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Conserved domains on  [gi|115533544|ref|NP_001041295|]
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Nematode cuticle collagen N-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

cuticular collagen family protein( domain architecture ID 18387949)

cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Gene Ontology:  GO:0042302|GO:0005581
PubMed:  1916105|21421911

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 156-318 1.51e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 97.67  E-value: 1.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 156 AGKDGSNGRPGNPGEDADGDDYKPDAsqfcfdcPEAPAGPPGRPGPDGENGGAGEPGRDGLAGRpGARGSPGPRGPSGNP 235
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETG-------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGED 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 236 GADGPAGQLGPQG--GSNVAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGK 313
Cdd:NF038329 248 GPQGPDGPAGKDGprGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327


                 ....*
gi 115533544 314 EGSRG 318
Cdd:NF038329 328 PGKDG 332
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 65-117 3.11e-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: 65.95  E-value: 3.11e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 115533544    65 RFAFFGIAVSTVSTLTAIVAVPMLCLYLQSVSSSLQDEVNFCRVRATSLEGEL 117
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 ...
 156-318 1.51e-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: 97.67  E-value: 1.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 156 AGKDGSNGRPGNPGEDADGDDYKPDAsqfcfdcPEAPAGPPGRPGPDGENGGAGEPGRDGLAGRpGARGSPGPRGPSGNP 235
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETG-------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGED 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 236 GADGPAGQLGPQG--GSNVAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGK 313
Cdd:NF038329 248 GPQGPDGPAGKDGprGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327


                 ....*
gi 115533544 314 EGSRG 318
Cdd:NF038329 328 PGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 189-318 6.09e-21

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: 93.05  E-value: 6.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 189 PEAPAGPPGRPGPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQG-----GSNVAPSPAGEPGAP 263
Cdd:NF038329 136 PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGprgetGPAGEQGPAGPAGPD 215

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 264 GAQGPKGPPGAAGRPGR-----DGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGKEGSRG 318
Cdd:NF038329 216 GEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-318 4.66e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 87.27  E-value: 4.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 150 PGFDGSAGKDGSNGRPGNPGEDADGDDYKPD-----ASQFCFDCPEAPAGPPGRPGPDGENGGAGEPGRDGLAGRPGARG 224
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERgekgpAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 225 SPGPRGPSGNPGADGPAGQLGPQGGSNVAPS-PAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGKSG 303
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDgDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                        170
                 ....*....|....*...
gi 115533544 304 SDGQPGA---PGKEGSRG 318
Cdd:NF038329 288 KDGQNGKdglPGKDGKDG 305
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 207-318 9.37e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 86.50  E-value: 9.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 207 GAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQGgsnvAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGA 286
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG----ERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115533544 287 PGDQGENGPDGAPGKSGSDGQPGAPGKEGSRG 318
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAG 222
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 65-117 3.11e-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: 65.95  E-value: 3.11e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 115533544    65 RFAFFGIAVSTVSTLTAIVAVPMLCLYLQSVSSSLQDEVNFCRVRATSLEGEL 117
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 68-117 1.31e-10

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: 55.93  E-value: 1.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 115533544   68 FFGIAVSTVSTLTAIVAVPMLCLYLQSVSSSLQDEVNFCRVRATSLEGEL 117
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 239-301 1.15e-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: 50.57  E-value: 1.15e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533544  239 GPAGQLGPQGgsnvapsPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGK 301
Cdd:pfam01391   1 GPPGPPGPPG-------PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 164-317 2.85e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.91  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 164 RPGNPGEDADGDDYKPDASQFCFDCPEAPAGPPGRPGPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQ 243
Cdd:PRK07764 614 RPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAP 693

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 244 LGPQGGSNVAPSPAGEPGAPGAQGPKGPPGAAGRPGR------DGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGKEGSR 317
Cdd:PRK07764 694 AGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASApspaadDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 156-264 3.59e-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: 42.20  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 156 AGKDGSNGRPGNPGED-ADGDDYKPdasqfcfdcpeapagppGRPGPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGN 234
Cdd:NF038329 274 DGKDGERGPVGPAGKDgQNGKDGLP-----------------GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336

