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Conserved domains on  [gi|17566918|ref|NP_506061|]
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Cuticle collagen lon-3 [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 ...
 124-297 2.47e-29

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: 116.54  E-value: 2.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  124 PTGPDGEEGEQGPDGQDGVDGVPGFDGQDCPDVEQQPsqgcftcpQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPG 203
Cdd:NF038329 136 PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP--------QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  204 MPGEMGPTGAPGDDGAPGASGMKGDDAEKPVGRQGQRGQPGEQGPDGEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDG 283
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                        170
                 ....*....|....
gi 17566918  284 EEGPRGPSGLPGKD 297
Cdd:NF038329 288 KDGQNGKDGLPGKD 301
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 5-57 4.49e-15

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: 68.26  E-value: 4.49e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17566918      5 TATSGALIFSGASLLVSLFAAASIYSQVSSIWTELDNEIDSFKLLTNDIWGDM 57
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 ...
 124-297 2.47e-29

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: 116.54  E-value: 2.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  124 PTGPDGEEGEQGPDGQDGVDGVPGFDGQDCPDVEQQPsqgcftcpQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPG 203
Cdd:NF038329 136 PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP--------QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  204 MPGEMGPTGAPGDDGAPGASGMKGDDAEKPVGRQGQRGQPGEQGPDGEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDG 283
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                        170
                 ....*....|....
gi 17566918  284 EEGPRGPSGLPGKD 297
Cdd:NF038329 288 KDGQNGKDGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 124-299 3.30e-29

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: 116.16  E-value: 3.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  124 PTGPDGEEGEQGPDGQDGVDGVPGFDGQDCPDVEQQPsqgcfTCPQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPG 203
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE-----KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  204 MPGEMGPTGAPGDDGAPGASGMKGDDAEKPVGRQGQRGQPGEQGPDGEEGPAGKDafeGPPGVEGEVGVPGYQGSAGPDG 283
Cdd:NF038329 199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD---GPAGKDGPRGDRGEAGPDGPDG 275

                        170
                 ....*....|....*.
gi 17566918  284 EEGPRGPSGLPGKDAE 299
Cdd:NF038329 276 KDGERGPVGPAGKDGQ 291
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 87-297 1.57e-27

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: 111.54  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918   87 PQFPQGDKGPLPVPGlPFGPNVSGGSDRCQCTVENTCPTGPDGEEGEQGPDGQDGVDGVPGFDGQDCPDVEQQPsqgcfT 166
Cdd:NF038329 127 PAGPAGEQGPRGDRG-ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE-----T 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  167 CPQGLPGPQGSQGAPGIRGMRGARGQPGYPGR--DGQPGMPGEMGPTGAPGDDGAPGASGMKGDDAEKpvGRQGQRGQPG 244
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA--GPDGPDGKDG 278

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17566918  245 EQGPDGEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDGEEGPRGPSGLPGKD 297
Cdd:NF038329 279 ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD 331
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 128-299 3.51e-22

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: 96.13  E-value: 3.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  128 DGEEGEQGPDGQDGVDGVPGfdgqdcpdveqqpsqgcftcPQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGE 207
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQG--------------------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  208 MGPTGAPGDDGAPGASGMKGDDAEkpVGRQGQRGQPGEQGPDGEEGPAGKDAFEGPPGVegevGVPGYQGSAGPDGEEGP 287
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGE--TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGP 249

                        170
                 ....*....|..
gi 17566918  288 RGPSGLPGKDAE 299
Cdd:NF038329 250 QGPDGPAGKDGP 261
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 5-57 4.49e-15

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: 68.26  E-value: 4.49e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17566918      5 TATSGALIFSGASLLVSLFAAASIYSQVSSIWTELDNEIDSFKLLTNDIWGDM 57
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 185-314 1.70e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 73.79  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  185 GMRGARGQPGYPGRDGQPGMPGEMGPTGAPGDDGAPGASGMKGDDaekpvgrqGQRGQPGEQGPDGEEGPAGKDAFEGPP 264
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK--------GPAGPQGEAGPQGPAGKDGEAGAKGPA 188

