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Conserved domains on  [gi|17551258|ref|NP_510522|]
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Nematode cuticle collagen N-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

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 ...
 130-289 4.66e-16

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: 79.56  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  130 HDIPGGCIKCPEGPAGPPGPDGDSGPEGFPGLQGQSGPSGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDGQPGTTYFPGQ 209
Cdd:NF038329 111 QQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  210 AGQPGEPGWLGEPGLPGQHGEPGKDGEEGPQGAPGTPGNAGH--DAFPGTPGQAGKPGAPGKDANYCPCPQRQDDRTPPS 287
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270


                 ..
gi 17551258  288 SG 289
Cdd:NF038329 271 DG 272
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 3-55 2.96e-13

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


:

Pssm-ID: 198156  Cd Length: 53  Bit Score: 64.03  E-value: 2.96e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17551258      3 TLGYIGAGVCLLGVFSALCSIGHIVQDINNLRSEVEGRVDEFKVLADDTWDRL 55
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
236-424 6.86e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 38.70  E-value: 6.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  236 EEGPQGAPGTPGNAGHDAFPgTPGQAGKPGAPGKDANYCPCPQRQDDRTPPSSGTSAPQPPPrgsTAAPGTRAPPATRAP 315
Cdd:PRK12323 396 APAPAAPPAAPAAAPAAAAA-ARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAA---APAAAARPAAAGPRP 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  316 PATRAPPATTRAPPATTRPAPASQPPVREPETPDSGYPSPAPQEPAHPSPSYPSPSYPSPSYPSPSYPSPSYPSPSYPAE 395
Cdd:PRK12323 472 VAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAP 551

                        170       180       190
                 ....*....|....*....|....*....|
gi 17551258  396 -PAYSVPPPAKPEQPSGGYDAPSPPQTGSY 424
Cdd:PRK12323 552 rAAAATEPVVAPRPPRASASGLPDMFDGDW 581
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 130-289 4.66e-16

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: 79.56  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  130 HDIPGGCIKCPEGPAGPPGPDGDSGPEGFPGLQGQSGPSGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDGQPGTTYFPGQ 209
Cdd:NF038329 111 QQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  210 AGQPGEPGWLGEPGLPGQHGEPGKDGEEGPQGAPGTPGNAGH--DAFPGTPGQAGKPGAPGKDANYCPCPQRQDDRTPPS 287
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270


                 ..
gi 17551258  288 SG 289
Cdd:NF038329 271 DG 272
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 3-55 2.96e-13

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


Pssm-ID: 198156  Cd Length: 53  Bit Score: 64.03  E-value: 2.96e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17551258      3 TLGYIGAGVCLLGVFSALCSIGHIVQDINNLRSEVEGRVDEFKVLADDTWDRL 55
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-55 1.49e-12

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


Pssm-ID: 460226  Cd Length: 50  Bit Score: 61.71  E-value: 1.49e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17551258     6 YIGAGVCLLGVFSALCSIGHIVQDINNLRSEVEGRVDEFKVLADDTWDRL 55
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 211-267 7.23e-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: 43.25  E-value: 7.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17551258   211 GQPGEPGWLGEPGLPGQHGEPGKDGEEGPQGAPGTPGNAGHDAFPGTPGQAGKPGAP 267
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-216 1.59e-05

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: 46.82  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  105 GKRGDEGHPGDEGRRGasgislatthdipggcikcpegpagppgpdgDSGPEGFPGLQGQSGPSGEDGAPGQEGAPGDQG 184
Cdd:NF038329 260 GPRGDRGEAGPDGPDG-------------------------------KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG 308

                         90       100       110
                 ....*....|....*....|....*....|..
gi 17551258  185 EQGPKGYDGTDGPDGQPGTTYFPGQAGQPGEP 216
Cdd:NF038329 309 KDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 153-362 4.26e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 4.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  153 SGPEGFPGLQGQSGPSGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDGQPGTTYFPGQAGQPGEPGWLGEPGLPGQhgePG 232
Cdd:PRK07764 601 PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGG---AA 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  233 KDGEEGPQGAPGTPGNAGHDAFPGTPGQAGKPGAPGKDANYCPCPQRQDDRTPPSSGTSAPQPPPRGSTAAPGTRAPPAT 312
Cdd:PRK07764 678 PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQ 757