                         90       100       110
                 ....*....|....*....|....*....|
gi 115533544 235 PGADGPAGQLGPQgGSNVAPSPAGEPGAPG 264
Cdd:NF038329 337 PGKPAPKTPEVPQ-KPDTAPHTPKTPQIPG 365
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 206-316 8.26e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 37.67  E-value: 8.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 206 GGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPGAPGAQGPKgppgaAGRPGRD-GQP 284
Cdd:cd21118  244 GGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPE-----CNNPGNDvRMA 318

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115533544 285 GAPGDQGENGPDGAPGKSGSDGQPGAPGKEGS 316
Cdd:cd21118  319 GGGGSQGSKESSGSHGSNGGNGQAEAVGGLNT 350
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 156-318 1.51e-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: 97.67  E-value: 1.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 156 AGKDGSNGRPGNPGEDADGDDYKPDAsqfcfdcPEAPAGPPGRPGPDGENGGAGEPGRDGLAGRpGARGSPGPRGPSGNP 235
Cdd:NF038329 176 AGKDGEAGAKGPAGEKGPQGPRGETG-------PAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGED 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 236 GADGPAGQLGPQG--GSNVAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGK 313
Cdd:NF038329 248 GPQGPDGPAGKDGprGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327


                 ....*
gi 115533544 314 EGSRG 318
Cdd:NF038329 328 PGKDG 332
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 189-318 6.09e-21

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: 93.05  E-value: 6.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 189 PEAPAGPPGRPGPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQG-----GSNVAPSPAGEPGAP 263
Cdd:NF038329 136 PRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGprgetGPAGEQGPAGPAGPD 215

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 264 GAQGPKGPPGAAGRPGR-----DGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGKEGSRG 318
Cdd:NF038329 216 GEAGPAGEDGPAGPAGDgqqgpDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 150-318 4.66e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 87.27  E-value: 4.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 150 PGFDGSAGKDGSNGRPGNPGEDADGDDYKPD-----ASQFCFDCPEAPAGPPGRPGPDGENGGAGEPGRDGLAGRPGARG 224
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERgekgpAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 225 SPGPRGPSGNPGADGPAGQLGPQGGSNVAPS-PAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGKSG 303
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDgDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAG 287

                        170
                 ....*....|....*...
gi 115533544 304 SDGQPGA---PGKEGSRG 318
Cdd:NF038329 288 KDGQNGKdglPGKDGKDG 305
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 207-318 9.37e-19

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 86.50  E-value: 9.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 207 GAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQGgsnvAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGA 286
Cdd:NF038329 115 GDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQG----ERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115533544 287 PGDQGENGPDGAPGKSGSDGQPGAPGKEGSRG 318
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAG 222
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 65-117 3.11e-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: 65.95  E-value: 3.11e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 115533544    65 RFAFFGIAVSTVSTLTAIVAVPMLCLYLQSVSSSLQDEVNFCRVRATSLEGEL 117
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 68-117 1.31e-10

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: 55.93  E-value: 1.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 115533544   68 FFGIAVSTVSTLTAIVAVPMLCLYLQSVSSSLQDEVNFCRVRATSLEGEL 117
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 239-301 1.15e-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: 50.57  E-value: 1.15e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533544  239 GPAGQLGPQGgsnvapsPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGK 301
Cdd:pfam01391   1 GPPGPPGPPG-------PPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 258-317 1.71e-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: 50.18  E-value: 1.71e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544  258 GEPGAPGAQGPKGPPGAagrPGRDGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGKEGSR 317
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGP---PGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 256-311 2.34e-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: 2.34e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 115533544  256 PAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGKSGSDGQPGAP 311
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 254-308 1.84e-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: 47.10  E-value: 1.84e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 115533544  254 PSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGKSGSDGQP 308
Cdd:pfam01391   3 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 164-317 2.85e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.91  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 164 RPGNPGEDADGDDYKPDASQFCFDCPEAPAGPPGRPGPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQ 243
Cdd:PRK07764 614 RPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAP 693

