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Conserved domains on  [gi|17506917|ref|NP_491595|]
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Cuticle collagen dpy-5 [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 ...
 95-270 2.55e-26

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: 106.91  E-value: 2.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917   95 PAGAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKEcIKCPAGPPGQDGLPGQEGFQGLPGDAGKRGTPGKDGE 174
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG-EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  175 PGRVGDIGDQGTPGQDGQPGLAGPPGRDGLTGKGQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQGPTGQ--------- 245
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKdgergpvgp 285

                        170       180
                 ....*....|....*....|....*
gi 17506917  246 PGKDGFNGNDGTPGQAGPQGAVGAD 270
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKD 310
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 5-56 8.74e-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: 61.71  E-value: 8.74e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17506917      5 VVGFGAACGISAIVACLWAALVITNDINDMYDDVMGELGGFRDISDDTWGTL 56
Cdd:smart01088   2 VAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 95-270 2.55e-26

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: 106.91  E-value: 2.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917   95 PAGAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKEcIKCPAGPPGQDGLPGQEGFQGLPGDAGKRGTPGKDGE 174
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG-EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  175 PGRVGDIGDQGTPGQDGQPGLAGPPGRDGLTGKGQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQGPTGQ--------- 245
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKdgergpvgp 285

                        170       180
                 ....*....|....*....|....*
gi 17506917  246 PGKDGFNGNDGTPGQAGPQGAVGAD 270
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKD 310
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 62-275 1.02e-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: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917   62 GAGESAEQYVRGIFGRHKRSNSQCSCGLPSQGCPAGAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKECiKCP 141
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE-KGP 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  142 AGPPGQDGLPGQEGFQGLPGDAGKRGTPGKDGEPGRVGDI-----GDQGTPGQDGQPGLAGPPGRDGltGKGQPGVAGRP 216
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDG--PRGDRGEAGPD 271

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17506917  217 GMPGPRGEPGNNGNPGEEGQTGAQGPTGQPGKDGFNGNDGTPGQAGPQGAVGADAEYCP 275
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-264 7.49e-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: 99.98  E-value: 7.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917   63 AGESAEQYVRGIFGRHKRSNSQCSCGLPSQGCPAGAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKEcikcPA 142
Cdd:NF038329 149 AGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAG----ED 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  143 GPPGQDGlPGQEGFQGLPGDAGKRGTPGKDGEPGRVGDIGDQGTPGQDGQPGLAGPPGRDGLTGK-GQPGVAGRPGMPGP 221
Cdd:NF038329 225 GPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKdGQNGKDGLPGKDGK 303

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17506917  222 RGEPGNNGNPGEEGQTGAQGPTGQPGKDGfngNDGTPGQAGPQ 264
Cdd:NF038329 304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDG---KDGQPGKPAPK 343
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 5-56 8.74e-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: 61.71  E-value: 8.74e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17506917      5 VVGFGAACGISAIVACLWAALVITNDINDMYDDVMGELGGFRDISDDTWGTL 56
Cdd:smart01088   2 VAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 8-53 6.37e-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: 56.31  E-value: 6.37e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 17506917     8 FGAACGISAIVACLWAALVITNDINDMYDDVMGELGGFRDISDDTW 53
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAW 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 208-263 1.88e-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: 44.41  E-value: 1.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17506917   208 GQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQGPTGQPGKDGFNGNDGTPGQAGP 263
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 97-240 1.16e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.04  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917   97 GAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKECIKCPAGPPGQDGLPGqEGFQGLPGDAGKRGTPGKDGEPG 176
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPG-PHEPAPPESHNPSPNQQPSSFLQ 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17506917  177 RVGDIGDQGTPGQDGQPGLAGPPGRDGLTGKGQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQ 240
Cdd:PHA03169 169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVE 232
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
95-262 8.12e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.78  E-value: 8.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  95 PAGAPGNPGAPGEPGGTGPD---GKNGPTGLPGLNIPIPNDFPKEcikcPAGPPGQDGLPGQEGFQGLPGDAGKRGTPGK 171
Cdd:COG5164  56 PAGNTGGTRPAGNQGATGPAqnqGGTTPAQNQGGTRPAGNTGGTT----PAGDGGATGPPDDGGATGPPDDGGSTTPPSG 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917 172 DGEPGRVGDIGDQGTPGQDGQPGLAGPPGRDGLTGKGQPGVAGRPGMPGPRGEPGNNGN---PGEEGQTGAQGPTGQPGK 248
Cdd:COG5164 132 GSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGEtgtDIPTGGTPRQGPDGPVKK 211

