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Conserved domains on  [gi|17552372|ref|NP_498729|]
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Putative cuticle collagen 90 [Caenorhabditis elegans]

Protein Classification

cuticular collagen family protein( domain architecture ID 18387949)

cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Gene Ontology:  GO:0042302|GO:0005581
PubMed:  1916105|21421911

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 ...
 111-270 1.67e-24

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: 102.29  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  111 GVVGDLGRSGASGISLAAVHHIPGGcincPAGPAGPPGQQGPVGPQGFPGVVGTCGPS--------GDDGQPGPAGPLGD 182
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRG----ETGPAGEQGPAGPAGPDGEAGPAGEDGPAgpagdgqqGPDGDPGPTGEDGP 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  183 KGAQGPKGFDGADGPDGMPGTAYFPGAVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRDaypGQPGKAG 262
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---GQPGKDG 326


                 ....*...
gi 17552372  263 EPGAVGKD 270
Cdd:NF038329 327 LPGKDGKD 334
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 3-55 1.31e-13

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


:

Pssm-ID: 198156  Cd Length: 53  Bit Score: 64.03  E-value: 1.31e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17552372      3 TIGYIGASICLLGVLSSLFSISHIVRDINSLRDEVEGRVDEFKVLADDTWQRL 55
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 111-270 1.67e-24

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: 102.29  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  111 GVVGDLGRSGASGISLAAVHHIPGGcincPAGPAGPPGQQGPVGPQGFPGVVGTCGPS--------GDDGQPGPAGPLGD 182
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRG----ETGPAGEQGPAGPAGPDGEAGPAGEDGPAgpagdgqqGPDGDPGPTGEDGP 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  183 KGAQGPKGFDGADGPDGMPGTAYFPGAVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRDaypGQPGKAG 262
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---GQPGKDG 326


                 ....*...
gi 17552372  263 EPGAVGKD 270
Cdd:NF038329 327 LPGKDGKD 334
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 129-297 2.89e-24

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: 101.91  E-value: 2.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  129 VHHIPGGCINCPAGPAGPPGQQGPVGPQGFPGVVGTCGPSGDDGQPGPAGPLGDKGAQGPKGFDGADGPDGMPGTAYFPG 208
Cdd:NF038329 110 LQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  209 AVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRdaypGQPGKAGEPGAVGKDANYCPC-PARRDSKTESV 287
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDgPAGKDGPRGDR 265

                        170
                 ....*....|
gi 17552372  288 HEPPAASQNG 297
Cdd:NF038329 266 GEAGPDGPDG 275
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 100-270 3.77e-24

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: 101.52  E-value: 3.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  100 PPGLPGKRGDEGVVGDLGRSGASGISLAAVHHIPGGcincPAGPAGPPGQQGPVGPQGFPGVVGTCGPSGDDGQPGPAGP 179
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG----PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  180 LGDKGAQGPKGFDGADGPDGMPGTAYfPGAVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRDAYPGQPG 259
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                        170
                 ....*....|.
gi 17552372  260 KAGEPGAVGKD 270
Cdd:NF038329 285 PAGKDGQNGKD 295
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 3-55 1.31e-13

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 64.03  E-value: 1.31e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17552372      3 TIGYIGASICLLGVLSSLFSISHIVRDINSLRDEVEGRVDEFKVLADDTWQRL 55
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-55 1.04e-12

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 61.71  E-value: 1.04e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17552372     6 YIGASICLLGVLSSLFSISHIVRDINSLRDEVEGRVDEFKVLADDTWQRL 55
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 211-267 3.07e-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: 43.64  E-value: 3.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17552372   211 GQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRDAYPGQPGKAGEPGAV 267
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 140-295 2.00e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  140 PAGPAGPPGQQGPVGPQGFPGVVGTCGPSGDDGQPGPAGPLGDKGAQGPKGFDGADGPDGMPGTAYFPGAVGQPGEPGWL 219
Cdd:PRK07764 621 PAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQ 700

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17552372  220 GQPGLPGK-HGEPGQDGEEGPKGAPGTPGSNGRDAYPGQP--GKAGEPGAVGKDANYCPCPARRDSKTESVHEPPAASQ 295
Cdd:PRK07764 701 PAPAPAATpPAGQADDPAAQPPQAAQGASAPSPAADDPVPlpPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 111-270 1.67e-24

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: 102.29  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  111 GVVGDLGRSGASGISLAAVHHIPGGcincPAGPAGPPGQQGPVGPQGFPGVVGTCGPS--------GDDGQPGPAGPLGD 182
Cdd:NF038329 174 GPAGKDGEAGAKGPAGEKGPQGPRG----ETGPAGEQGPAGPAGPDGEAGPAGEDGPAgpagdgqqGPDGDPGPTGEDGP 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  183 KGAQGPKGFDGADGPDGMPGTAYFPGAVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRDaypGQPGKAG 262
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD---GQPGKDG 326