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 244 LGPQGGSNVAPSPAGEPGAPGAQGPKGPPGAAGRPGR------DGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGKEGSR 317
Cdd:PRK07764 694 AGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASApspaadDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAA 773
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 215-330 6.43e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 50.83  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 215 GLAGRPGARGSPGPrgPSGNPGADGPAGQLGPQGGSNvAPSPAGEPGAPGAQGPKGPPgaAGRPGRDGQPGAPGDQGeNG 294
Cdd:PRK14959 376 GGASAPSGSAAEGP--ASGGAATIPTPGTQGPQGTAP-AAGMTPSSAAPATPAPSAAP--SPRVPWDDAPPAPPRSG-IP 449

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 115533544 295 PDGAPGKSGSDGQPGAPGKEGSRGGC--DHCPPPRTAP 330
Cdd:PRK14959 450 PRPAPRMPEASPVPGAPDSVASASDAppTLGDPSDTAE 487
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 267-318 1.45e-06

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 44.79  E-value: 1.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 115533544  267 GPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGKEGSRG 318
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 155-299 2.90e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.83  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 155 SAGKDGSNGRPGNPGEDADGDDYKPDASqfcfDCPEAPAGPPGRPGPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGN 234
Cdd:PRK07764 636 PAEASAAPAPGVAAPEHHPKHVAVPDAS----DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPA 711

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533544 235 PGADGPAGQLGPQGGSNVAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAP 299
Cdd:PRK07764 712 GQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPP 776
PHA03378 PHA03378
EBNA-3B; Provisional
 222-330 6.29e-06

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 47.75  E-value: 6.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 222 ARGSPGPRGPSGNPGADGPAGQLG-PQGGSNVAPSPAGEPGA--PGAQGPKGPPGAAGRPGRDGQP-GAPGDQgeNGPDG 297
Cdd:PHA03378 692 GTMQPPPRAPTPMRPPAAPPGRAQrPAAATGRARPPAAAPGRarPPAAAPGRARPPAAAPGRARPPaAAPGRA--RPPAA 769

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 115533544 298 APGKSGSDGQPGAP--GKEGSRGGCDHCPPPRTAP 330
Cdd:PHA03378 770 APGAPTPQPPPQAPpaPQQRPRGAPTPQPPPQAGP 804
PHA03169 PHA03169
hypothetical protein; Provisional
 204-319 1.69e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.12  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 204 ENGGAGEPGRDGL---AGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPGAPGA--QGPKGPPGAAGRP 278
Cdd:PHA03169 106 SPSGSAEELASGLspeNTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSheDSPEEPEPPTSEP 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 115533544 279 GRDGQPGAPGDQGENGPDGA-----PGKSGSDGQPGAPGKEGSRGG 319
Cdd:PHA03169 186 EPDSPGPPQSETPTSSPPPQsppdePGEPQSPTPQQAPSPNTQQAV 231
PHA03169 PHA03169
hypothetical protein; Provisional
 155-306 2.01e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 46.12  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 155 SAGKDGSNGRPGNPGEDADGDDYKPDASqfcfDCPEAPAGPPGRPGPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGN 234
Cdd:PHA03169  88 GQGGPSGSGSESVGSPTPSPSGSAEELA----SGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQP 163

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533544 235 PGADGPAGQLGPQGGSnvapSPAGEPGAPGAQGPKGPPGAAGRPGRDGqPGAPGDQGENGPDGAPGKSGSDG 306
Cdd:PHA03169 164 SSFLQPSHEDSPEEPE----PPTSEPEPDSPGPPQSETPTSSPPPQSP-PDEPGEPQSPTPQQAPSPNTQQA 230
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 217-315 2.60e-05

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 45.77  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 217 AGRPGARGSPGPRG-PSGNPGADGPAGQLGpqGGSNVAPSPAGEPGAPGAQGPKGPPGaagrpgrdgqPGAPGDQgengP 295
Cdd:PHA03264 272 GGSPAPPGDDRPEAkPEPGPVEDGAPGRET--GGEGEGPEPAGRDGAAGGEPKPGPPR----------PAPDADR----P 335

