NNEAENLNTKTVERGSKLVYQVWLDTTKFD---AANKDNIQT-VGISDNYDEAKLNLN 866
Cdd:NF033875   907 RSNTVVTHTP--DDPKptkavhNKKGEDINHGKVARGDVLSYEMTWDLKGYDkdfAFDTVDLATgVSFFDDYDETKVTPI 984
                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 2310739773  867 AADIKAYDSvTGAEVTDKFDIAVNN--GVITATLKD 900
Cdd:NF033875   985 KDLLRVKDS-KGVDITNQFTISWDDakGTVTISAKD 1019
isopep_sspB_C2 TIGR04228
adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 ...
813-899 1.89e-09

adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 in seed alignment) and Asn at 177 that form an intramolecular isopeptide bond. The Asp (or Glu) at position 59


Pssm-ID: 275068 [Multi-domain]  Cd Length: 173  Bit Score: 57.69  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310739773 813 NNEAENLNTKTVERGSKLVYQVWLDTTKF---DAANKDNIQTVGISDNYDEAKLNLNAADIKAYDSvTGAEVTDKFDIAV 889
Cdd:TIGR04228   7 NDAGVNIDGKTVLPGSTNYYRLTWDLSQYkgiKASKEAIAKGFGYVDDYDEEALTVDQDKITITDS-NGKDVTGLFTMYH 85
                          90
                  ....*....|
gi 2310739773 890 NNGVITATLK 899
Cdd:TIGR04228  86 VLSVKEAPAK 95
strep_pil_rpt TIGR03786
streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once ...
247-303 3.60e-07

streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation.


Pssm-ID: 274781 [Multi-domain]  Cd Length: 63  Bit Score: 48.07  E-value: 3.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2310739773 247 FDAIEYNAVGEHTYTVREKAGNDINIDYDTMNAEVKVKVTKDAATGLLSTAVTMPED 303
Cdd:TIGR03786   1 FSPLTFTKVGTYTYTVTEVKGKEPGVTYDTTVHTVTVTVTDDEQGKLVATVIYDKEK 57
strep_pil_rpt TIGR03786
streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once ...
21-83 3.93e-07

streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation.


Pssm-ID: 274781 [Multi-domain]  Cd Length: 63  Bit Score: 47.68  E-value: 3.93e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310739773  21 FDAISYAAAGTHTYTVREKAGTDTNIDYDPMNAVVTVNVTKDAQtGLLNAAVTMPADTEFNNF 83
Cdd:TIGR03786   1 FSPLTFTKVGTYTYTVTEVKGKEPGVTYDTTVHTVTVTVTDDEQ-GKLVATVIYDKEKNPITF 62
strep_pil_rpt TIGR03786
streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once ...
359-406 5.73e-04

streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation.


Pssm-ID: 274781 [Multi-domain]  Cd Length: 63  Bit Score: 38.82  E-value: 5.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2310739773 359 FSELSFdnTKVGTHTYTVEEVipANKEFGMTYDQMKATVTVEVAKNGH 406
Cdd:TIGR03786   1 FSPLTF--TKVGTYTYTVTEV--KGKEPGVTYDTTVHTVTVTVTDDEQ 44
strep_pil_rpt TIGR03786
streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once ...
133-199 1.26e-03

streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation.


Pssm-ID: 274781 [Multi-domain]  Cd Length: 63  Bit Score: 38.05  E-value: 1.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310739773 133 FDDLTFdnTQVGTHKYTVEEVipENKETGMTYDPMKAEVTITVTKEGHVLKATNTLPADTEFNNTFT 199
Cdd:TIGR03786   1 FSPLTF--TKVGTYTYTVTEV--KGKEPGVTYDTTVHTVTVTVTDDEQGKLVATVIYDKEKNPITFT 63
strep_pil_rpt TIGR03786
streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once ...
695-750 1.92e-03

streptococcal pilin isopeptide linkage domain; This model describes a domain that occurs once in the major pilin of Streptococcus pyogenes, Spy0128, but in higher copy numbers in other streptococcal proteins. The domain occurs nine times in a surface-anchored protein of Bifidobacterium longum. All members of this family have LPXTG-type sortase target sequences. The S. pyogenes major pilin has been shown to undergo isopeptide bond cross-linking, mediated by sortases, that are critical to maintaining pilus structural integrity. One such Lys-to-Asn isopeptide bond is to a near-invariant Asn near the C-terminal end of this domain (column 81 of the seed alignment). A Glu in the S. pyogenes major pilin (column 25 of the seed alignment), invariant as Glu or Gln, is described as catalytic for isopeptide bond formation.


Pssm-ID: 274781 [Multi-domain]  Cd Length: 63  Bit Score: 37.28  E-value: 1.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2310739773 695 FKTLEFgrdDLGKTYNYTVEETPGTDATVKYDTMVATVKVVVSHDGTAKaIVANVT 750
Cdd:TIGR03786   1 FSPLTF---TKVGTYTYTVTEVKGKEPGVTYDTTVHTVTVTVTDDEQGK-LVATVI 52
 
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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