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Conserved domains on  [gi|1370456365|ref|XP_024303583|]
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collagen alpha-1(XIII) chain isoform X5 [Homo sapiens]

Protein Classification

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 ...
 301-559 1.38e-18

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: 89.19  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 301 QGYHGRKGERGMPGMPGKHGAKGAPGiaVAGMKGEPGIPGTKGDPGAEGKPGPPGLLGKRGQRGEKGAEGSPGLPGLLGQ 380
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAG--PAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 381 KGEKGDAGNSIGGGRGEPGPPGLPGPPGPKGEAGVDGQVGPPGQPGDKGERGAAGEQGPDGPKGSKGEPGKGemvdyngn 460
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD-------- 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 461 inealqeirtlalmGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPGHDGEKGprgkpgdmgppgpqgppgKDGPPGVKGEN 540
Cdd:NF038329  272 --------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------------KDGLPGKDGKD 319

                         250
                  ....*....|....*....
gi 1370456365 541 GHPGSPGEKGEKGETGQAG 559
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPG 338
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 642-690 1.76e-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: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370456365 642 GSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDG 690
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 301-559 1.38e-18

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: 89.19  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 301 QGYHGRKGERGMPGMPGKHGAKGAPGiaVAGMKGEPGIPGTKGDPGAEGKPGPPGLLGKRGQRGEKGAEGSPGLPGLLGQ 380
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAG--PAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 381 KGEKGDAGNSIGGGRGEPGPPGLPGPPGPKGEAGVDGQVGPPGQPGDKGERGAAGEQGPDGPKGSKGEPGKGemvdyngn 460
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD-------- 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 461 inealqeirtlalmGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPGHDGEKGprgkpgdmgppgpqgppgKDGPPGVKGEN 540
Cdd:NF038329  272 --------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------------KDGLPGKDGKD 319

                         250
                  ....*....|....*....
gi 1370456365 541 GHPGSPGEKGEKGETGQAG 559
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 426-703 1.45e-17

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: 85.73  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 426 GDKGERGAAGEQGPDGPKGSKGEPGkgemvdyngninealqeirTLALMGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPG 505
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRG-------------------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 506 HDGEKGPrgkpgdmgppgpqgppgkdgppgvKGENGHPGSPGEKGEKGETGQAGSPVPGLPGPEGPPGPPGLQGVPGPKG 585
Cdd:NF038329  178 KDGEAGA------------------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 586 EAGLDGAKGEKGFQGEKGDRGPLGLPGASGLDgrpgppgtpgpiGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPP 665
Cdd:NF038329  234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR------------GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370456365 666 GDKGNRGHRGFKGEKGEPGLPGLDGLdaPCPLGEDGLP 703
Cdd:NF038329  302 GKDGQNGKDGLPGKDGKDGQPGKDGL--PGKDGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 178-451 9.53e-12

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: 67.62  E-value: 9.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 178 GFPGFPGPIGLDGKPGHPGPKGDMGLTGPPGQPGPQGQKGEKGQCGEyphrllpllnsvrlapppvikrrtfQGEQsqas 257
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP-------------------------AGPQ---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 258 iqgppgppGPPGPSGPLGHPGLPGPMGPPGLPGPPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGAPGIAVAGMKGEPG 337
Cdd:NF038329  168 --------GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 338 IPGTKGDPGAEGKPGPPGLLGKRGQRGEKGAEGSPGLPGLLGQKGEKGDAGNSigggrgepgppglpGPPGPKGEAGVDG 417
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN--------------GKDGLPGKDGKDG 305

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370456365 418 QVGPPGQPGDKGERGAAGEQGPDGPKGSKGEPGK 451
Cdd:NF038329  306 QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 334-388 5.45e-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: 38.63  E-value: 5.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370456365 334 GEPGIPGTKGDPGAEGKPGPPGLLGKRGQRGEKGAEGSPGLPGLLGQKGEKGDAG 388
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 642-690 1.76e-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: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370456365 642 GSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDG 690
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 301-559 1.38e-18

