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Conserved domains on  [gi|17511053|ref|NP_492245|]
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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 ...
 7-59 5.72e-14

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: 65.57  E-value: 5.72e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17511053      7 LVAGTAVALCGVAIVPAIFAALFVLHDINSFQSGVYEDLAEFKTLAEDAWTTM 59
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 98-293 3.41e-11

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: 64.16  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053   98 GPQPKDCPAGPPGPPGNPGTPGDDGPAGRAGNPGSDSTEGDRMA------DFNKDVKCPAGPPGPPGPNGFPGHPGPDGD 171
Cdd:NF038329 144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPagekgpQGPRGETGPAGEQGPAGPAGPDGEAGPAGE 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  172 FGV-----DGTNGKDGEPGPDGPEGDEGTPGLPGPPGEDGPVGQNGTRGQ----GQPGPVGAPGAPGGPGRDGEPGENGQ 242
Cdd:NF038329 224 DGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPdgkdGERGPVGPAGKDGQNGKDGLPGKDGK 303

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17511053  243 DGQQGPEGPAGADGQPGHPGPDGPSGDVGEVGAPGADAAYCPCPPRSAEMA 293
Cdd:NF038329 304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA 354
PRK07003 super family cl35530
DNA polymerase III subunit gamma/tau;
248-378 2.36e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK07003:

Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  248 PEGPAGADGQPGHPGPdGPSGDVGEVGAPGADAAYCPCPPRSAEMAATGSSDSQPASYEAPAPAATKGYDSPAPAAPKGY 327
Cdd:PRK07003 417 AAAATRAEAPPAAPAP-PATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPR 495

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17511053  328 DAPAPTAPHPPPPAPVAPPKLHDYESPAPVADAHDAAPAAQPYKRRKVARA 378
Cdd:PRK07003 496 AAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARA 546
 
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 ...
 7-59 5.72e-14

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: 65.57  E-value: 5.72e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17511053      7 LVAGTAVALCGVAIVPAIFAALFVLHDINSFQSGVYEDLAEFKTLAEDAWTTM 59
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 12-59 2.24e-12

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


Pssm-ID: 460226  Cd Length: 50  Bit Score: 61.32  E-value: 2.24e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 17511053    12 AVALCGVAIVPAIFAALFVLHDINSFQSGVYEDLAEFKTLAEDAWTTM 59
Cdd:pfam01484   3 AVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 98-293 3.41e-11

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: 64.16  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053   98 GPQPKDCPAGPPGPPGNPGTPGDDGPAGRAGNPGSDSTEGDRMA------DFNKDVKCPAGPPGPPGPNGFPGHPGPDGD 171
Cdd:NF038329 144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPagekgpQGPRGETGPAGEQGPAGPAGPDGEAGPAGE 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  172 FGV-----DGTNGKDGEPGPDGPEGDEGTPGLPGPPGEDGPVGQNGTRGQ----GQPGPVGAPGAPGGPGRDGEPGENGQ 242
Cdd:NF038329 224 DGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPdgkdGERGPVGPAGKDGQNGKDGLPGKDGK 303

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17511053  243 DGQQGPEGPAGADGQPGHPGPDGPSGDVGEVGAPGADAAYCPCPPRSAEMA 293
Cdd:NF038329 304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA 354
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 120-279 3.56e-11

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: 64.16  E-value: 3.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  120 DDGPAGRAGNPGSDSTEGDRMADFNKDVKCPAGPPGPPgpngfpghpgpdgdfGVDGTNGKDGEPGPDGPEGDEGTPGLP 199
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA---------------GKDGEAGAKGPAGEKGPQGPRGETGPA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  200 GPPGEDGPVGQNGTRGQGQPGPVGAPGAPGGPGRDGEPGENGQDGQQGPEGPAGADGQ------PGHPGPDGPSGDVGEV 273
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPrgdrgeAGPDGPDGKDGERGPV 283