                 ....*...
gi 17552372  263 EPGAVGKD 270
Cdd:NF038329 327 LPGKDGKD 334
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 129-297 2.89e-24

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: 101.91  E-value: 2.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  129 VHHIPGGCINCPAGPAGPPGQQGPVGPQGFPGVVGTCGPSGDDGQPGPAGPLGDKGAQGPKGFDGADGPDGMPGTAYFPG 208
Cdd:NF038329 110 LQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  209 AVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRdaypGQPGKAGEPGAVGKDANYCPC-PARRDSKTESV 287
Cdd:NF038329 190 EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGPQGPDgPAGKDGPRGDR 265

                        170
                 ....*....|
gi 17552372  288 HEPPAASQNG 297
Cdd:NF038329 266 GEAGPDGPDG 275
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 100-270 3.77e-24

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: 101.52  E-value: 3.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  100 PPGLPGKRGDEGVVGDLGRSGASGISLAAVHHIPGGcincPAGPAGPPGQQGPVGPQGFPGVVGTCGPSGDDGQPGPAGP 179
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAG----PQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  180 LGDKGAQGPKGFDGADGPDGMPGTAYfPGAVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRDAYPGQPG 259
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVG 284

                        170
                 ....*....|.
gi 17552372  260 KAGEPGAVGKD 270
Cdd:NF038329 285 PAGKDGQNGKD 295
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 3-55 1.31e-13

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 64.03  E-value: 1.31e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17552372      3 TIGYIGASICLLGVLSSLFSISHIVRDINSLRDEVEGRVDEFKVLADDTWQRL 55
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-55 1.04e-12

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 61.71  E-value: 1.04e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17552372     6 YIGASICLLGVLSSLFSISHIVRDINSLRDEVEGRVDEFKVLADDTWQRL 55
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 211-267 3.07e-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: 43.64  E-value: 3.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17552372   211 GQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRDAYPGQPGKAGEPGAV 267
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 142-197 7.51e-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: 42.48  E-value: 7.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17552372   142 GPAGPPGQQGPVGPQGFPGVVGTCGPSGDDGQPGPAGPLGDKGAQGPKGFDGADGP 197
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 148-202 4.16e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 4.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17552372   148 GQQGPVGPQGFPGVVGTCGPSGDDGQPGPAGPLGDKGAQGPKGFDGADGPDGMPG 202
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 175-231 4.20e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.55  E-value: 4.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17552372   175 GPAGPLGDKGAQGPKGFDGADGPDGMPGTAYFPGAVGQPGEPGWLGQPGLPGKHGEP 231
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 140-190 4.82e-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: 40.17  E-value: 4.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17552372   140 PAGPAGPPGQQGPVGPQGFPGVVGTCGPSGDDGQPGPAGPLGDKGAQGPKG 190
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 196-250 1.63e-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: 1.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17552372   196 GPDGMPGTAYFPGAVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNG 250
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 207-258 1.87e-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: 38.63  E-value: 1.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17552372   207 PGAVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRDAYPGQP 258
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 140-295 2.00e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.05  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  140 PAGPAGPPGQQGPVGPQGFPGVVGTCGPSGDDGQPGPAGPLGDKGAQGPKGFDGADGPDGMPGTAYFPGAVGQPGEPGWL 219
Cdd:PRK07764 621 PAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQ 700

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17552372  220 GQPGLPGK-HGEPGQDGEEGPKGAPGTPGSNGRDAYPGQP--GKAGEPGAVGKDANYCPCPARRDSKTESVHEPPAASQ 295
Cdd:PRK07764 701 PAPAPAATpPAGQADDPAAQPPQAAQGASAPSPAADDPVPlpPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
PHA03169 PHA03169
hypothetical protein; Provisional
 142-250 3.16e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.88  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  142 GPAGPPGQQGPVGPQGFPGVvgtcGPSGDDGQPGPAGPLGDKGAQGPKGFDGADGPDGMPGTAYFPGAVGQPGEPGWLGQ 221
Cdd:PHA03169 127 SPESPASHSPPPSPPSHPGP----HEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSP 202

                         90       100
                 ....*....|....*....|....*....
gi 17552372  222 PGLPGKHgEPGQDGEEGPKGAPGTPGSNG 250
Cdd:PHA03169 203 PPQSPPD-EPGEPQSPTPQQAPSPNTQQA 230
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 112-298 3.68e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  112 VVGDLGRSGASGISLAAVHHIPGGCINCPAGPAGPPGQQGPVGPQGFPgvvgtcGPSGDDGQPGPAGPLGDKGAQGPKGF 191
Cdd:PRK07764 587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAA------APAEASAAPAPGVAAPEHHPKHVAVP 660

