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Conserved domains on  [gi|6680962|ref|NP_031757|]
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collagen alpha-1(XIII) chain isoform 1 [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 ...
 500-721 6.03e-25

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: 108.45  E-value: 6.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   500 DGDKGPRGKPGDMGPAGPQGPPGKDGPpgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIG 579
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGE---TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   580 LPGFTGEKGEAGEKGDPGAEVPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLPGTPGPIGVPG 659
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6680962   660 PAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLD 721
Cdd:NF038329 273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 357-600 6.47e-20

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: 93.05  E-value: 6.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   357 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 436
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   437 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 516
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   517 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 596
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343


                 ....
gi 6680962   597 GAEV 600
Cdd:NF038329 344 TPEV 347
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 135-381 1.61e-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: 60.69  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   135 GAIGMPGRVGIKGQPGEKGAPGDAGmsivgprgppgQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQK 214
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRG-----------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   215 GEKGQCGEYPHREYPGGMLAALRSNPIMSLKLLPLLNSVRLAPPPVIKRRTFQGEQSQTGIQGPPGPPGPPGPSGPLGHP 294
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   295 GLPGPigppglpgppgpkgdpgiQGYHGRKGERGMPGMPGKHGAKGVPGIA-VAGMKGEPGTPGTKGEKGAAGSPGLLGQ 373
Cdd:NF038329 266 GEAGP------------------DGPDGKDGERGPVGPAGKDGQNGKDGLPgKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327


                 ....*...
gi 6680962   374 KGEKGDAG 381
Cdd:NF038329 328 PGKDGKDG 335
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 500-721 6.03e-25

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: 108.45  E-value: 6.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   500 DGDKGPRGKPGDMGPAGPQGPPGKDGPpgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIG 579
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGE---TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   580 LPGFTGEKGEAGEKGDPGAEVPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLPGTPGPIGVPG 659
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6680962   660 PAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLD 721
Cdd:NF038329 273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 492-732 7.65e-25

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: 108.07  E-value: 7.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   492 GLPGPPGHDGDKGPRGKPGDMGPAGPQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGA 571
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   572 TGLPGPIGLPGFTGEKGEAGEKGDpgaevpgppgpegppgppglqgfpgpkgeaGLEGSKGEKGSQGEKGDRGPLGLPGT 651
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAGD------------------------------GQQGPDGDPGPTGEDGPQGPDGPAGK 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   652 PGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLdaPCPLGEDGL 731
Cdd:NF038329 259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL--PGKDGKDGQ 336


                 .
gi 6680962   732 P 732
Cdd:NF038329 337 P 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 357-600 6.47e-20

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: 93.05  E-value: 6.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   357 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 436
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   437 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 516
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   517 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 596
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343


                 ....
gi 6680962   597 GAEV 600
Cdd:NF038329 344 TPEV 347
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 135-381 1.61e-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: 60.69  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   135 GAIGMPGRVGIKGQPGEKGAPGDAGmsivgprgppgQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQK 214
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRG-----------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   215 GEKGQCGEYPHREYPGGMLAALRSNPIMSLKLLPLLNSVRLAPPPVIKRRTFQGEQSQTGIQGPPGPPGPPGPSGPLGHP 294
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   295 GLPGPigppglpgppgpkgdpgiQGYHGRKGERGMPGMPGKHGAKGVPGIA-VAGMKGEPGTPGTKGEKGAAGSPGLLGQ 373
Cdd:NF038329 266 GEAGP------------------DGPDGKDGERGPVGPAGKDGQNGKDGLPgKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327


                 ....*...
gi 6680962   374 KGEKGDAG 381
Cdd:NF038329 328 PGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 646-723 2.49e-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: 56.84  E-value: 2.49e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6680962   646 LGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAP 723
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 194-444 3.86e-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: 56.45  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   194 GPKGEMGLVGPRGQPGPQGQKGEKGQCGEyphreypggmlaalrsnpimslkllpllnSVRLAPPPVIKRRTFQGEQSQT 273
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGP-----------------------------AGPAGPPGPQGERGEKGPAGPQ 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   274 GIQGPPGPPGPPGPSGPLGHPGLPGPIGPPGLPGPPGPkgdpgiQGYHGRKGERGMPGMPGKHGAKGVPGIAVAGMKGEP 353
Cdd:NF038329 168 GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   354 GTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPS 433
Cdd:NF038329 242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPD--GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                        250
                 ....*....|.
gi 6680962   434 GPKGAKGEPGK 444
Cdd:NF038329 320 GQPGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 176-444 8.90e-06