                 ....*.
gi 17511053  274 GAPGAD 279
Cdd:NF038329 284 GPAGKD 289
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 81-266 5.76e-07

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: 51.06  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053   81 GDAGVAGSASGSSGCNCGPQPKDCPAGPPGPPGNPGTPGDDGPAGRAGNPGSDSTEGDRMADFNKDVKCPAGPPGPpgpn 160
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP---- 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  161 gfpghpgpDGDFGVDGTNGKDGEPGPDGPEGdegtpglpgppgedgpvgQNGTRGqgqpgpvgapgapggpgRDGEPGEN 240
Cdd:NF038329 283 --------VGPAGKDGQNGKDGLPGKDGKDG------------------QNGKDG-----------------LPGKDGKD 319

                        170       180
                 ....*....|....*....|....*.
gi 17511053  241 GQDGQQGPEGPAGADGQPGHPGPDGP 266
Cdd:NF038329 320 GQPGKDGLPGKDGKDGQPGKPAPKTP 345
PHA03169 PHA03169
hypothetical protein; Provisional
 169-310 8.69e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  169 DGDFGVDGTNGKDGEPGPDGPEG-DEGTPGLPGPPGEDGPVGQNGTRGQGQPGPVGAPGAPGGPGRDGEPGENGQDGQQG 247
Cdd:PHA03169  95 SGSESVGSPTPSPSGSAEELASGlSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDS 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511053  248 PEGPAGADGQPGHPGPDGPSGDVGEVGAPGADAAYCPCPPR--------SAEMAATGSSDSQPASYEAPAP 310
Cdd:PHA03169 175 PEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQsptpqqapSPNTQQAVEHEDEPTEPEREGP 245
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 234-278 1.38e-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: 1.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 17511053   234 DGEPGENGQDGQQGPEGPAGADGQPGHPGPDGPSGDVGEVGAPGA 278
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 235-288 1.18e-04

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 43.74  E-value: 1.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17511053  235 GEPGENGQDGQQGPEGPAGADGQPGHPGPDGPSGDVGEVGAPGADAAYCPCPPR 288
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
248-378 2.36e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  248 PEGPAGADGQPGHPGPdGPSGDVGEVGAPGADAAYCPCPPRSAEMAATGSSDSQPASYEAPAPAATKGYDSPAPAAPKGY 327
Cdd:PRK07003 417 AAAATRAEAPPAAPAP-PATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPR 495

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17511053  328 DAPAPTAPHPPPPAPVAPPKLHDYESPAPVADAHDAAPAAQPYKRRKVARA 378
Cdd:PRK07003 496 AAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARA 546
 
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 ...
 7-59 5.72e-14

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: 65.57  E-value: 5.72e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17511053      7 LVAGTAVALCGVAIVPAIFAALFVLHDINSFQSGVYEDLAEFKTLAEDAWTTM 59
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 12-59 2.24e-12

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


Pssm-ID: 460226  Cd Length: 50  Bit Score: 61.32  E-value: 2.24e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 17511053    12 AVALCGVAIVPAIFAALFVLHDINSFQSGVYEDLAEFKTLAEDAWTTM 59
Cdd:pfam01484   3 AVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 98-293 3.41e-11

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: 64.16  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053   98 GPQPKDCPAGPPGPPGNPGTPGDDGPAGRAGNPGSDSTEGDRMA------DFNKDVKCPAGPPGPPGPNGFPGHPGPDGD 171
Cdd:NF038329 144 GPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPagekgpQGPRGETGPAGEQGPAGPAGPDGEAGPAGE 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  172 FGV-----DGTNGKDGEPGPDGPEGDEGTPGLPGPPGEDGPVGQNGTRGQ----GQPGPVGAPGAPGGPGRDGEPGENGQ 242
Cdd:NF038329 224 DGPagpagDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPdgkdGERGPVGPAGKDGQNGKDGLPGKDGK 303

