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Conserved domains on  [gi|1587062743|ref|NP_001355814|]
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collagen alpha-1(XIII) chain isoform 26 [Homo sapiens]

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 ...
 393-628 1.40e-23

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: 104.22  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 393 GDKGERGAAGEQGPDGPKGSKGEPGKGEMVDYNGNINEALQEirtlalmGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPG 472
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER-------GEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 473 HDGEKGPRGKPGDMGPPGPQGPPGKDGPPGVKGENGHPGSPGekgeKGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQ 552
Cdd:NF038329  190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1587062743 553 GEKGDRGPLGLPGTPGPigvPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 628
Cdd:NF038329  266 GEAGPDGPDGKDGERGP---VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 166-418 9.81e-09

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: 57.99  E-value: 9.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 166 GFPGFPGPIGLDGKPGHPGPKGDMGLTGPPGQPGPQGQKGEKGQCGEyphrllpllnsvrlapppvikrrtfQGEQsqas 245
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP-------------------------AGPQ---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 246 iqgppgppGPPGPSGPLGHPGLPGPMGPPGLPGPPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGAPGIAVAGMKGEPG 325
Cdd:NF038329  168 --------GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 326 IPGTKGEKGAEGSPGLPGLLGQKGEKGDAGnsigggrgepgppglpgppgPKGEAGVDGQVGPPGQPGDKGERGAAGEQG 405
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAG--------------------PDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299

                         250
                  ....*....|...
gi 1587062743 406 PDGPKGSKGEPGK 418
Cdd:NF038329  300 KDGKDGQNGKDGL 312
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 393-628 1.40e-23

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: 104.22  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 393 GDKGERGAAGEQGPDGPKGSKGEPGKGEMVDYNGNINEALQEirtlalmGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPG 472
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER-------GEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 473 HDGEKGPRGKPGDMGPPGPQGPPGKDGPPGVKGENGHPGSPGekgeKGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQ 552
Cdd:NF038329  190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1587062743 553 GEKGDRGPLGLPGTPGPigvPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 628
Cdd:NF038329  266 GEAGPDGPDGKDGERGP---VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 430-644 8.32e-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: 98.82  E-value: 8.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 430 EALQEIRTLALMGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPGHDGEKGPRGKPGDMGPPGPQGPPGKDGPPGVKGENGH 509
Cdd:NF038329  105 ELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 510 PGSPGEKGE---KGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQGeKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKG 586
Cdd:NF038329  185 KGPAGEKGPqgpRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1587062743 587 DPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDGLD-APCPLGEDGLP 644
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDgLPGKDGKDGQP 322
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 384-609 8.27e-21

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: 95.74  E-value: 8.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 384 GQVGPPGQPGDKGERGAAGEQGPDGPKGSKGEPGKGEMVDYNGNINEALQEirtlALMGPPGLPGQIGPPGAPGIPGQKG 463
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ----GPAGKDGEAGAKGPAGEKGPQGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 464 EIGLPGPPGHDGEKGPRGKPGDMGPPGPQGPPGKDGPPGvKGENGHPGSPGEKGEKGETGQAGSPGLQGVPGPKGEAGLD 543
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGP-DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1587062743 544 GAKGEKGFQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDK 609
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 319-593 1.07e-19

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: 92.28  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 319 GMKGEPGIPGTKGEKGAEGSPGLPGLLGQKGEKGDAGnsigggrgepgppgLPGPPGPKGEAGVDGQVGPPGQPGDKGER 398
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG--------------PQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 399 GAAGEQGPDGPKGSKGEPGKGEMVDYNGninealqeirtlaLMGPPGLPGQIGPPGAPGIPG--QKGEIGLPGPPGHDGE 476
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAG-------------PAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 477 KGPRgkpgdmgppgpqgppgkdgppgvkGENGHPGSPGEKGEKGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQGEKG 556
Cdd:NF038329  250 QGPD------------------------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1587062743 557 DRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGP 593
Cdd:NF038329  306 QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 166-418 9.81e-09

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: 57.99  E-value: 9.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 166 GFPGFPGPIGLDGKPGHPGPKGDMGLTGPPGQPGPQGQKGEKGQCGEyphrllpllnsvrlapppvikrrtfQGEQsqas 245
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP-------------------------AGPQ---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 246 iqgppgppGPPGPSGPLGHPGLPGPMGPPGLPGPPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGAPGIAVAGMKGEPG 325
Cdd:NF038329  168 --------GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 326 IPGTKGEKGAEGSPGLPGLLGQKGEKGDAGnsigggrgepgppglpgppgPKGEAGVDGQVGPPGQPGDKGERGAAGEQG 405
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAG--------------------PDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299