                       170
                ....*....|....
gi 17506917 249 DGFNGNDGTPGQAG 262
Cdd:COG5164 212 DDKNGKGNPPDDRG 225
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 95-270 2.55e-26

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: 106.91  E-value: 2.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917   95 PAGAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKEcIKCPAGPPGQDGLPGQEGFQGLPGDAGKRGTPGKDGE 174
Cdd:NF038329 127 PAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG-EAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  175 PGRVGDIGDQGTPGQDGQPGLAGPPGRDGLTGKGQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQGPTGQ--------- 245
Cdd:NF038329 206 QGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKdgergpvgp 285

                        170       180
                 ....*....|....*....|....*
gi 17506917  246 PGKDGFNGNDGTPGQAGPQGAVGAD 270
Cdd:NF038329 286 AGKDGQNGKDGLPGKDGKDGQNGKD 310
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 62-275 1.02e-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: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917   62 GAGESAEQYVRGIFGRHKRSNSQCSCGLPSQGCPAGAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKECiKCP 141
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE-KGP 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  142 AGPPGQDGLPGQEGFQGLPGDAGKRGTPGKDGEPGRVGDI-----GDQGTPGQDGQPGLAGPPGRDGltGKGQPGVAGRP 216
Cdd:NF038329 194 QGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGqqgpdGDPGPTGEDGPQGPDGPAGKDG--PRGDRGEAGPD 271

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 17506917  217 GMPGPRGEPGNNGNPGEEGQTGAQGPTGQPGKDGFNGNDGTPGQAGPQGAVGADAEYCP 275
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGK 330
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 63-264 7.49e-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: 99.98  E-value: 7.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917   63 AGESAEQYVRGIFGRHKRSNSQCSCGLPSQGCPAGAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKEcikcPA 142
Cdd:NF038329 149 AGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAG----ED 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  143 GPPGQDGlPGQEGFQGLPGDAGKRGTPGKDGEPGRVGDIGDQGTPGQDGQPGLAGPPGRDGLTGK-GQPGVAGRPGMPGP 221
Cdd:NF038329 225 GPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKdGQNGKDGLPGKDGK 303

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 17506917  222 RGEPGNNGNPGEEGQTGAQGPTGQPGKDGfngNDGTPGQAGPQ 264
Cdd:NF038329 304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDG---KDGQPGKPAPK 343
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 5-56 8.74e-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: 61.71  E-value: 8.74e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17506917      5 VVGFGAACGISAIVACLWAALVITNDINDMYDDVMGELGGFRDISDDTWGTL 56
Cdd:smart01088   2 VAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 8-53 6.37e-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: 56.31  E-value: 6.37e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 17506917     8 FGAACGISAIVACLWAALVITNDINDMYDDVMGELGGFRDISDDTW 53
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAW 47
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 208-263 1.88e-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: 44.41  E-value: 1.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17506917   208 GQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQGPTGQPGKDGFNGNDGTPGQAGP 263
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 217-272 2.37e-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: 40.94  E-value: 2.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17506917   217 GMPGPRGEPGNNGNPGEEGQTGAQGPTGQPGKDGFNGNDGTPGQAGPQGAVGADAE 272
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 214-269 3.63e-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: 3.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17506917   214 GRPGMPGPRGEPGNNGNPGEEGQTGAQGPTGQPGKDGFNGNDGTPGQAGPQGAVGA 269
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 211-267 5.32e-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: 5.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17506917   211 GVAGRPGMPGPRGEPGNNGNPGEEGQTGAQGPTGQPGKDGFNGNDGTPGQAGPQGAV 267
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 143-199 6.61e-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: 39.78  E-value: 6.61e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17506917   143 GPPGQDGLPGQEGFQGLPGDAGKRGTPGKDGEPGRVGDIGDQGTPGQDGQPGLAGPP 199
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 97-240 1.16e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.04  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917   97 GAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKECIKCPAGPPGQDGLPGqEGFQGLPGDAGKRGTPGKDGEPG 176
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPG-PHEPAPPESHNPSPNQQPSSFLQ 168