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  192 DGADGPDGMPGTAYFPGAVGQPGEPGWLGQPGLPGkhGEPGQDGEEGPKGAPGTPGSNGRDAYPGQPGKAGEPGAVGKDA 271
Cdd:PRK07764 661 DASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAG--AAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738

                        170       180
                 ....*....|....*....|....*..
gi 17552372  272 nyCPCPARRDSKTESVHEPPAASQNGG 298
Cdd:PRK07764 739 --VPLPPEPDDPPDPAGAPAQPPPPPA 763
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 140-188 4.20e-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: 4.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17552372   140 PAGPAGPPGQQGPVGPQGFPGVVGTCGPSGDDGQPGPAGPLGDKGAQGP 188
Cdd:pfam01391   8 PPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 116-293 9.43e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 9.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  116 LGRSGASGISLAAVHHIPGGC--INCPAGPAGPPGQ-QGPVGPQGFPGVVGTCGPsgdDGQPGPAGPLGDKGAQGPKGFD 192
Cdd:PRK07764 561 FASPGNAEVLVTALAEELGGDwqVEAVVGPAPGAAGgEGPPAPASSGPPEEAARP---AAPAAPAAPAAPAPAGAAAAPA 637

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  193 GADGPDGMPGTAYFPGAVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGAPGTPGSNGRDAYPGQPGKAGEPGAVGKDAN 272
Cdd:PRK07764 638 EASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDP 717

                        170       180
                 ....*....|....*....|.
gi 17552372  273 YCPCPARRDSKTESVHEPPAA 293
Cdd:PRK07764 718 AAQPPQAAQGASAPSPAADDP 738
PHA03169 PHA03169
hypothetical protein; Provisional
 156-270 1.94e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.57  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  156 QGFPGVVGTCGPSGDDGQPGPAGPLGDKGAQGPKGFDGAD------GPDGMPGTAYFPGAVGQPGEPGWLGQPGLPGKHG 229
Cdd:PHA03169  89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPespashSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 17552372  230 EPGQDGEEGPKGAPGTPGSNGRDAYPGQPGKAGEPGAVGKD 270
Cdd:PHA03169 169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD 209
Med15 pfam09606
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ...
 126-268 1.94e-03

ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.


Pssm-ID: 312941 [Multi-domain]  Cd Length: 732  Bit Score: 39.61  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372   126 LAAVHHIPGGCINCPAGPAGPPGQQ-GPVG-----------PQGFPGVVGTCGPSGDDGQPGPAGplgdkGAQGPKGFDG 193
Cdd:pfam09606  89 LAGQGTRPQMMGPMGPGPGGPMGQQmGGPGtasnllaslgrPQMPMGGAGFPSQMSRVGRMQPGG-----QAGGMMQPSS 163

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552372   194 ADGPDGMPGTAYFPGAVGQPGEPGWLGQPGLPGKHGEPGQDGEEGPKGaPGTPGSNGRDAYPGQPGKAGEPGAVG 268
Cdd:pfam09606 164 GQPGSGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPG-PADAGAQMGQQAQANGGMNPQQMGGA 237
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 118-232 2.24e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 39.66  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  118 RSGASGISLAAVHHIPGGCINCpAGPAGPPGQQGPVGPQGFPGVVGTCGPSGDDG---QPGPAGPLGDKGAQGPKGFDGA 194
Cdd:PRK14959 372 RPSGGGASAPSGSAAEGPASGG-AATIPTPGTQGPQGTAPAAGMTPSSAAPATPApsaAPSPRVPWDDAPPAPPRSGIPP 450

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 17552372  195 DGPDGMPGTAYFPGA----VGQPGEPGWLGQPGLPGKHgEPG 232
Cdd:PRK14959 451 RPAPRMPEASPVPGApdsvASASDAPPTLGDPSDTAEH-TPS 491
dnaA PRK14086
chromosomal replication initiator protein DnaA;
140-278 8.29e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 37.88  E-value: 8.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552372  140 PAGPAGPPGQQGPVGPQGFPGvvgtcgpSGDDGQPGP-AGPLGDKGAQGPK-GFDGADGP----DGMPGTAYF--PGAVG 211
Cdd:PRK14086 128 DRPPGLPRQDQLPTARPAYPA-------YQQRPEPGAwPRAADDYGWQQQRlGFPPRAPYaspaSYAPEQERDrePYDAG 200

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552372  212 QPGEPGWLGQPGLPGKHGE-PGQDGEEGPKGAPGT-------PGSNGRDAYPGQPGKAGEPGAVGKDANYCPCPA 278
Cdd:PRK14086 201 RPEYDQRRRDYDHPRPDWDrPRRDRTDRPEPPPGAghvhrggPGPPERDDAPVVPIRPSAPGPLAAQPAPAPGPG 275
 
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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