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: 48.75  E-value: 8.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   176 GFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGEyphreypggmlaalrsnpimslkllpllnsvrl 255
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP--------------------------------- 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   256 apppvikrrtfQGEQSQTGIQGPPGPPGPPGPsgplghpglpgpigppglpgppgpKGDPGIQGYHGRKGERGMPGMPGK 335
Cdd:NF038329 164 -----------AGPQGEAGPQGPAGKDGEAGA------------------------KGPAGEKGPQGPRGETGPAGEQGP 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   336 HGAKGVPGIAVAGMKGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrGEPGPPGLPGPPGPKGEAGVDGQAGPP 415
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPA-----GKDGPRGDRGEAGPDGPDGKDGERGPV 283

                        250       260
                 ....*....|....*....|....*....
gi 6680962   416 GQQGDKGQPGAAGEQGPSGPKGAKGEPGK 444
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 531-582 1.58e-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: 42.87  E-value: 1.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6680962    531 GEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPG 582
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 134-222 1.04e-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: 42.20  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   134 KGAIGMPGRVGIKGQPGEKGAPGDAGMSIVGPRGPPGQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQ 213
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288


                 ....*....
gi 6680962   214 KGEKGQCGE 222
Cdd:NF038329 289 DGQNGKDGL 297
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 175-220 6.73e-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: 6.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 6680962    175 RGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQC 220
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 500-721 6.03e-25

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: 108.45  E-value: 6.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   500 DGDKGPRGKPGDMGPAGPQGPPGKDGPpgmKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIG 579
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGE---TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKG 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   580 LPGFTGEKGEAGEKGDPGAEVPGPPGPEGPPGPPGLQGFPGPKGEAGLEGSKGEKGSQGEKGDRGPLGLPGTPGPIGVPG 659
Cdd:NF038329 193 PQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDG 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6680962   660 PAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLD 721
Cdd:NF038329 273 PDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKD 334
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 492-732 7.65e-25

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: 108.07  E-value: 7.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   492 GLPGPPGHDGDKGPRGKPGDMGPAGPQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGA 571
Cdd:NF038329 129 GPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGP 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   572 TGLPGPIGLPGFTGEKGEAGEKGDpgaevpgppgpegppgppglqgfpgpkgeaGLEGSKGEKGSQGEKGDRGPLGLPGT 651
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAGD------------------------------GQQGPDGDPGPTGEDGPQGPDGPAGK 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   652 PGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLdaPCPLGEDGL 731
Cdd:NF038329 259 DGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL--PGKDGKDGQ 336


                 .
gi 6680962   732 P 732
Cdd:NF038329 337 P 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 357-600 6.47e-20

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: 93.05  E-value: 6.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   357 GTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPSGPK 436
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGET--GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQ 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   437 GAKGEPGKGEMVDYNGsinealqeirtLALMGPPGLPGQTGPPGPPGTPGQRGEIGLPGPPGHDGDKGPRGKPGDMGPAG 516
Cdd:NF038329 195 GPRGETGPAGEQGPAG-----------PAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   517 PQGPPGKDGPPGMKGEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEAGEKGDP 596
Cdd:NF038329 264 DRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPK 343


                 ....
gi 6680962   597 GAEV 600
Cdd:NF038329 344 TPEV 347
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 135-381 1.61e-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: 60.69  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   135 GAIGMPGRVGIKGQPGEKGAPGDAGmsivgprgppgQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQK 214
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRG-----------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAK 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   215 GEKGQCGEYPHREYPGGMLAALRSNPIMSLKLLPLLNSVRLAPPPVIKRRTFQGEQSQTGIQGPPGPPGPPGPSGPLGHP 294
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   295 GLPGPigppglpgppgpkgdpgiQGYHGRKGERGMPGMPGKHGAKGVPGIA-VAGMKGEPGTPGTKGEKGAAGSPGLLGQ 373
Cdd:NF038329 266 GEAGP------------------DGPDGKDGERGPVGPAGKDGQNGKDGLPgKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327