                         250
                  ....*....|...
gi 1587062743 406 PDGPKGSKGEPGK 418
Cdd:NF038329  300 KDGKDGQNGKDGL 312
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 136-418 1.15e-08

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: 57.61  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 136 KGQPGEKGSPGDAGLSiiGPRGPPGQPGTRGFPGFPGPIGLDGKPGHPGPKGDMGLTGPPGQPGPQGQKGEKGQCGEYPH 215
Cdd:NF038329  119 KGEPGPAGPAGPAGEQ--GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 216 RllpllnsvrlapppvikrrtfqGEQSQASIQGPPGPPGPPGPSGPLGHPGLPGPMGPPGLPGPPGpkgdpgiQGYHGRK 295
Cdd:NF038329  197 R----------------------GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD-------PGPTGED 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 296 GERGMPGMPGKHGAKGApgiavagmKGEPGIPGTKGEKGAEGSPGLPGLLGQKGEKGDAGnsigggrgepgppglpgppg 375
Cdd:NF038329  248 GPQGPDGPAGKDGPRGD--------RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG-------------------- 299

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1587062743 376 pkgEAGVDGQVGPPGQPGDKGERGAAGEQGPDGPKGSKGEPGK 418
Cdd:NF038329  300 ---KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 532-588 4.78e-06

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: 44.02  E-value: 4.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1587062743 532 GVPGPKGEAGLDGAKGEKGFQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDP 588
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 511-642 2.52e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 511 GSPGEKGEKGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGM 590
Cdd:PHA03169   82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQ 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1587062743 591 TGPTGAAGLPGLHGPPGDKGNR-----GHRGFKGEKGEPGLPGLDGLDAPCPLGEDG 642
Cdd:PHA03169  162 QPSSFLQPSHEDSPEEPEPPTSepepdSPGPPQSETPTSSPPPQSPPDEPGEPQSPT 218
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 296-355 7.64e-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: 35.16  E-value: 7.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 296 GERGMPGMPGKHGAKGAPGIAvagmkGEPGIPGTKGEKGAEGSPGLPGLLGQKGEKGDAG 355
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP-----GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 393-628 1.40e-23

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: 104.22  E-value: 1.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 393 GDKGERGAAGEQGPDGPKGSKGEPGKGEMVDYNGNINEALQEirtlalmGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPG 472
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGER-------GEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 473 HDGEKGPRGKPGDMGPPGPQGPPGKDGPPGVKGENGHPGSPGekgeKGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQ 552
Cdd:NF038329  190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1587062743 553 GEKGDRGPLGLPGTPGPigvPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 628
Cdd:NF038329  266 GEAGPDGPDGKDGERGP---VGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 430-644 8.32e-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: 98.82  E-value: 8.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 430 EALQEIRTLALMGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPGHDGEKGPRGKPGDMGPPGPQGPPGKDGPPGVKGENGH 509
Cdd:NF038329  105 ELDEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGA 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 510 PGSPGEKGE---KGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQGeKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKG 586
Cdd:NF038329  185 KGPAGEKGPqgpRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1587062743 587 DPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDGLD-APCPLGEDGLP 644
Cdd:NF038329  264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDgLPGKDGKDGQP 322
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 384-609 8.27e-21

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: 95.74  E-value: 8.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 384 GQVGPPGQPGDKGERGAAGEQGPDGPKGSKGEPGKGEMVDYNGNINEALQEirtlALMGPPGLPGQIGPPGAPGIPGQKG 463
Cdd:NF038329  123 GPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ----GPAGKDGEAGAKGPAGEKGPQGPRG 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 464 EIGLPGPPGHDGEKGPRGKPGDMGPPGPQGPPGKDGPPGvKGENGHPGSPGEKGEKGETGQAGSPGLQGVPGPKGEAGLD 543
Cdd:NF038329  199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGP-DGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKD 277

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1587062743 544 GAKGEKGFQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDK 609
Cdd:NF038329  278 GERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 319-593 1.07e-19

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: 92.28  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 319 GMKGEPGIPGTKGEKGAEGSPGLPGLLGQKGEKGDAGnsigggrgepgppgLPGPPGPKGEAGVDGQVGPPGQPGDKGER 398
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPG--------------PQGERGEKGPAGPQGEAGPQGPAGKDGEA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 399 GAAGEQGPDGPKGSKGEPGKGEMVDYNGninealqeirtlaLMGPPGLPGQIGPPGAPGIPG--QKGEIGLPGPPGHDGE 476
Cdd:NF038329  183 GAKGPAGEKGPQGPRGETGPAGEQGPAG-------------PAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGP 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 477 KGPRgkpgdmgppgpqgppgkdgppgvkGENGHPGSPGEKGEKGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQGEKG 556
Cdd:NF038329  250 QGPD------------------------GPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1587062743 557 DRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGP 593
Cdd:NF038329  306 QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAP 342
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 166-418 9.81e-09