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: 89.19  E-value: 1.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 301 QGYHGRKGERGMPGMPGKHGAKGAPGiaVAGMKGEPGIPGTKGDPGAEGKPGPPGLLGKRGQRGEKGAEGSPGLPGLLGQ 380
Cdd:NF038329  122 PGPAGPAGPAGEQGPRGDRGETGPAG--PAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 381 KGEKGDAGNSIGGGRGEPGPPGLPGPPGPKGEAGVDGQVGPPGQPGDKGERGAAGEQGPDGPKGSKGEPGKGemvdyngn 460
Cdd:NF038329  200 TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD-------- 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 461 inealqeirtlalmGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPGHDGEKGprgkpgdmgppgpqgppgKDGPPGVKGEN 540
Cdd:NF038329  272 --------------GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG------------------KDGLPGKDGKD 319

                         250
                  ....*....|....*....
gi 1370456365 541 GHPGSPGEKGEKGETGQAG 559
Cdd:NF038329  320 GQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 426-703 1.45e-17

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: 85.73  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 426 GDKGERGAAGEQGPDGPKGSKGEPGkgemvdyngninealqeirTLALMGPPGLPGQIGPPGAPGIPGQKGEIGLPGPPG 505
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRG-------------------ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 506 HDGEKGPrgkpgdmgppgpqgppgkdgppgvKGENGHPGSPGEKGEKGETGQAGSPVPGLPGPEGPPGPPGLQGVPGPKG 585
Cdd:NF038329  178 KDGEAGA------------------------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 586 EAGLDGAKGEKGFQGEKGDRGPLGLPGASGLDgrpgppgtpgpiGVPGPAGPKGERGSKGDPGMTGPTGAAGLPGLHGPP 665
Cdd:NF038329  234 QQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDR------------GEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370456365 666 GDKGNRGHRGFKGEKGEPGLPGLDGLdaPCPLGEDGLP 703
Cdd:NF038329  302 GKDGQNGKDGLPGKDGKDGQPGKDGL--PGKDGKDGQP 337
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 178-451 9.53e-12

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: 67.62  E-value: 9.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 178 GFPGFPGPIGLDGKPGHPGPKGDMGLTGPPGQPGPQGQKGEKGQCGEyphrllpllnsvrlapppvikrrtfQGEQsqas 257
Cdd:NF038329  117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGP-------------------------AGPQ---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 258 iqgppgppGPPGPSGPLGHPGLPGPMGPPGLPGPPGPKGDPGIQGYHGRKGERGMPGMPGKHGAKGAPGIAVAGMKGEPG 337
Cdd:NF038329  168 --------GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370456365 338 IPGTKGDPGAEGKPGPPGLLGKRGQRGEKGAEGSPGLPGLLGQKGEKGDAGNSigggrgepgppglpGPPGPKGEAGVDG 417
Cdd:NF038329  240 DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQN--------------GKDGLPGKDGKDG 305

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370456365 418 QVGPPGQPGDKGERGAAGEQGPDGPKGSKGEPGK 451
Cdd:NF038329  306 QNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 334-388 5.45e-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: 38.63  E-value: 5.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370456365 334 GEPGIPGTKGDPGAEGKPGPPGLLGKRGQRGEKGAEGSPGLPGLLGQKGEKGDAG 388
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 642-690 1.76e-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: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370456365 642 GSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPGLDG 690
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 639-687 3.37e-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: 36.32  E-value: 3.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370456365 639 GERGSKGDPGMTGPTGAAGLPGLHGPPGDKGNRGHRGFKGEKGEPGLPG 687
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 311-375 7.49e-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: 7.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370456365 311 GMPGMPGKHGAKGAPGiavagmkgEPGIPGTKGDPGAEGKPGPPGLLGKRGQRGEKGAEGSPGLP 375
Cdd:pfam01391   1 GPPGPPGPPGPPGPPG--------PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 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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