                         90       100
                 ....*....|....*....|
gi 115533544 296 DGAPGKSGSDGQPGAPGKEG 315
Cdd:PHA03264 336 EGWPSLEAITFPPPTPATPA 355
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 183-330 2.71e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 183 QFCFDCPEAPAGPPGRPGPDGENGGAGEPGRdglAGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPGA 262
Cdd:PRK07764 581 DWQVEAVVGPAPGAAGGEGPPAPASSGPPEE---AARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHV 657

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533544 263 PGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGKEGSRGGCDHCPPPRTAP 330
Cdd:PRK07764 658 AVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAA 725
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 207-316 1.09e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 207 GAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSnvAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGA 286
Cdd:PRK07764 384 RLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAA--APQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAA 461

                         90       100       110
                 ....*....|....*....|....*....|
gi 115533544 287 PGDQGENGPDGAPGKSGSDGQPGAPGKEGS 316
Cdd:PRK07764 462 PSAQPAPAPAAAPEPTAAPAPAPPAAPAPA 491
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 189-331 1.40e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.44  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 189 PEAPAGPPGRPGPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPGAPGAQGP 268
Cdd:PRK07764 621 PAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQ 700

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533544 269 KGPPGAAGRPGRDGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGKEGSRGGCDHCPPPRTAPG 331
Cdd:PRK07764 701 PAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPA 763
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 206-311 2.78e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 206 GGAGEPGrdglAGRPGARGSPG----PRGPSGNPGADGPAGQLGPQGGSnvAPSPAGEPGAPGAQGPKGPPGAAGRPGRD 281
Cdd:PRK07764 389 GGAGAPA----AAAPSAAAAAPaaapAPAAAAPAAAAAPAPAAAPQPAP--APAPAPAPPSPAGNAPAGGAPSPPPAAAP 462

                         90       100       110
                 ....*....|....*....|....*....|
gi 115533544 282 GQPGAPGDQGENGPDGAPGKSGSDGQPGAP 311
Cdd:PRK07764 463 SAQPAPAPAAAPEPTAAPAPAPPAAPAPAA 492
PHA03169 PHA03169
hypothetical protein; Provisional
 209-319 3.02e-04

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 42.27  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 209 GEPGRDGlAGRPGARGSPGPRGPSGNPGADGP--AGQLGPQGGSNVAP------SPAGEPGAPGAQGPKGPPGAAGRPGR 280
Cdd:PHA03169  82 GEKEERG-QGGPSGSGSESVGSPTPSPSGSAEelASGLSPENTSGSSPespashSPPPSPPSHPGPHEPAPPESHNPSPN 160

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 115533544 281 DGQPGAPGDQGENGPDGAPGKSGSDGQPGAPGKEGSRGG 319
Cdd:PHA03169 161 QQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPT 199
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 156-264 3.59e-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: 42.20  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 156 AGKDGSNGRPGNPGED-ADGDDYKPdasqfcfdcpeapagppGRPGPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGN 234
Cdd:NF038329 274 DGKDGERGPVGPAGKDgQNGKDGLP-----------------GKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQ 336

                         90       100       110
                 ....*....|....*....|....*....|
gi 115533544 235 PGADGPAGQLGPQgGSNVAPSPAGEPGAPG 264
Cdd:NF038329 337 PGKPAPKTPEVPQ-KPDTAPHTPKTPQIPG 365
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 213-330 3.74e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 213 RDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPgAPGAQGPKGPPGAAGRPGRDGQPG-APGDQG 291
Cdd:PRK07764 384 RLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQP-APAPAPAPAPPSPAGNAPAGGAPSpPPAAAP 462

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 115533544 292 ENGPDGAPGKSGSDGQPGAPGKEGSRGGCDHCPPPRTAP 330
Cdd:PRK07764 463 SAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPA 501
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 197-330 4.16e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 197 GRPGPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGqLGPQGGSNVAPSPAGEPGAPGAQGPKGPPGAAG 276
Cdd:PRK07764 620 APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDG-GDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAP 698

