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Conserved domains on  [gi|17535685|ref|NP_496589|]
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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

 Zoom to residue level

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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 ...
 267-438 1.46e-25

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: 108.45  E-value: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  267 PGAPGRPGPPGKAGANGLPGNSGKPTKRPCNPVTKPPCVPCPQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKG 346
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  347 RRGEKGKDGEPGAPGAPGENVKEVPAIPGPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPG 426
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                        170
                 ....*....|..
gi 17535685  427 RDGTHGHGGEKG 438
Cdd:NF038329 288 KDGQNGKDGLPG 299
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 12-64 1.03e-12

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


:

Pssm-ID: 198156  Cd Length: 53  Bit Score: 62.48  E-value: 1.03e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17535685     12 IIGYVTVTVSTLAIIALCVTLPIVHGYIKEVQHSMKIEMNQCQNNAKTLWTDV 64
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 ...
 267-438 1.46e-25

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: 108.45  E-value: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  267 PGAPGRPGPPGKAGANGLPGNSGKPTKRPCNPVTKPPCVPCPQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKG 346
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  347 RRGEKGKDGEPGAPGAPGENVKEVPAIPGPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPG 426
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                        170
                 ....*....|..
gi 17535685  427 RDGTHGHGGEKG 438
Cdd:NF038329 288 KDGQNGKDGLPG 299
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 283-438 6.57e-25

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: 106.53  E-value: 6.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  283 GLPGNSGKPTKRPCNPVTKPPCVPCPQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPG-----QKGRRGEKGKDGEP 357
Cdd:NF038329 168 GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGED 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  358 GAPGAPGENVKEVP-AIPGPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDGTHGHGGE 436
Cdd:NF038329 248 GPQGPDGPAGKDGPrGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327


                 ..
gi 17535685  437 KG 438
Cdd:NF038329 328 PG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 281-438 2.24e-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: 99.21  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  281 ANGLPGNSGKPTKRPCNPVTKPPCVPCPQGPLGPAGPAGPQGNLG--GPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEPG 358
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  359 APGAPGEnvkevpaiPGPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDGTHGHGGEKG 438
Cdd:NF038329 264 DRGEAGP--------DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 309-438 8.05e-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: 97.28  E-value: 8.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  309 QGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEPGAPGAPGEnvkevpaiPGPQGTPGPRGRQGP 388
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP--------AGKDGEAGAKGPAGE 190

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17535685  389 RGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDG--THGHGGEKG 438
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPG 242
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 310-457 7.00e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.51  E-value: 7.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  310 GPLGPAGPAGPQGNLGGPgvfGEKGPQGPVGAPGQKGRRGEKGKDGEPGAPGAPGEnvkevpaiPGPQGTPGPRGRQGPR 389
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQ---GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE--------AGPQGPAGKDGEAGAK 185

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535685  390 GAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDGTHGHGGEKGVCPKYCSADGGVFYEDGTR 457
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD 253
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 12-64 1.03e-12

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


Pssm-ID: 198156  Cd Length: 53  Bit Score: 62.48  E-value: 1.03e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17535685     12 IIGYVTVTVSTLAIIALCVTLPIVHGYIKEVQHSMKIEMNQCQNNAKTLWTDV 64
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 15-64 2.18e-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: 58.62  E-value: 2.18e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17535685    15 YVTVTVSTLAIIALCVTLPIVHGYIKEVQHSMKIEMNQCQNNAKTLWTDV 64
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 308-397 1.41e-10

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: 63.00  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  308 PQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEP---------GAPGAPGENvkevpaipGPQG 378
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPgkdgkdgqnGKDGLPGKD--------GKDG 320

                         90
                 ....*....|....*....
gi 17535685  379 TPGPRGRQGPRGAPGIPGK 397
Cdd:NF038329 321 QPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 375-429 3.81e-08

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: 49.80  E-value: 3.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17535685   375 GPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDG 429
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 316-425 9.13e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 45.06  E-value: 9.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  316 GPAGPQGNLGGPGvfGEKGPQGPVGAPGQKGRRGEKGKDG---EPGAPGAPGENVKEVPAIPGPQGTPGPRGRQG-PRGA 391
Cdd:PRK14959 376 GGASAPSGSAAEG--PASGGAATIPTPGTQGPQGTAPAAGmtpSSAAPATPAPSAAPSPRVPWDDAPPAPPRSGIpPRPA 453

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17535685  392 PGIPGKdglggdQGAPGEP----GADGEPGMDGVPGNP 425
Cdd:PRK14959 454 PRMPEA------SPVPGAPdsvaSASDAPPTLGDPSDT 485
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 281-374 2.44e-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: 43.36  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  281 ANGLPGNSGKPTKRPCNPVTKPPCVPCPQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEPGAP 360
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340

                         90
                 ....*....|....
gi 17535685  361 gAPgeNVKEVPAIP 374
Cdd:NF038329 341 -AP--KTPEVPQKP 351
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 267-438 1.46e-25

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: 108.45  E-value: 1.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  267 PGAPGRPGPPGKAGANGLPGNSGKPTKRPCNPVTKPPCVPCPQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKG 346
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  347 RRGEKGKDGEPGAPGAPGENVKEVPAIPGPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPG 426
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                        170
                 ....*....|..
gi 17535685  427 RDGTHGHGGEKG 438
Cdd:NF038329 288 KDGQNGKDGLPG 299
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 283-438 6.57e-25

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: 106.53  E-value: 6.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  283 GLPGNSGKPTKRPCNPVTKPPCVPCPQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPG-----QKGRRGEKGKDGEP 357
Cdd:NF038329 168 GEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpagdgQQGPDGDPGPTGED 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  358 GAPGAPGENVKEVP-AIPGPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDGTHGHGGE 436
Cdd:NF038329 248 GPQGPDGPAGKDGPrGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327


