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Conserved domains on  [gi|755571595|ref|NP_001291686|]
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collagen alpha-1(XIII) chain isoform 2 [Mus musculus]

Protein Classification

collagen-like domain-containing protein( domain architecture ID 1903237)

collagen-like domain-containing protein such as collagens, which are extracellular structural proteins involved in formation of connective tissue structure

PubMed:  21421911|15837519

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 388-659 5.04e-22

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.59  E-value: 5.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 388 GDKGQPGAAGEQGPSGPKGAKGEPGkgemvdyngsinealqeirtlalmgppglpgqtgppgppgtpgQRGEIGLPGPPG 467
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRG-------------------------------------------ETGPAGPAGPPG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 468 HDGDKGPRGKPGDMGPAGPQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGEKGEAGEKGDPGAEVPGPPGPEGPPG 547
Cdd:NF038329 154 PQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 548 PPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPP 627
Cdd:NF038329 234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP 313

                        250       260       270
                 ....*....|....*....|....*....|..
gi 755571595 628 GDKGNRGERGKKGSRGPKGDKGDQGAPGLDAP 659
Cdd:NF038329 314 GKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 294-533 3.87e-14

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.94  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 294 GERGMPGMPGKHGAKGVPGiaVAGMKGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpGPPGPKG 373
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQG--PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ--------------GPAGKDG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 374 EAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGKGEMVDYNGSINEALQEIRTLA-LMGPPGLPGQTGPPGPPG 452
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPgPTGEDGPQGPDGPAGKDG 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 453 TPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAGPQGPPGKDGPpgmKGEVGPPGSPGEKGETGQAGPQGEKGEAGEKGDP 532
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                 .
gi 755571595 533 G 533
Cdd:NF038329 338 G 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 135-413 6.84e-11

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.93  E-value: 6.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 135 GAIGMPGRVGAPGDAGMsiVGPRGPPGQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGEY 214
Cdd:NF038329 117 GEKGEPGPAGPAGPAGE--QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 215 PHREYPGGmlaalrsnpimslKGEQSQTGIQGPPGPPGPPGPSGPLGHPGLPGPIGPPGlpgppgpkgdpgiQGYHGRKG 294
Cdd:NF038329 195 GPRGETGP-------------AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD-------------PGPTGEDG 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 295 ERGMPGMPGKHGAKGVPGIAvagmkGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgpkge 374
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEA-----GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD---------------------- 301

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755571595 375 aGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGK 413
Cdd:NF038329 302 -GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 388-659 5.04e-22

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.59  E-value: 5.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 388 GDKGQPGAAGEQGPSGPKGAKGEPGkgemvdyngsinealqeirtlalmgppglpgqtgppgppgtpgQRGEIGLPGPPG 467
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRG-------------------------------------------ETGPAGPAGPPG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 468 HDGDKGPRGKPGDMGPAGPQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGEKGEAGEKGDPGAEVPGPPGPEGPPG 547
Cdd:NF038329 154 PQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 548 PPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPP 627
Cdd:NF038329 234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP 313

                        250       260       270
                 ....*....|....*....|....*....|..
gi 755571595 628 GDKGNRGERGKKGSRGPKGDKGDQGAPGLDAP 659
Cdd:NF038329 314 GKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 509-666 2.08e-14

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 76.10  E-value: 2.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 509 GEKGETGQAGPQGEKGEAGEKGDPGAEvpgppgpegppgppglqgfpgpkgeagleGSKGEKGSQGEKGDRGPLGLPGTP 588
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET-----------------------------GPAGPAGPPGPQGERGEKGPAGPQ 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755571595 589 GPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAPCPLGEDG 666
Cdd:NF038329 168 GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTG 245
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 294-533 3.87e-14

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.94  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 294 GERGMPGMPGKHGAKGVPGiaVAGMKGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpGPPGPKG 373
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQG--PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ--------------GPAGKDG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 374 EAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGKGEMVDYNGSINEALQEIRTLA-LMGPPGLPGQTGPPGPPG 452
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPgPTGEDGPQGPDGPAGKDG 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 453 TPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAGPQGPPGKDGPpgmKGEVGPPGSPGEKGETGQAGPQGEKGEAGEKGDP 532
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                 .
gi 755571595 533 G 533
Cdd:NF038329 338 G 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 135-413 6.84e-11

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.93  E-value: 6.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 135 GAIGMPGRVGAPGDAGMsiVGPRGPPGQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGEY 214
Cdd:NF038329 117 GEKGEPGPAGPAGPAGE--QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 215 PHREYPGGmlaalrsnpimslKGEQSQTGIQGPPGPPGPPGPSGPLGHPGLPGPIGPPGlpgppgpkgdpgiQGYHGRKG 294
Cdd:NF038329 195 GPRGETGP-------------AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD-------------PGPTGEDG 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 295 ERGMPGMPGKHGAKGVPGIAvagmkGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgpkge 374
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEA-----GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD---------------------- 301

