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Conserved domains on  [gi|392927765|ref|NP_001257223|]
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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
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 89-264 5.54e-20

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.19  E-value: 5.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  89 GLQSQGCPDGPPGARGPQGAPGLPGAPGVDGKPGVDGKSLTYVHAAEADCIPCPGGEAGPPGPDGEPGVR-GPNGPPGPN 167
Cdd:NF038329 165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQqGPDGDPGPT 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 168 GHPGQPgrpGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQ 247
Cdd:NF038329 245 GEDGPQ---GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                        170
                 ....*....|....*..
gi 392927765 248 PGVPGEPGEDGTPGEPG 264
Cdd:NF038329 322 PGKDGLPGKDGKDGQPG 338
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 3-55 7.76e-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. 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: 59.02  E-value: 7.76e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392927765     3 YAVAVTSAASIVATGMLLISVGNIISDLNNLQLEITDGMNDFKMKSDETWSRI 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 ...
 89-264 5.54e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.19  E-value: 5.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  89 GLQSQGCPDGPPGARGPQGAPGLPGAPGVDGKPGVDGKSLTYVHAAEADCIPCPGGEAGPPGPDGEPGVR-GPNGPPGPN 167
Cdd:NF038329 165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQqGPDGDPGPT 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 168 GHPGQPgrpGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQ 247
Cdd:NF038329 245 GEDGPQ---GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                        170
                 ....*....|....*..
gi 392927765 248 PGVPGEPGEDGTPGEPG 264
Cdd:NF038329 322 PGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 96-272 2.34e-19

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: 87.27  E-value: 2.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  96 PDGPPGARGPQGAPGLPGAPGVDGKPGVDGksltyvhaaeadcipcPGGEAGPPGPDGEPGVRGPNGPPGPNGHPGQPGR 175
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPG----------------PQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 176 PGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKP-----------GDVGPCGPEGPKGAPGTPGKNGAPGDRGF 244
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAgpagdgqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                        170       180
                 ....*....|....*....|....*...
gi 392927765 245 GGQPGVPGEPGEDGTPGEPGADGAPGDD 272
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKD 295
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 89-272 4.71e-19

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: 86.50  E-value: 4.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  89 GLQSQGCPDGPPGARGPQGAPGLPGAPGVDGKPGVDGKsltyvhaaeadcipCPGGEAGPPGPDGEPGVRGPNGPPGPNG 168
Cdd:NF038329 156 GERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--------------QGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 169 HPGQPGRPGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQP 248
Cdd:NF038329 222 GEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                        170       180
                 ....*....|....*....|....
gi 392927765 249 GVPGEPGEDGTPGEPGADGAPGDD 272
Cdd:NF038329 302 GKDGQNGKDGLPGKDGKDGQPGKD 325
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 176-272 2.75e-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: 81.10  E-value: 2.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 176 PGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQPGVPGEPG 255
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90
                 ....*....|....*..
gi 392927765 256 EDGTPGEPGADGAPGDD 272
Cdd:NF038329 202 PAGEQGPAGPAGPDGEA 218
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 97-272 2.40e-16

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: 78.41  E-value: 2.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  97 DGPPGARGPQGAPGLPGAPGVDGKPGVDGksltyvhaaeadcipcpggeagppgpdgepgvrgpngPPGPNGHPGQPGRP 176
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETG-------------------------------------PAGPAGPPGPQGER 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 177 GPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQPGvPGEPGE 256
Cdd:NF038329 159 GEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGP 237

                        170
                 ....*....|....*.
gi 392927765 257 DGTPGEPGADGAPGDD 272
Cdd:NF038329 238 DGDPGPTGEDGPQGPD 253
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 3-55 7.76e-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. 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: 59.02  E-value: 7.76e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392927765     3 YAVAVTSAASIVATGMLLISVGNIISDLNNLQLEITDGMNDFKMKSDETWSRI 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 ...
 7-55 6.27e-11

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: 56.70  E-value: 6.27e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392927765    7 VTSAASIVATGMLLISVGNIISDLNNLQLEITDGMNDFKMKSDETWSRI 55
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 213-269 7.74e-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: 45.18  E-value: 7.74e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392927765  213 GKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQPGVPGEPGEDGTPGEPGADGAP 269
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 96-274 2.69e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  96 PDGPPGARGPQGAPGLPGAPGVDGKPGVDGKSLTYVHAAEADCIPCPGGEAGPPGPDGEPGVRGPNGPPGPNGHPGQPGR 175
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 176 PGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPgdvGPCGPEGPKGAPGTPGKNGAPGDRGFGGQPGVPGEPG 255
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATP---PAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746

                        170
                 ....*....|....*....
gi 392927765 256 EDGTPGEPGADGAPGDDAG 274
Cdd:PRK07764 747 DPPDPAGAPAQPPPPPAPA 765
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 89-264 5.54e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 89.19  E-value: 5.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  89 GLQSQGCPDGPPGARGPQGAPGLPGAPGVDGKPGVDGKSLTYVHAAEADCIPCPGGEAGPPGPDGEPGVR-GPNGPPGPN 167
Cdd:NF038329 165 GPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQqGPDGDPGPT 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 168 GHPGQPgrpGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQ 247
Cdd:NF038329 245 GEDGPQ---GPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQ 321

                        170
                 ....*....|....*..
gi 392927765 248 PGVPGEPGEDGTPGEPG 264
Cdd:NF038329 322 PGKDGLPGKDGKDGQPG 338
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 96-272 2.34e-19