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17566918  265 GVEGEVGVPGYQGSAGPDGEEGPRGPSGLPGKDAEYCKCPTRDDGGNSHR 314
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD 238
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 9-57 2.26e-13

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


Pssm-ID: 460226  Cd Length: 50  Bit Score: 63.63  E-value: 2.26e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17566918     9 GALIFSGASLLVSLFAAASIYSQVSSIWTELDNEIDSFKLLTNDIWGDM 57
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 168-222 6.99e-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: 42.87  E-value: 6.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17566918   168 PQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGEMGPTGAPGDDGAPGA 222
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 126-309 1.43e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.50  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  126 GPDGEEGEQGPDGQDGVDGVPGFDGQDcpdvEQQPSQGCFTCPQGLPGPQGSQGAPGirgmRGARGQPGYPGRDGQPGMP 205
Cdd:PHA03169  93 SGSGSESVGSPTPSPSGSAEELASGLS----PENTSGSSPESPASHSPPPSPPSHPG----PHEPAPPESHNPSPNQQPS 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  206 GEMGPTGAPGDDGAPGASGMKGDDAEKP-VGRQGQRGQPGEQGPDgEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDGE 284
Cdd:PHA03169 165 SFLQPSHEDSPEEPEPPTSEPEPDSPGPpQSETPTSSPPPQSPPD-EPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPERE 243

                        170       180
                 ....*....|....*....|....*
gi 17566918  285 EGPRGPSGLPGKDAEYCKCPTRDDG 309
Cdd:PHA03169 244 GPPFPGHRSHSYTVVGWKPSTRPGG 268
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 75-285 6.35e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 38.44  E-value: 6.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918     75 GGYGATGTNAPEPQFPQGDKGPLPVPGLPFGPNVSGGSDRCQCTVENTCPTGPDGEEGEQgpdgqdgvDGVPGFDGQDCP 154
Cdd:TIGR00927  671 GETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEG--------EIETGEEGEEVE 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918    155 DVEQQPSQGCFTCPQglpgpQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGEMgpTGAPGDDGAPGASGMKGDDAEKPV 234
Cdd:TIGR00927  743 DEGEGEAEGKHEVET-----EGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEM--KGDEGAEGKVEHEGETEAGEKDEH 815

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 17566918    235 GRQGQRGQPGEQGPDgEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDGEE 285
Cdd:TIGR00927  816 EGQSETQADDTEVKD-ETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEE 865
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 124-297 2.47e-29

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: 116.54  E-value: 2.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  124 PTGPDGEEGEQGPDGQDGVDGVPGFDGQDCPDVEQQPsqgcftcpQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPG 203
Cdd:NF038329 136 PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP--------QGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  204 MPGEMGPTGAPGDDGAPGASGMKGDDAEKPVGRQGQRGQPGEQGPDGEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDG 283
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                        170
                 ....*....|....
gi 17566918  284 EEGPRGPSGLPGKD 297
Cdd:NF038329 288 KDGQNGKDGLPGKD 301
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 124-299 3.30e-29

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: 116.16  E-value: 3.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  124 PTGPDGEEGEQGPDGQDGVDGVPGFDGQDCPDVEQQPsqgcfTCPQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPG 203
Cdd:NF038329 124 PAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGE-----KGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  204 MPGEMGPTGAPGDDGAPGASGMKGDDAEKPVGRQGQRGQPGEQGPDGEEGPAGKDafeGPPGVEGEVGVPGYQGSAGPDG 283
Cdd:NF038329 199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD---GPAGKDGPRGDRGEAGPDGPDG 275

                        170
                 ....*....|....*.
gi 17566918  284 EEGPRGPSGLPGKDAE 299
Cdd:NF038329 276 KDGERGPVGPAGKDGQ 291
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 87-297 1.57e-27

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: 111.54  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918   87 PQFPQGDKGPLPVPGlPFGPNVSGGSDRCQCTVENTCPTGPDGEEGEQGPDGQDGVDGVPGFDGQDCPDVEQQPsqgcfT 166
Cdd:NF038329 127 PAGPAGEQGPRGDRG-ETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGE-----T 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  167 CPQGLPGPQGSQGAPGIRGMRGARGQPGYPGR--DGQPGMPGEMGPTGAPGDDGAPGASGMKGDDAEKpvGRQGQRGQPG 244
Cdd:NF038329 201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEA--GPDGPDGKDG 278