                 ....*...
gi 6680962   374 KGEKGDAG 381
Cdd:NF038329 328 PGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 646-723 2.49e-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: 56.84  E-value: 2.49e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6680962   646 LGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAP 723
Cdd:NF038329 113 LKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 194-444 3.86e-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: 56.45  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   194 GPKGEMGLVGPRGQPGPQGQKGEKGQCGEyphreypggmlaalrsnpimslkllpllnSVRLAPPPVIKRRTFQGEQSQT 273
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGP-----------------------------AGPAGPPGPQGERGEKGPAGPQ 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   274 GIQGPPGPPGPPGPSGPLGHPGLPGPIGPPGLPGPPGPkgdpgiQGYHGRKGERGMPGMPGKHGAKGVPGIAVAGMKGEP 353
Cdd:NF038329 168 GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE------QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDP 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   354 GTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigGGRGEPGPPGLPGPPGPKGEAGVDGQAGPPGQQGDKGQPGAAGEQGPS 433
Cdd:NF038329 242 GPTGEDGPQGPDGPAGKDGPRGDRGEAGPD--GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD 319

                        250
                 ....*....|.
gi 6680962   434 GPKGAKGEPGK 444
Cdd:NF038329 320 GQPGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 176-444 8.90e-06

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: 48.75  E-value: 8.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   176 GFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQCGEyphreypggmlaalrsnpimslkllpllnsvrl 255
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP--------------------------------- 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   256 apppvikrrtfQGEQSQTGIQGPPGPPGPPGPsgplghpglpgpigppglpgppgpKGDPGIQGYHGRKGERGMPGMPGK 335
Cdd:NF038329 164 -----------AGPQGEAGPQGPAGKDGEAGA------------------------KGPAGEKGPQGPRGETGPAGEQGP 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   336 HGAKGVPGIAVAGMKGEPGTPGTKGEKGAAGSPGLLGQKGEKGDAGNAigggrGEPGPPGLPGPPGPKGEAGVDGQAGPP 415
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPA-----GKDGPRGDRGEAGPDGPDGKDGERGPV 283

                        250       260
                 ....*....|....*....|....*....
gi 6680962   416 GQQGDKGQPGAAGEQGPSGPKGAKGEPGK 444
Cdd:NF038329 284 GPAGKDGQNGKDGLPGKDGKDGQNGKDGL 312
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 531-582 1.58e-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: 42.87  E-value: 1.58e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6680962    531 GEVGPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPG 582
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 534-590 1.82e-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: 1.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6680962    534 GPPGSPGEKGETGQAGPQGLDGPTGEKGEPGDEGRPGATGLPGPIGLPGFTGEKGEA 590
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 638-692 2.11e-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: 2.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6680962    638 GEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPG 692
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 644-700 4.27e-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: 4.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6680962    644 GPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGER 700
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 653-708 7.56e-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: 7.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6680962    653 GPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGP 708
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 650-706 7.71e-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: 7.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6680962    650 GTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSR 706
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 629-685 2.85e-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: 2.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6680962    629 GSKGEKGSQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDPGMTGPTGAAGLP 685
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 662-718 2.99e-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: 2.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6680962    662 GPKGERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAP 718
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 668-724 3.87e-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: 3.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6680962    668 GSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGERGKKGSRGPKGDKGDQGAPGLDAPC 724
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 134-222 1.04e-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: 42.20  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680962   134 KGAIGMPGRVGIKGQPGEKGAPGDAGMSIVGPRGPPGQPGTRGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQ 213
Cdd:NF038329 209 AGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGK 288


                 ....*....
gi 6680962   214 KGEKGQCGE 222
Cdd:NF038329 289 DGQNGKDGL 297
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 625-673 1.96e-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: 1.96e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 6680962    625 AGLEGSKGEKGSQGEKGDRGPLGLPGTPGPIGVPGPAGPKGERGSKGDP 673
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 175-220 6.73e-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: 6.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 6680962    175 RGFPGFPGPIGLDGRPGHPGPKGEMGLVGPRGQPGPQGQKGEKGQC 220
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
 
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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