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 115533544 277 RPGRDGQPGAPgdqgenGPDGAPGKSGSDGQPGAPGKEGSRGGCDHCPPPRTAP 330
Cdd:PRK07764 699 AQPAPAPAATP------PAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 215-329 4.98e-04

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 41.43  E-value: 4.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 215 GLAGRPGARGSPG----PRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPGAPGAQGpkgppGAAGRPGRDGQPGAPGDQ 290
Cdd:PRK13875 293 GLAAGGGAAAAGGaaaaARGGAAAAGGASSAYSAGAAGGSGAAGVAAGLGGVARAGA-----SAAASPLRRAASRAAESM 367

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 115533544 291 GENGPDGAPGKSGSDGQPGAPGKEGSRGGcdhcPPPRTA 329
Cdd:PRK13875 368 KSSFRAGARSTGGGAGGAAAAAAAGAAAA----GPPAWA 402
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 217-331 5.75e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 5.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 217 AGRPGARGSPGPRGPSGNPGADGPAgqlgPQGGSNVAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPD 296
Cdd:PRK07764 390 GAGAPAAAAPSAAAAAPAAAPAPAA----AAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQ 465

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 115533544 297 GAPGKSGSDGQPGAPGKEGSRGGCDHCPPPRTAPG 331
Cdd:PRK07764 466 PAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAP 500
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 217-311 1.10e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 217 AGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGAPGDQGENGPD 296
Cdd:PRK07764 412 PAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPA 491

                         90
                 ....*....|....*
gi 115533544 297 GAPGKSGSDGQPGAP 311
Cdd:PRK07764 492 AAPAAPAAPAAPAGA 506
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
 240-330 1.61e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 40.05  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 240 PAGQLGPQGGSNVAPSPAGEPGA----------PGAQGPKGPPGAAGRPGRDGQPGAPgdqgenGPDGAPGKSGS-DGQP 308
Cdd:PRK14959 367 PVESLRPSGGGASAPSGSAAEGPasggaatiptPGTQGPQGTAPAAGMTPSSAAPATP------APSAAPSPRVPwDDAP 440

                         90       100
                 ....*....|....*....|..
gi 115533544 309 GAPGKEGSrggcdhcpPPRTAP 330
Cdd:PRK14959 441 PAPPRSGI--------PPRPAP 454
PHA03169 PHA03169
hypothetical protein; Provisional
 204-295 1.75e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.95  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 204 ENGGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSNVAP-SPAGEPGAPGAQGPKGPPGAAGRPGRDG 282
Cdd:PHA03169 154 SHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPqSPPDEPGEPQSPTPQQAPSPNTQQAVEH 233

                         90
                 ....*....|...
gi 115533544 283 QPGAPGDQGENGP 295
Cdd:PHA03169 234 EDEPTEPEREGPP 246
PHA03378 PHA03378
EBNA-3B; Provisional
 217-307 1.79e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.05  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 217 AGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPGAPG-AQGPKGPPGAAGRPgRDG-----QPGAPGDQ 290
Cdd:PHA03378 728 AAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTpQPPPQAPPAPQQRP-RGAptpqpPPQAGPTS 806

                         90
                 ....*....|....*..
gi 115533544 291 GENGPDGAPGKSGSDGQ 307
Cdd:PHA03378 807 MQLMPRAAPGQQGPTKQ 823
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 207-330 2.72e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 39.77  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544  207 GAGEPGRDGLAGRPgaRGSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPGA 286
Cdd:PHA03307  776 EPAEPQRGAGSSPP--VRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPGAAARPPPARSSES 853

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 115533544  287 PGDQGENGPDGAPGKSGSDGQPGAPGKE---GSRGGCDHCPPPRTAP 330
Cdd:PHA03307  854 SKSKPAAAGGRARGKNGRRRPRPPEPRArpgAAAPPKAAAAAPPAGA 900
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 200-248 2.78e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 35.55  E-value: 2.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 115533544  200 GPDGENGGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQG 248
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
206-330 2.81e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 39.45  E-value: 2.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 206 GGAGEPGRDGLAGRPGARGSPGPRGPSGnPGADGPAGQLGPQGGSNVAPSP-------AGEPGAPGAQGPKGPPGAAGRP 278
Cdd:PRK07003 363 TGGGAPGGGVPARVAGAVPAPGARAAAA-VGASAVPAVTAVTGAAGAALAPkaaaaaaATRAEAPPAAPAPPATADRGDD 441