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17566918  245 EQGPDGEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDGEEGPRGPSGLPGKD 297
Cdd:NF038329 279 ERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD 331
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 128-299 3.51e-22

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: 96.13  E-value: 3.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  128 DGEEGEQGPDGQDGVDGVPGfdgqdcpdveqqpsqgcftcPQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGE 207
Cdd:NF038329 116 DGEKGEPGPAGPAGPAGEQG--------------------PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  208 MGPTGAPGDDGAPGASGMKGDDAEkpVGRQGQRGQPGEQGPDGEEGPAGKDAFEGPPGVegevGVPGYQGSAGPDGEEGP 287
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGE--TGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD----GQQGPDGDPGPTGEDGP 249

                        170
                 ....*....|..
gi 17566918  288 RGPSGLPGKDAE 299
Cdd:NF038329 250 QGPDGPAGKDGP 261
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 5-57 4.49e-15

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: 68.26  E-value: 4.49e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17566918      5 TATSGALIFSGASLLVSLFAAASIYSQVSSIWTELDNEIDSFKLLTNDIWGDM 57
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 185-314 1.70e-14

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 73.79  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  185 GMRGARGQPGYPGRDGQPGMPGEMGPTGAPGDDGAPGASGMKGDDaekpvgrqGQRGQPGEQGPDGEEGPAGKDAFEGPP 264
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEK--------GPAGPQGEAGPQGPAGKDGEAGAKGPA 188

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 17566918  265 GVEGEVGVPGYQGSAGPDGEEGPRGPSGLPGKDAEYCKCPTRDDGGNSHR 314
Cdd:NF038329 189 GEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPD 238
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 9-57 2.26e-13

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


Pssm-ID: 460226  Cd Length: 50  Bit Score: 63.63  E-value: 2.26e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17566918     9 GALIFSGASLLVSLFAAASIYSQVSSIWTELDNEIDSFKLLTNDIWGDM 57
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 168-222 6.99e-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: 42.87  E-value: 6.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17566918   168 PQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGEMGPTGAPGDDGAPGA 222
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PHA03169 PHA03169
hypothetical protein; Provisional
 126-309 1.43e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.50  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  126 GPDGEEGEQGPDGQDGVDGVPGFDGQDcpdvEQQPSQGCFTCPQGLPGPQGSQGAPGirgmRGARGQPGYPGRDGQPGMP 205
Cdd:PHA03169  93 SGSGSESVGSPTPSPSGSAEELASGLS----PENTSGSSPESPASHSPPPSPPSHPG----PHEPAPPESHNPSPNQQPS 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  206 GEMGPTGAPGDDGAPGASGMKGDDAEKP-VGRQGQRGQPGEQGPDgEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDGE 284
Cdd:PHA03169 165 SFLQPSHEDSPEEPEPPTSEPEPDSPGPpQSETPTSSPPPQSPPD-EPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPERE 243

                        170       180
                 ....*....|....*....|....*
gi 17566918  285 EGPRGPSGLPGKDAEYCKCPTRDDG 309
Cdd:PHA03169 244 GPPFPGHRSHSYTVVGWKPSTRPGG 268
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 173-227 8.16e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.78  E-value: 8.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17566918   173 GPQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGEMGPTGAPGDDGAPGASGMKG 227
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 130-312 1.69e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 43.04  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  130 EEGEQGPDGQDGVDGVPGFDGQDCPDVEQQPSqgcftcpqGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGEMG 209
Cdd:PHA03169  85 EERGQGGPSGSGSESVGSPTPSPSGSAEELAS--------GLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHN 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  210 PTGAPGDDGAPGASGMKGDD-AEKPVGRQGQRGQPGEQGPDGEEGPAGKDafegPPGVEGEvgvpgyqgSAGPDGEEGPR 288
Cdd:PHA03169 157 PSPNQQPSSFLQPSHEDSPEePEPPTSEPEPDSPGPPQSETPTSSPPPQS----PPDEPGE--------PQSPTPQQAPS 224

