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Conserved domains on  [gi|568905688|ref|XP_006495712|]
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collagen alpha-1(IX) chain isoform X1 [Mus musculus]

Protein Classification

LamG domain-containing protein( domain architecture ID 10641961)

LamG (Laminin G) domain-containing protein may serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules

PubMed:  31092689

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 1.31e-58

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 191.03  E-value: 1.31e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688    50 GQDDLPGFDLISqfqiekaaSRRTIQRVVGSTALQVAYKLGSNVDFRIPTRHLYPSGLPEEYSFLTTFRMTGStleKHWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPK---SRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688   130 IWQIQDSAGREQVGVKINGQTKSVAFSYKGLDGSLQTAAFLNLPsLFDSRWHKLMIGVERTSATLFIDCIRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP-LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 568905688   210 GQ--IDADGFAVLGKLVDNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GQppIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-350 8.99e-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: 42.87  E-value: 8.99e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568905688  319 PGTPGADGLTGPDGSPGSVGPRGQKGEPGVPG 350
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG 40
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 299-451 1.31e-05

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: 47.21  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688 299 GPPGPPGPPGDPGKPGAPGKPGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppGTTGLPGELGRV 378
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA--------------GEKGPQGPRGET 200

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568905688 379 GPIGDPGKRGPPGPPGPPGPsgtigfhDGDPLCPNSCPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKVRKG 451
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGP-------AGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 1.31e-58

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 191.03  E-value: 1.31e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688    50 GQDDLPGFDLISqfqiekaaSRRTIQRVVGSTALQVAYKLGSNVDFRIPTRHLYPSGLPEEYSFLTTFRMTGStleKHWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPK---SRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688   130 IWQIQDSAGREQVGVKINGQTKSVAFSYKGLDGSLQTAAFLNLPsLFDSRWHKLMIGVERTSATLFIDCIRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP-LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 568905688   210 GQ--IDADGFAVLGKLVDNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GQppIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-350 8.99e-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: 42.87  E-value: 8.99e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568905688  319 PGTPGADGLTGPDGSPGSVGPRGQKGEPGVPG 350
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG 40
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 299-451 1.31e-05

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: 47.21  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688 299 GPPGPPGPPGDPGKPGAPGKPGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppGTTGLPGELGRV 378
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA--------------GEKGPQGPRGET 200

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568905688 379 GPIGDPGKRGPPGPPGPPGPsgtigfhDGDPLCPNSCPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKVRKG 451
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGP-------AGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 319-445 1.74e-04

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: 43.74  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688 319 PGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppgttglpgelGRVGPigdpgkrgppgpPGPPGP 398
Cdd:NF038329 241 PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD-----------------------GKDGE------------RGPVGP 285

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568905688 399 SGTIGFHDGDPLCPNSCPPGRSGYPGLPGMRGHKGAKGEIGEPGRQG 445
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 418-451 5.92e-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: 5.92e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568905688  418 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKVRKG 451
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG 34
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 302-451 2.28e-03

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 40.27  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688 302 GPPGPPGDPGKPGAPGKPGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRGFPGRGIPGPPGPPGTTGLPGELGRVGPi 381
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP- 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688 382 gdpgkrgppgppgppgpsgtigfhDGDPlcPNSCPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKVRKG 451
Cdd:NF038329 253 ------------------------DGPA--GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-244 1.31e-58

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 191.03  E-value: 1.31e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688    50 GQDDLPGFDLISqfqiekaaSRRTIQRVVGSTALQVAYKLGSNVDFRIPTRHLYPSGLPEEYSFLTTFRMTGStleKHWN 129
Cdd:smart00210   1 GQDLLQVFDLPS--------LSFAIRQVVGPEPGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPK---SRGV 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688   130 IWQIQDSAGREQVGVKINGQTKSVAFSYKGLDGSLQTAAFLNLPsLFDSRWHKLMIGVERTSATLFIDCIRIESLPIKPR 209
Cdd:smart00210  70 LFAIYDAQNVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRNLP-LADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRP 148

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 568905688   210 GQ--IDADGFAVLGKLVDNpQVSVPFELQWMLIHCDP 244
Cdd:smart00210 149 GQppIDTDGIEVRGAQAAD-RKPFQGDLQQLKIVCDP 184
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 319-350 8.99e-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: 42.87  E-value: 8.99e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568905688  319 PGTPGADGLTGPDGSPGSVGPRGQKGEPGVPG 350
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG 40
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 299-451 1.31e-05

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: 47.21  E-value: 1.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688 299 GPPGPPGPPGDPGKPGAPGKPGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppGTTGLPGELGRV 378
Cdd:NF038329 135 GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPA--------------GEKGPQGPRGET 200

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568905688 379 GPIGDPGKRGPPGPPGPPGPsgtigfhDGDPLCPNSCPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKVRKG 451
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGP-------AGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG 266
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 319-445 1.74e-04

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: 43.74  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688 319 PGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRgfpgrgipgppgppgttglpgelGRVGPigdpgkrgppgpPGPPGP 398
Cdd:NF038329 241 PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPD-----------------------GKDGE------------RGPVGP 285

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 568905688 399 SGTIGFHDGDPLCPNSCPPGRSGYPGLPGMRGHKGAKGEIGEPGRQG 445
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDG 332
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 418-451 5.92e-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: 5.92e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 568905688  418 GRSGYPGLPGMRGHKGAKGEIGEPGRQGHKVRKG 451
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPG 34
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 302-451 2.28e-03

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 40.27  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688 302 GPPGPPGDPGKPGAPGKPGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRGFPGRGIPGPPGPPGTTGLPGELGRVGPi 381
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGP- 252

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688 382 gdpgkrgppgppgppgpsgtigfhDGDPlcPNSCPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKVRKG 451
Cdd:NF038329 253 ------------------------DGPA--GKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDG 296
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 320-441 2.95e-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: 35.93  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568905688  320 GTPGADGLTGPDGSPGSVGPRGQKGEPGVPGsrgfpgrgipgppgppgttglpgelgrvgpigdpgkrgppgppgppgps 399
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPG------------------------------------------------- 31

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568905688  400 gtigfhdgdplcpnscPPGRSGYPGLPGMRGHKGAKGEIGEP 441
Cdd:pfam01391  32 ----------------EPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 416-445 3.96e-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: 35.55  E-value: 3.96e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 568905688  416 PPGRSGYPGLPGMRGHKGAKGEIGEPGRQG 445
Cdd:pfam01391  14 PPGPPGPPGPPGPPGPPGEPGPPGPPGPPG 43
 
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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