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 115533544 279 GRDGQPGAPGDQGENGPDGAPGKSgSDGQPGAPGKEGSRGGCDHCPPPRTAP 330
Cdd:PRK07003 442 AADGDAPVPAKANARASADSRCDE-RDAQPPADSGSASAPASDAPPDAAFEP 492
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 204-243 3.16e-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: 3.16e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 115533544  204 ENGGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQ 243
Cdd:pfam01391  17 PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
motB PRK05996
MotB family protein;
205-296 4.91e-03

MotB family protein;


Pssm-ID: 235665 [Multi-domain]  Cd Length: 423  Bit Score: 38.53  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 205 NGGAGEPGR-DGLAGRPGAR-----------------GSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPGAPGAQ 266
Cdd:PRK05996 159 DGGAAQSGPaTGADGGEAYRdpfdpdfwskqvevttaGDLLPPGQAREQAQGAKSATAAPATVPQAAPLPQAQPKKAATE 238

                         90       100       110
                 ....*....|....*....|....*....|
gi 115533544 267 GPKGPPGAAGRPGRDGQPGAPGDQGENGPD 296
Cdd:PRK05996 239 EELIADAKKAATGEPAANAAKAAKPEPMPD 268
PHA03270 PHA03270
envelope glycoprotein C; Provisional
 224-284 5.12e-03

envelope glycoprotein C; Provisional


Pssm-ID: 165528 [Multi-domain]  Cd Length: 466  Bit Score: 38.38  E-value: 5.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533544 224 GSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPA---GEPGAPGAQGPKGPPGAAGRPGRDGQP 284
Cdd:PHA03270  22 GAGAPRGAVSNASEAPTSGSPGSAEGPRTTPTPTrgkGTPTGPASPPKSGPPKSPPAPFRCKRP 85
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 204-246 5.13e-03

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 34.78  E-value: 5.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 115533544  204 ENGGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGP 246
Cdd:pfam01391  14 PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
PRK13875 PRK13875
conjugal transfer protein TrbL; Provisional
 206-308 7.87e-03

conjugal transfer protein TrbL; Provisional


Pssm-ID: 237537  Cd Length: 440  Bit Score: 37.97  E-value: 7.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 206 GGAGEPGRDGlAGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSnvAPSPAGEPGAPGAQGPKGPPGAAGRPGRDGQPG 285
Cdd:PRK13875 304 GGAAAAARGG-AAAAGGASSAYSAGAAGGSGAAGVAAGLGGVARA--GASAAASPLRRAASRAAESMKSSFRAGARSTGG 380

                         90       100
                 ....*....|....*....|...
gi 115533544 286 APGDqgenGPDGAPGKSGSDGQP 308
Cdd:PRK13875 381 GAGG----AAAAAAAGAAAAGPP 399
dermokine cd21118
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 206-316 8.26e-03

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


Pssm-ID: 411053 [Multi-domain]  Cd Length: 495  Bit Score: 37.67  E-value: 8.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533544 206 GGAGEPGRDGLAGRPGARGSPGPRGPSGNPGADGPAGQLGPQGGSNVAPSPAGEPGAPGAQGPKgppgaAGRPGRD-GQP 284
Cdd:cd21118  244 GGQGNGGNNGSSSSNSGNSGGSNGGSSGNSGSGSGGSSSGGSNGWGGSSSSGGSGGSGGGNKPE-----CNNPGNDvRMA 318

                         90       100       110
                 ....*....|....*....|....*....|..
gi 115533544 285 GAPGDQGENGPDGAPGKSGSDGQPGAPGKEGS 316
Cdd:cd21118  319 GGGGSQGSKESSGSHGSNGGNGQAEAVGGLNT 350
 
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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