                 ..
gi 17535685  437 KG 438
Cdd:NF038329 328 PG 329
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 281-438 2.24e-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: 99.21  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  281 ANGLPGNSGKPTKRPCNPVTKPPCVPCPQGPLGPAGPAGPQGNLG--GPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEPG 358
Cdd:NF038329 184 AKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGpaGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRG 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  359 APGAPGEnvkevpaiPGPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDGTHGHGGEKG 438
Cdd:NF038329 264 DRGEAGP--------DGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDG 335
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 309-438 8.05e-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: 97.28  E-value: 8.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  309 QGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEPGAPGAPGEnvkevpaiPGPQGTPGPRGRQGP 388
Cdd:NF038329 119 KGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGP--------AGKDGEAGAKGPAGE 190

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17535685  389 RGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDG--THGHGGEKG 438
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPG 242
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 310-457 7.00e-20

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 91.51  E-value: 7.00e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  310 GPLGPAGPAGPQGNLGGPgvfGEKGPQGPVGAPGQKGRRGEKGKDGEPGAPGAPGEnvkevpaiPGPQGTPGPRGRQGPR 389
Cdd:NF038329 117 GEKGEPGPAGPAGPAGEQ---GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGE--------AGPQGPAGKDGEAGAK 185

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17535685  390 GAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDGTHGHGGEKGVCPKYCSADGGVFYEDGTR 457
Cdd:NF038329 186 GPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD 253
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 12-64 1.03e-12

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


Pssm-ID: 198156  Cd Length: 53  Bit Score: 62.48  E-value: 1.03e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17535685     12 IIGYVTVTVSTLAIIALCVTLPIVHGYIKEVQHSMKIEMNQCQNNAKTLWTDV 64
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 15-64 2.18e-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: 58.62  E-value: 2.18e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17535685    15 YVTVTVSTLAIIALCVTLPIVHGYIKEVQHSMKIEMNQCQNNAKTLWTDV 64
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 308-397 1.41e-10

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: 63.00  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  308 PQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEP---------GAPGAPGENvkevpaipGPQG 378
Cdd:NF038329 249 PQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPgkdgkdgqnGKDGLPGKD--------GKDG 320

                         90
                 ....*....|....*....
gi 17535685  379 TPGPRGRQGPRGAPGIPGK 397
Cdd:NF038329 321 QPGKDGLPGKDGKDGQPGK 339
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 375-429 3.81e-08

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: 49.80  E-value: 3.81e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17535685   375 GPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDG 429
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 310-366 9.21e-08

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: 48.64  E-value: 9.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17535685   310 GPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEPGAPGAPGEN 366
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 378-432 1.15e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 48.26  E-value: 1.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17535685   378 GTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDGTHG 432
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 374-425 3.60e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.72  E-value: 3.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17535685   374 PGPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNP 425
Cdd:pfam01391   6 PGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 308-363 4.83e-07

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 46.33  E-value: 4.83e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 17535685   308 PQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEPGAPGAP 363
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 384-438 5.83e-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: 43.64  E-value: 5.83e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17535685   384 GRQGPRGAPGIPGKDGLGGDQGAPGEPGADGEPGMDGVPGNPGRDGTHGHGGEKG 438
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 316-425 9.13e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 45.06  E-value: 9.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  316 GPAGPQGNLGGPGvfGEKGPQGPVGAPGQKGRRGEKGKDG---EPGAPGAPGENVKEVPAIPGPQGTPGPRGRQG-PRGA 391
Cdd:PRK14959 376 GGASAPSGSAAEG--PASGGAATIPTPGTQGPQGTAPAAGmtpSSAAPATPAPSAAPSPRVPWDDAPPAPPRSGIpPRPA 453

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 17535685  392 PGIPGKdglggdQGAPGEP----GADGEPGMDGVPGNP 425
Cdd:PRK14959 454 PRMPEA------SPVPGAPdsvaSASDAPPTLGDPSDT 485
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 281-374 2.44e-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: 43.36  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  281 ANGLPGNSGKPTKRPCNPVTKPPCVPCPQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEPGAP 360
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340

                         90
                 ....*....|....
gi 17535685  361 gAPgeNVKEVPAIP 374
Cdd:NF038329 341 -AP--KTPEVPQKP 351
PHA03247 PHA03247
large tegument protein UL36; Provisional
 285-430 5.42e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.54  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685   285 PGNSGKPTKRPCNPVTKPPCVPCPQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQKGRRGEKGKDGEPGAPGAPG 364
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPP 2680

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17535685   365 E------------NVKEVPAIPGPQGTPGPRGRQGPRGAPGIPGKDGLGGDQGA-PGEPGADGEPGMDGVPGNPGRDGT 430
Cdd:PHA03247 2681 QrprrraarptvgSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAlPAAPAPPAVPAGPATPGGPARPAR 2759
PHA03378 PHA03378
EBNA-3B; Provisional
 298-392 7.48e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 38.89  E-value: 7.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17535685  298 PVTKPPCVPCPQGPLGPAGPAGPQGNLGGPGVFGEKGPQGPVGAPGQ-KGRRGEKGKDGEPGAPGAPGENVKEVPAIPGP 376
Cdd:PHA03378 697 PPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRaRPPAAAPGRARPPAAAPGRARPPAAAPGAPTP 776

                         90
                 ....*....|....*...
gi 17535685  377 QGTP--GPRGRQGPRGAP 392
Cdd:PHA03378 777 QPPPqaPPAPQQRPRGAP 794
 
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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