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17511053  243 DGQQGPEGPAGADGQPGHPGPDGPSGDVGEVGAPGADAAYCPCPPRSAEMA 293
Cdd:NF038329 304 DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKPAPKTPEVPQKPDTA 354
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 120-279 3.56e-11

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: 64.16  E-value: 3.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  120 DDGPAGRAGNPGSDSTEGDRMADFNKDVKCPAGPPGPPgpngfpghpgpdgdfGVDGTNGKDGEPGPDGPEGDEGTPGLP 199
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA---------------GKDGEAGAKGPAGEKGPQGPRGETGPA 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  200 GPPGEDGPVGQNGTRGQGQPGPVGAPGAPGGPGRDGEPGENGQDGQQGPEGPAGADGQ------PGHPGPDGPSGDVGEV 273
Cdd:NF038329 204 GEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPrgdrgeAGPDGPDGKDGERGPV 283


                 ....*.
gi 17511053  274 GAPGAD 279
Cdd:NF038329 284 GPAGKD 289
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 81-266 5.76e-07

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: 51.06  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053   81 GDAGVAGSASGSSGCNCGPQPKDCPAGPPGPPGNPGTPGDDGPAGRAGNPGSDSTEGDRMADFNKDVKCPAGPPGPpgpn 160
Cdd:NF038329 207 GPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGP---- 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  161 gfpghpgpDGDFGVDGTNGKDGEPGPDGPEGdegtpglpgppgedgpvgQNGTRGqgqpgpvgapgapggpgRDGEPGEN 240
Cdd:NF038329 283 --------VGPAGKDGQNGKDGLPGKDGKDG------------------QNGKDG-----------------LPGKDGKD 319

                        170       180
                 ....*....|....*....|....*.
gi 17511053  241 GQDGQQGPEGPAGADGQPGHPGPDGP 266
Cdd:NF038329 320 GQPGKDGLPGKDGKDGQPGKPAPKTP 345
PHA03169 PHA03169
hypothetical protein; Provisional
 169-310 8.69e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  169 DGDFGVDGTNGKDGEPGPDGPEG-DEGTPGLPGPPGEDGPVGQNGTRGQGQPGPVGAPGAPGGPGRDGEPGENGQDGQQG 247
Cdd:PHA03169  95 SGSESVGSPTPSPSGSAEELASGlSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDS 174

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17511053  248 PEGPAGADGQPGHPGPDGPSGDVGEVGAPGADAAYCPCPPR--------SAEMAATGSSDSQPASYEAPAP 310
Cdd:PHA03169 175 PEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQsptpqqapSPNTQQAVEHEDEPTEPEREGP 245
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 234-278 1.38e-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: 1.38e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 17511053   234 DGEPGENGQDGQQGPEGPAGADGQPGHPGPDGPSGDVGEVGAPGA 278
Cdd:pfam01391  12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 235-288 1.18e-04

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 43.74  E-value: 1.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 17511053  235 GEPGENGQDGQQGPEGPAGADGQPGHPGPDGPSGDVGEVGAPGADAAYCPCPPR 288
Cdd:NF038329 120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ 173
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 235-276 2.66e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.63  E-value: 2.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 17511053   235 GEPGENGQDGQQGPEGPAGADGQPGHPGPDGPSGDVGEVGAP 276
Cdd:pfam01391  16 GPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
248-378 2.36e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.22  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17511053  248 PEGPAGADGQPGHPGPdGPSGDVGEVGAPGADAAYCPCPPRSAEMAATGSSDSQPASYEAPAPAATKGYDSPAPAAPKGY 327
Cdd:PRK07003 417 AAAATRAEAPPAAPAP-PATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPR 495

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 17511053  328 DAPAPTAPHPPPPAPVAPPKLHDYESPAPVADAHDAAPAAQPYKRRKVARA 378
Cdd:PRK07003 496 AAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARA 546
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 238-279 4.27e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.16  E-value: 4.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 17511053   238 GENGQDGQQGPEGPAGADGQPGHPGPDGPSGDVGEVGAPGAD 279
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPP 42
 
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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