                        170       180
                 ....*....|....*....|....
gi 17566918  289 GPSGLPGKDAEYCKCPTRDDGGNS 312
Cdd:PHA03169 225 PNTQQAVEHEDEPTEPEREGPPFP 248
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 176-231 2.16e-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: 2.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17566918   176 GSQGAPGIRGMRGARGQPGYPGRDGQPGMPGEMGPTGAPGDDGAPGASGMKGDDAE 231
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 238-294 5.19e-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: 37.47  E-value: 5.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17566918   238 GQRGQPGEQGPDGEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDGEEGPRGPSGLP 294
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 168-214 6.01e-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: 37.47  E-value: 6.01e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 17566918   168 PQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGEMGPTGAP 214
Cdd:pfam01391  11 PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 235-290 7.39e-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: 7.39e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17566918   235 GRQGQRGQPGEQGPDGEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDGEEGPRGP 290
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 185-255 2.39e-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: 35.55  E-value: 2.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17566918   185 GMRGARGQPGYPGRDGQPGMPGEMGPTGAPGDDGAPGAsgmkgddaekpvgrQGQRGQPGEQGPDGEEGPA 255
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGP--------------PGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 124-292 2.85e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.58  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  124 PTGPDGEEGEQGPDGQDGVDGVPGFDGQDCPDVEQQPSQGCFTCPQGLPGPQGSQGAPGIRGMRGAR----GQPGYPGRD 199
Cdd:PRK07764 597 GEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASdggdGWPAKAGGA 676

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  200 GQPGMPGEMGPTGAPGDDGAPGASGMKGDDAEKPVGR-QGQRGQ-PGEQGPDGEEGPAGKDAFEGPPGVEGEVGVPGYQG 277
Cdd:PRK07764 677 APAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQaDDPAAQpPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA 756

                        170
                 ....*....|....*
gi 17566918  278 SAGPDGEEGPRGPSG 292
Cdd:PRK07764 757 QPPPPPAPAPAAAPA 771
PRK12678 PRK12678
transcription termination factor Rho; Provisional
 136-322 5.01e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 38.73  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  136 PDGQDGVDGVPGFDGQDCPDVEQQPSQGcftcPQGLPGPQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGEMGPTGAPG 215
Cdd:PRK12678  83 AAAAARQAEQPAAEAAAAKAEAAPAARA----AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918  216 DDGAPGASGMKGDDAEKP-VGRQGQRGQPGEQGPDGEEGPAGKDAFEGPPGVEGE-VGVPGYQGSAGPDGEEGPRGPSGL 293
Cdd:PRK12678 159 DAAERTEEEERDERRRRGdREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDrREERGRRDGGDRRGRRRRRDRRDA 238

                        170       180
                 ....*....|....*....|....*....
gi 17566918  294 PGKDAEYCKCPTRDDGGNSHRAWRRKHKR 322
Cdd:PRK12678 239 RGDDNREDRGDRDGDDGEGRGGRRGRRFR 267
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 75-285 6.35e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 38.44  E-value: 6.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918     75 GGYGATGTNAPEPQFPQGDKGPLPVPGLPFGPNVSGGSDRCQCTVENTCPTGPDGEEGEQgpdgqdgvDGVPGFDGQDCP 154
Cdd:TIGR00927  671 GETETKGENESEGEIPAERKGEQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEG--------EIETGEEGEEVE 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17566918    155 DVEQQPSQGCFTCPQglpgpQGSQGAPGIRGMRGARGQPGYPGRDGQPGMPGEMgpTGAPGDDGAPGASGMKGDDAEKPV 234
Cdd:TIGR00927  743 DEGEGEAEGKHEVET-----EGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEM--KGDEGAEGKVEHEGETEAGEKDEH 815

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 17566918    235 GRQGQRGQPGEQGPDgEEGPAGKDAFEGPPGVEGEVGVPGYQGSAGPDGEE 285
Cdd:TIGR00927  816 EGQSETQADDTEVKD-ETGEQELNAENQGEAKQDEKGVDGGGGSDGGDSEE 865
 
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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