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Conserved domains on  [gi|17538760|ref|NP_501867|]
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Nematode cuticle collagen N-terminal domain-containing protein [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
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
12-64 2.85e-16

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: 71.34  E-value: 2.85e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17538760     12 FVGYAALTFSTIAVLSVCITLPMMYNYIHHTRKVMHSDIVECKSEAQRLFSQV 64
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
94-271 6.61e-14

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: 71.47  E-value: 6.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   94 PGAQGPPGTPGSAGRPGKPGAPGLNGNPGRPPKEPCEPLTPPPCKPCPEGPPGPAGPPGPDGNKGPLGPPGPPGPEGPNG 173
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  174 EPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQPGAPGEPGQPGQPGQRGPAGEPGKDGSPGGQGEKGAS---------G 244
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDgpdgkdgerG 281
                        170       180
                 ....*....|....*....|....*..
gi 17538760  245 EPGQPGRDGQPGHPGQPGKDGRPGEKG 271
Cdd:NF038329 282 PVGPAGKDGQNGKDGLPGKDGKDGQNG 308
 
Name Accession Description Interval E-value
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
12-64 2.85e-16

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: 71.34  E-value: 2.85e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17538760     12 FVGYAALTFSTIAVLSVCITLPMMYNYIHHTRKVMHSDIVECKSEAQRLFSQV 64
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
94-271 6.61e-14

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: 71.47  E-value: 6.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   94 PGAQGPPGTPGSAGRPGKPGAPGLNGNPGRPPKEPCEPLTPPPCKPCPEGPPGPAGPPGPDGNKGPLGPPGPPGPEGPNG 173
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  174 EPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQPGAPGEPGQPGQPGQRGPAGEPGKDGSPGGQGEKGAS---------G 244
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDgpdgkdgerG 281
                        170       180
                 ....*....|....*....|....*..
gi 17538760  245 EPGQPGRDGQPGHPGQPGKDGRPGEKG 271
Cdd:NF038329 282 PVGPAGKDGQNGKDGLPGKDGKDGQNG 308
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
15-64 1.82e-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, 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: 63.63  E-value: 1.82e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17538760    15 YAALTFSTIAVLSVCITLPMMYNYIHHTRKVMHSDIVECKSEAQRLFSQV 64
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
94-271 7.24e-13

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: 68.39  E-value: 7.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   94 PGAQGPPGTPGSAGRPGKPGAPGLNGNPGRPPKEPCEPLTPPPCKPCPEGPPGPAGPPGPDGNKGPLGPPGPPGPEGPNG 173
Cdd:NF038329 152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  174 EPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQPGAPGEPGQPGQPGQRGPAGEPGKDGSPGGQGEKGASGEPGQPGRDG 253
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
                        170       180
                 ....*....|....*....|.
gi 17538760  254 QP---GHPGQPGKDGRPGEKG 271
Cdd:NF038329 312 LPgkdGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
93-268 4.73e-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: 65.70  E-value: 4.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   93 LPGAQGPPGTPGSAGRPGKPGAPGLNGNPGrPPKEPCEPLTPPPCKPCPEGPPGPAGPPGPDGNKGPLGPPGPPGPEGPN 172
Cdd:NF038329 160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAG-EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  173 GEPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQP----GAPGEPGQPGQPGQRGPAGEPGKDGSPGGQGEKGASGEPGQ 248
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPdgkdGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
                        170       180
                 ....*....|....*....|
gi 17538760  249 PGRDGQPGHPGQPGKDGRPG 268
Cdd:NF038329 319 DGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
94-261 7.00e-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: 56.07  E-value: 7.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   94 PGAQGPPGTPGSAGRPGKPGAPGLNGNPGRPPKEPCEPLTPPPCKPCPEGPPGPAGPPGPDGNKGPLGPPGPPGPEGPNG 173
Cdd:NF038329 170 AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGP 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  174 EPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQPGAPGEPGQPGQ---PGQRGPAGEPGKDGSPGGQGEKGASGEPGQPG 250
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKdglPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
                        170
                 ....*....|.
gi 17538760  251 RDGQPGHPGQP 261
Cdd:NF038329 330 KDGKDGQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
211-267 1.07e-07

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: 47.87  E-value: 1.07e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17538760   211 GEPGQPGQPGQRGPAGEPGKDGSPGGQGEKGASGEPGQPGRDGQPGHPGQPGKDGRP 267
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
73-269 6.24e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.04  E-value: 6.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   73 AHNRTARQAGEGNGQCEGCCLPGAQGPPGTPGSAGRPGKPGAPGlngnPGRPPKEPCEPLTPPPCKPCPEGPPGPAGPPG 152
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPA----EASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  153 PDGNKGPLGPPGPPGPEGPNGEPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQPGAPGEPGQPGQPGQRGPAGEPGKDG 232
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17538760  233 SPGgqgekGASGEPGQPGRDGQPGHPGQPGKDGRPGE 269
Cdd:PRK07764 750 DPA-----GAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
 