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17506917  177 RVGDIGDQGTPGQDGQPGLAGPPGRDGLTGKGQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQ 240
Cdd:PHA03169 169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQAVE 232
PHA03169 PHA03169
hypothetical protein; Provisional
 106-266 1.74e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.65  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  106 GEPGGTGPDGKNGPTGLPGlnipipndfpkecikcPAGPPGQDGLPGQEGFQGLP-GDAGKRGTPGKDGEPGrvgdigdq 184
Cdd:PHA03169  90 GGPSGSGSESVGSPTPSPS----------------GSAEELASGLSPENTSGSSPeSPASHSPPPSPPSHPG-------- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  185 gtPGQDGQPGLAGPPGRDGLTGKGQPGVAGRPGMP-GPRGEPGNNGNPGEEGQTGAQGPTGQ-----PGKDGFNGNDGTP 258
Cdd:PHA03169 146 --PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPePPTSEPEPDSPGPPQSETPTSSPPPQsppdePGEPQSPTPQQAP 223


                 ....*...
gi 17506917  259 GQAGPQGA 266
Cdd:PHA03169 224 SPNTQQAV 231
PHA03169 PHA03169
hypothetical protein; Provisional
 157-272 5.36e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.11  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  157 QGLPGDAGKRGTPGKDGEPGRVGDIGDQGTPGQDGQPGlaGPPGRDGLTGKGQPGVAGRPGMPGPRGEPGNNGNPGEEGQ 236
Cdd:PHA03169  89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGS--SPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSF 166

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 17506917  237 TG---------AQGPTGQPGKDGFNGNDGTPGQAGPQGAVGADAE 272
Cdd:PHA03169 167 LQpshedspeePEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEP 211
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 206-261 6.63e-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: 37.09  E-value: 6.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17506917   206 GKGQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQGPTGQPgkdGFNGNDGTPGQA 261
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPP---GPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
95-262 8.12e-04

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 40.78  E-value: 8.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  95 PAGAPGNPGAPGEPGGTGPD---GKNGPTGLPGLNIPIPNDFPKEcikcPAGPPGQDGLPGQEGFQGLPGDAGKRGTPGK 171
Cdd:COG5164  56 PAGNTGGTRPAGNQGATGPAqnqGGTTPAQNQGGTRPAGNTGGTT----PAGDGGATGPPDDGGATGPPDDGGSTTPPSG 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917 172 DGEPGRVGDIGDQGTPGQDGQPGLAGPPGRDGLTGKGQPGVAGRPGMPGPRGEPGNNGN---PGEEGQTGAQGPTGQPGK 248
Cdd:COG5164 132 GSTTPPGDGGSTPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNKGEtgtDIPTGGTPRQGPDGPVKK 211

                       170
                ....*....|....
gi 17506917 249 DGFNGNDGTPGQAG 262
Cdd:COG5164 212 DDKNGKGNPPDDRG 225
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 90-272 9.31e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 9.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917   90 PSQGCPAGAPGNPGAPGEPGGTGPDGKNGPTGLPGLNIPIPNDFPKECIKCPAGPPGQDGLPGQEGFQGLPGDAGKRGTP 169
Cdd:PRK07764 603 PASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPP 682

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  170 GKDGEPGRVGDIGDQGTPGQDGQPGLAGPPGRDGLTGkGQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQGPTGQPGKD 249
Cdd:PRK07764 683 PAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAA-QPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPP 761

                        170       180
                 ....*....|....*....|...
gi 17506917  250 GFNGNDGTPGQAGPQGAVGADAE 272
Cdd:PRK07764 762 PAPAPAAAPAAAPPPSPPSEEEE 784
PHA03169 PHA03169
hypothetical protein; Provisional
 165-278 1.33e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.95  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17506917  165 KRGTPGKDGEPGRVGDiGDQGTPGQDGQPGLAGPPGRDGLTGK-GQPGVAGRPGMPGPRGEPGNNGNPGEEGQTGAQGPT 243
Cdd:PHA03169  80 RHGEKEERGQGGPSGS-GSESVGSPTPSPSGSAEELASGLSPEnTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPS 158

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 17506917  244 GQPGKDGFNGNDGTPGQAGPQGAVGADAEYCPCPE 278
Cdd:PHA03169 159 PNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPP 193
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 158-222 6.78e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 34.39  E-value: 6.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17506917   158 GLPGDAGKRGTPGKDGEPGRVGDIGDQGTPGQDGQPGLAGPPgrdgltgkGQPGVAGRPGMPGPR 222
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP--------GPPGPPGAPGAPGPP 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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