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: 87.27  E-value: 2.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  96 PDGPPGARGPQGAPGLPGAPGVDGKPGVDGksltyvhaaeadcipcPGGEAGPPGPDGEPGVRGPNGPPGPNGHPGQPGR 175
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPG----------------PQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 176 PGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKP-----------GDVGPCGPEGPKGAPGTPGKNGAPGDRGF 244
Cdd:NF038329 188 AGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAgpagdgqqgpdGDPGPTGEDGPQGPDGPAGKDGPRGDRGE 267

                        170       180
                 ....*....|....*....|....*...
gi 392927765 245 GGQPGVPGEPGEDGTPGEPGADGAPGDD 272
Cdd:NF038329 268 AGPDGPDGKDGERGPVGPAGKDGQNGKD 295
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 89-272 4.71e-19

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: 86.50  E-value: 4.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  89 GLQSQGCPDGPPGARGPQGAPGLPGAPGVDGKPGVDGKsltyvhaaeadcipCPGGEAGPPGPDGEPGVRGPNGPPGPNG 168
Cdd:NF038329 156 GERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGP--------------QGPRGETGPAGEQGPAGPAGPDGEAGPA 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 169 HPGQPGRPGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQP 248
Cdd:NF038329 222 GEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                        170       180
                 ....*....|....*....|....
gi 392927765 249 GVPGEPGEDGTPGEPGADGAPGDD 272
Cdd:NF038329 302 GKDGQNGKDGLPGKDGKDGQPGKD 325
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 176-272 2.75e-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: 81.10  E-value: 2.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 176 PGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQPGVPGEPG 255
Cdd:NF038329 122 PGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETG 201

                         90
                 ....*....|....*..
gi 392927765 256 EDGTPGEPGADGAPGDD 272
Cdd:NF038329 202 PAGEQGPAGPAGPDGEA 218
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 97-272 2.40e-16

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: 78.41  E-value: 2.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  97 DGPPGARGPQGAPGLPGAPGVDGKPGVDGksltyvhaaeadcipcpggeagppgpdgepgvrgpngPPGPNGHPGQPGRP 176
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQGPRGDRGETG-------------------------------------PAGPAGPPGPQGER 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 177 GPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQPGvPGEPGE 256
Cdd:NF038329 159 GEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGP 237

                        170
                 ....*....|....*.
gi 392927765 257 DGTPGEPGADGAPGDD 272
Cdd:NF038329 238 DGDPGPTGEDGPQGPD 253
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 3-55 7.76e-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. 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: 59.02  E-value: 7.76e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392927765     3 YAVAVTSAASIVATGMLLISVGNIISDLNNLQLEITDGMNDFKMKSDETWSRI 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 ...
 7-55 6.27e-11

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: 56.70  E-value: 6.27e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 392927765    7 VTSAASIVATGMLLISVGNIISDLNNLQLEITDGMNDFKMKSDETWSRI 55
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 213-269 7.74e-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: 45.18  E-value: 7.74e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392927765  213 GKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQPGVPGEPGEDGTPGEPGADGAP 269
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 210-265 1.24e-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: 44.79  E-value: 1.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392927765  210 GVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQPGVPGEPGEDGTPGEPGA 265
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 222-272 7.78e-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: 7.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392927765  222 GPEGPKGAPGTPGKNGAPGDRGFGGQPGVPGEPGEDGTPGEPGADGAPGDD 272
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 189-243 1.89e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392927765  189 GPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRG 243
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 177-233 1.93e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 41.33  E-value: 1.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392927765  177 GPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTP 233
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 96-274 2.69e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  96 PDGPPGARGPQGAPGLPGAPGVDGKPGVDGKSLTYVHAAEADCIPCPGGEAGPPGPDGEPGVRGPNGPPGPNGHPGQPGR 175
Cdd:PRK07764 590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 176 PGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPgdvGPCGPEGPKGAPGTPGKNGAPGDRGFGGQPGVPGEPG 255
Cdd:PRK07764 670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATP---PAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746

                        170
                 ....*....|....*....
gi 392927765 256 EDGTPGEPGADGAPGDDAG 274
Cdd:PRK07764 747 DPPDPAGAPAQPPPPPAPA 765
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 96-274 5.15e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765  96 PDGPPGARGPQGAPGLPGAPGVDGKPGVDGKSLTYVHAAEADCIPCPGGEAGPPGPDGEPGVRGPNGPPGPNGHPGQPGR 175
Cdd:PRK07764 615 PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPA 694

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 176 PGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGPKGAPGTPGKNGAPGDRGFGGQPGVPGEPG 255
Cdd:PRK07764 695 GAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAP 774

                        170
                 ....*....|....*....
gi 392927765 256 EDGTPGEPgaDGAPGDDAG 274
Cdd:PRK07764 775 PPSPPSEE--EEMAEDDAP 791
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 175-226 2.62e-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: 38.24  E-value: 2.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392927765  175 RPGPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDVGPCGPEGP 226
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 177-274 8.34e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 40.34  E-value: 8.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392927765 177 GPAGPAGPEGKDGPVGPHGPAGPAGPRGTRHSAGVPGKPGDvGPCGPEGPKGA-PGTPGKNGAPGDRGFGGQPGVPGE-- 253
Cdd:PHA03169 124 SGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPS-SFLQPSHEDSPeEPEPPTSEPEPDSPGPPQSETPTSsp 202

                         90       100
                 ....*....|....*....|....*.
gi 392927765 254 -----PGEDGTPGEPGADGAPGDDAG 274
Cdd:PHA03169 203 ppqspPDEPGEPQSPTPQQAPSPNTQ 228
 
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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