Name Accession Description Interval E-value
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
12-64 2.85e-16

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: 71.34  E-value: 2.85e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17538760     12 FVGYAALTFSTIAVLSVCITLPMMYNYIHHTRKVMHSDIVECKSEAQRLFSQV 64
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
94-271 6.61e-14

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: 71.47  E-value: 6.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   94 PGAQGPPGTPGSAGRPGKPGAPGLNGNPGRPPKEPCEPLTPPPCKPCPEGPPGPAGPPGPDGNKGPLGPPGPPGPEGPNG 173
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  174 EPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQPGAPGEPGQPGQPGQRGPAGEPGKDGSPGGQGEKGAS---------G 244
Cdd:NF038329 202 PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDgpdgkdgerG 281
                        170       180
                 ....*....|....*....|....*..
gi 17538760  245 EPGQPGRDGQPGHPGQPGKDGRPGEKG 271
Cdd:NF038329 282 PVGPAGKDGQNGKDGLPGKDGKDGQNG 308
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
15-64 1.82e-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, 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: 63.63  E-value: 1.82e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17538760    15 YAALTFSTIAVLSVCITLPMMYNYIHHTRKVMHSDIVECKSEAQRLFSQV 64
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
94-271 7.24e-13

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: 68.39  E-value: 7.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   94 PGAQGPPGTPGSAGRPGKPGAPGLNGNPGRPPKEPCEPLTPPPCKPCPEGPPGPAGPPGPDGNKGPLGPPGPPGPEGPNG 173
Cdd:NF038329 152 PGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  174 EPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQPGAPGEPGQPGQPGQRGPAGEPGKDGSPGGQGEKGASGEPGQPGRDG 253
Cdd:NF038329 232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311
                        170       180
                 ....*....|....*....|.
gi 17538760  254 QP---GHPGQPGKDGRPGEKG 271
Cdd:NF038329 312 LPgkdGKDGQPGKDGLPGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
93-268 4.73e-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: 65.70  E-value: 4.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   93 LPGAQGPPGTPGSAGRPGKPGAPGLNGNPGrPPKEPCEPLTPPPCKPCPEGPPGPAGPPGPDGNKGPLGPPGPPGPEGPN 172
Cdd:NF038329 160 EKGPAGPQGEAGPQGPAGKDGEAGAKGPAG-EKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  173 GEPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQP----GAPGEPGQPGQPGQRGPAGEPGKDGSPGGQGEKGASGEPGQ 248
Cdd:NF038329 239 GDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPdgkdGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
                        170       180
                 ....*....|....*....|
gi 17538760  249 PGRDGQPGHPGQPGKDGRPG 268
Cdd:NF038329 319 DGQPGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
94-261 7.00e-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: 56.07  E-value: 7.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   94 PGAQGPPGTPGSAGRPGKPGAPGLNGNPGRPPKEPCEPLTPPPCKPCPEGPPGPAGPPGPDGNKGPLGPPGPPGPEGPNG 173
Cdd:NF038329 170 AGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGP 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  174 EPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQPGAPGEPGQPGQ---PGQRGPAGEPGKDGSPGGQGEKGASGEPGQPG 250
Cdd:NF038329 250 QGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKdglPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPG 329
                        170
                 ....*....|.
gi 17538760  251 RDGQPGHPGQP 261
Cdd:NF038329 330 KDGKDGQPGKP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
211-267 1.07e-07

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: 47.87  E-value: 1.07e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17538760   211 GEPGQPGQPGQRGPAGEPGKDGSPGGQGEKGASGEPGQPGRDGQPGHPGQPGKDGRP 267
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
217-271 5.44e-07

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: 45.95  E-value: 5.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17538760   217 GQPGQRGPAGEPGKDGSPGGQGEKGASGEPGQPGRDGQPGHPGQPGKDGRPGEKG 271
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
207-255 1.07e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 42.10  E-value: 1.07e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17538760   207 PGAPGEPGQPGQPGQRGPAGEPGKDGSPGGQGEKGASGEPGQPGRDGQP 255
Cdd:pfam01391   9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
73-269 6.24e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.04  E-value: 6.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760   73 AHNRTARQAGEGNGQCEGCCLPGAQGPPGTPGSAGRPGKPGAPGlngnPGRPPKEPCEPLTPPPCKPCPEGPPGPAGPPG 152
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPA----EASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538760  153 PDGNKGPLGPPGPPGPEGPNGEPGNKGPAGPPGPGGKPGPAGPPGENGNNGEPQPGAPGEPGQPGQPGQRGPAGEPGKDG 232
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP 749
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17538760  233 SPGgqgekGASGEPGQPGRDGQPGHPGQPGKDGRPGE 269
Cdd:PRK07764 750 DPA-----GAPAQPPPPPAPAPAAAPAAAPPPSPPSE 781
 
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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