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755571595 375 aGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGK 413
Cdd:NF038329 302 -GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 574-628 1.92e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 1.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755571595  574 GEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPG 628
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 134-213 2.69e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 40.66  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 134 KGAIGMPGRVGAPGDAGMSIVGPRGPPGQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGE 213
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 166-211 6.13e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 6.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 755571595  166 RGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQC 211
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 509-668 7.48e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.18  E-value: 7.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 509 GEKGETGQAGPQGEKGEAGEKGDPGaevpgppgpegppgppglqgfpgPKGEAGLEGSKGEKGSQGEKGDRGPLGLPGTP 588
Cdd:PHA03169  82 GEKEERGQGGPSGSGSESVGSPTPS-----------------------PSGSAEELASGLSPENTSGSSPESPASHSPPP 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 589 GPIGVPGPAGPKGERGSKGDPGmTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAPCPLGEDGLP 668
Cdd:PHA03169 139 SPPSHPGPHEPAPPESHNPSPN-QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSP 217
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 388-659 5.04e-22

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 99.59  E-value: 5.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 388 GDKGQPGAAGEQGPSGPKGAKGEPGkgemvdyngsinealqeirtlalmgppglpgqtgppgppgtpgQRGEIGLPGPPG 467
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRG-------------------------------------------ETGPAGPAGPPG 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 468 HDGDKGPRGKPGDMGPAGPQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGEKGEAGEKGDPGAEVPGPPGPEGPPG 547
Cdd:NF038329 154 PQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 548 PPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPP 627
Cdd:NF038329 234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLP 313

                        250       260       270
                 ....*....|....*....|....*....|..
gi 755571595 628 GDKGNRGERGKKGSRGPKGDKGDQGAPGLDAP 659
Cdd:NF038329 314 GKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTP 345
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 509-666 2.08e-14

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 76.10  E-value: 2.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 509 GEKGETGQAGPQGEKGEAGEKGDPGAEvpgppgpegppgppglqgfpgpkgeagleGSKGEKGSQGEKGDRGPLGLPGTP 588
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET-----------------------------GPAGPAGPPGPQGERGEKGPAGPQ 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755571595 589 GPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAPCPLGEDG 666
Cdd:NF038329 168 GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTG 245
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 294-533 3.87e-14

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 74.94  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 294 GERGMPGMPGKHGAKGVPGiaVAGMKGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpGPPGPKG 373
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQG--PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ--------------GPAGKDG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 374 EAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGKGEMVDYNGSINEALQEIRTLA-LMGPPGLPGQTGPPGPPG 452
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPgPTGEDGPQGPDGPAGKDG 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 453 TPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAGPQGPPGKDGPpgmKGEVGPPGSPGEKGETGQAGPQGEKGEAGEKGDP 532
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337


                 .
gi 755571595 533 G 533
Cdd:NF038329 338 G 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 135-413 6.84e-11

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 64.93  E-value: 6.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 135 GAIGMPGRVGAPGDAGMsiVGPRGPPGQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGEY 214
Cdd:NF038329 117 GEKGEPGPAGPAGPAGE--QGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 215 PHREYPGGmlaalrsnpimslKGEQSQTGIQGPPGPPGPPGPSGPLGHPGLPGPIGPPGlpgppgpkgdpgiQGYHGRKG 294
Cdd:NF038329 195 GPRGETGP-------------AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD-------------PGPTGEDG 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 295 ERGMPGMPGKHGAKGVPGIAvagmkGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrgepgppglpgppgpkge 374
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEA-----GPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD---------------------- 301

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 755571595 375 aGVDGQAGPPGQQGDKGQPGAAGEQGPSGPKGAKGEPGK 413
Cdd:NF038329 302 -GKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 574-628 1.92e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.48  E-value: 1.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755571595  574 GEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPG 628
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 580-636 3.90e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.71  E-value: 3.90e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755571595  580 GPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGER 636
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 589-644 6.89e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 6.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 755571595  589 GPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGP 644
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 586-642 7.03e-05

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.94  E-value: 7.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755571595  586 GTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSR 642
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 565-621 2.60e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 2.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755571595  565 GSKGEKGSQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLP 621
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 598-654 2.73e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.40  E-value: 2.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755571595  598 GPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAP 654
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 604-660 3.53e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 3.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755571595  604 GSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAPC 660
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 561-609 1.79e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.09  E-value: 1.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755571595  561 AGLEGSKGEKGSQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDP 609
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 134-213 2.69e-03

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 40.66  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 134 KGAIGMPGRVGAPGDAGMSIVGPRGPPGQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGE 213
Cdd:NF038329 203 AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP 282
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 166-211 6.13e-03

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 6.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 755571595  166 RGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQC 211
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 509-668 7.48e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.18  E-value: 7.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 509 GEKGETGQAGPQGEKGEAGEKGDPGaevpgppgpegppgppglqgfpgPKGEAGLEGSKGEKGSQGEKGDRGPLGLPGTP 588
Cdd:PHA03169  82 GEKEERGQGGPSGSGSESVGSPTPS-----------------------PSGSAEELASGLSPENTSGSSPESPASHSPPP 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755571595 589 GPIGVPGPAGPKGERGSKGDPGmTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAPCPLGEDGLP 668
Cdd:PHA03169 139 SPPSHPGPHEPAPPESHNPSPN-QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSP 217
 
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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