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: 57.99  E-value: 9.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 166 GFPGFPGPIGLDGKPGHPGPKGDMGLTGPPGQPGPQGQKGEKGQCGEyphrllpllnsvrlapppvikrrtfQGEQsqas 245
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP-------------------------AGPQ---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 246 iqgppgppGPPGPSGPLGHPGLPGPMGPPGLPGPPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGAPGIAVAGMKGEPG 325
Cdd:NF038329  168 --------GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 326 IPGTKGEKGAEGSPGLPGLLGQKGEKGDAGnsigggrgepgppglpgppgPKGEAGVDGQVGPPGQPGDKGERGAAGEQG 405
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAG--------------------PDGPDGKDGERGPVGPAGKDGQNGKDGLPG 299

                         250
                  ....*....|...
gi 1587062743 406 PDGPKGSKGEPGK 418
Cdd:NF038329  300 KDGKDGQNGKDGL 312
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 136-418 1.15e-08

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: 57.61  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 136 KGQPGEKGSPGDAGLSiiGPRGPPGQPGTRGFPGFPGPIGLDGKPGHPGPKGDMGLTGPPGQPGPQGQKGEKGQCGEYPH 215
Cdd:NF038329  119 KGEPGPAGPAGPAGEQ--GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 216 RllpllnsvrlapppvikrrtfqGEQSQASIQGPPGPPGPPGPSGPLGHPGLPGPMGPPGLPGPPGpkgdpgiQGYHGRK 295
Cdd:NF038329  197 R----------------------GETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD-------PGPTGED 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 296 GERGMPGMPGKHGAKGApgiavagmKGEPGIPGTKGEKGAEGSPGLPGLLGQKGEKGDAGnsigggrgepgppglpgppg 375
Cdd:NF038329  248 GPQGPDGPAGKDGPRGD--------RGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPG-------------------- 299

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1587062743 376 pkgEAGVDGQVGPPGQPGDKGERGAAGEQGPDGPKGSKGEPGK 418
Cdd:NF038329  300 ---KDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 532-588 4.78e-06

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: 44.02  E-value: 4.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1587062743 532 GVPGPKGEAGLDGAKGEKGFQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDP 588
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 523-578 4.78e-06

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: 44.02  E-value: 4.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1587062743 523 GQAGSPGLQGVPGPKGEAGLDGAKGEKGFQGEKGDRGPLGLPGTPGPIGVPGPAGP 578
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 553-607 1.85e-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: 1.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1587062743 553 GEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPG 607
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 529-583 2.59e-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: 42.10  E-value: 2.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1587062743 529 GLQGVPGPKGEAGLDGAKGEKGFQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERG 583
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 574-628 3.27e-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: 3.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1587062743 574 GPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 628
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 559-613 8.92e-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: 40.55  E-value: 8.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1587062743 559 GPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRG 613
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 508-564 1.56e-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: 39.78  E-value: 1.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1587062743 508 GHPGSPGEKGEKGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQGEKGDRGPLGLP 564
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 547-601 7.11e-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: 37.86  E-value: 7.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1587062743 547 GEKGFQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPG 601
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 583-631 1.61e-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: 1.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1587062743 583 GSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDG 631
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 505-558 2.10e-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: 36.70  E-value: 2.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1587062743 505 GENGHPGSPGEKGEKGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQGEKGDR 558
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 511-642 2.52e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.72  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 511 GSPGEKGEKGETGQAGSPGLQGVPGPKGEAGLDGAKGEKGFQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGM 590
Cdd:PHA03169   82 GEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQ 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1587062743 591 TGPTGAAGLPGLHGPPGDKGNR-----GHRGFKGEKGEPGLPGLDGLDAPCPLGEDG 642
Cdd:PHA03169  162 QPSSFLQPSHEDSPEEPEPPTSepepdSPGPPQSETPTSSPPPQSPPDEPGEPQSPT 218
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 296-355 7.64e-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: 35.16  E-value: 7.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1587062743 296 GERGMPGMPGKHGAKGAPGIAvagmkGEPGIPGTKGEKGAEGSPGLPGLLGQKGEKGDAG 355
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPP-----GPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
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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