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17551258  313 RAPPATRAPPATTRAPPATTRPAPAsQPPVREPETPDSGYPSPAPQEPAH 362
Cdd:PRK07764 758 PPPPPAPAPAAAPAAAPPPSPPSEE-EEMAEDDAPSMDDEDRRDAEEVAM 806
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
236-424 6.86e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 38.70  E-value: 6.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  236 EEGPQGAPGTPGNAGHDAFPgTPGQAGKPGAPGKDANYCPCPQRQDDRTPPSSGTSAPQPPPrgsTAAPGTRAPPATRAP 315
Cdd:PRK12323 396 APAPAAPPAAPAAAPAAAAA-ARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAA---APAAAARPAAAGPRP 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  316 PATRAPPATTRAPPATTRPAPASQPPVREPETPDSGYPSPAPQEPAHPSPSYPSPSYPSPSYPSPSYPSPSYPSPSYPAE 395
Cdd:PRK12323 472 VAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAP 551

                        170       180       190
                 ....*....|....*....|....*....|
gi 17551258  396 -PAYSVPPPAKPEQPSGGYDAPSPPQTGSY 424
Cdd:PRK12323 552 rAAAATEPVVAPRPPRASASGLPDMFDGDW 581
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 130-289 4.66e-16

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: 79.56  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  130 HDIPGGCIKCPEGPAGPPGPDGDSGPEGFPGLQGQSGPSGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDGQPGTTYFPGQ 209
Cdd:NF038329 111 QQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  210 AGQPGEPGWLGEPGLPGQHGEPGKDGEEGPQGAPGTPGNAGH--DAFPGTPGQAGKPGAPGKDANYCPCPQRQDDRTPPS 287
Cdd:NF038329 191 KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDgqQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGP 270


                 ..
gi 17551258  288 SG 289
Cdd:NF038329 271 DG 272
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 3-55 2.96e-13

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


Pssm-ID: 198156  Cd Length: 53  Bit Score: 64.03  E-value: 2.96e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17551258      3 TLGYIGAGVCLLGVFSALCSIGHIVQDINNLRSEVEGRVDEFKVLADDTWDRL 55
Cdd:smart01088   1 LVAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 6-55 1.49e-12

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


Pssm-ID: 460226  Cd Length: 50  Bit Score: 61.71  E-value: 1.49e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 17551258     6 YIGAGVCLLGVFSALCSIGHIVQDINNLRSEVEGRVDEFKVLADDTWDRL 55
Cdd:pfam01484   1 YVAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 211-267 7.23e-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: 43.25  E-value: 7.23e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17551258   211 GQPGEPGWLGEPGLPGQHGEPGKDGEEGPQGAPGTPGNAGHDAFPGTPGQAGKPGAP 267
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 105-216 1.59e-05

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: 46.82  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  105 GKRGDEGHPGDEGRRGasgislatthdipggcikcpegpagppgpdgDSGPEGFPGLQGQSGPSGEDGAPGQEGAPGDQG 184
Cdd:NF038329 260 GPRGDRGEAGPDGPDG-------------------------------KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNG 308

                         90       100       110
                 ....*....|....*....|....*....|..
gi 17551258  185 EQGPKGYDGTDGPDGQPGTTYFPGQAGQPGEP 216
Cdd:NF038329 309 KDGLPGKDGKDGQPGKDGLPGKDGKDGQPGKP 340
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 153-362 4.26e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.75  E-value: 4.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  153 SGPEGFPGLQGQSGPSGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDGQPGTTYFPGQAGQPGEPGWLGEPGLPGQhgePG 232
Cdd:PRK07764 601 PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGG---AA 677

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  233 KDGEEGPQGAPGTPGNAGHDAFPGTPGQAGKPGAPGKDANYCPCPQRQDDRTPPSSGTSAPQPPPRGSTAAPGTRAPPAT 312
Cdd:PRK07764 678 PAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQ 757

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 17551258  313 RAPPATRAPPATTRAPPATTRPAPAsQPPVREPETPDSGYPSPAPQEPAH 362
Cdd:PRK07764 758 PPPPPAPAPAAAPAAAPPPSPPSEE-EEMAEDDAPSMDDEDRRDAEEVAM 806
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 167-361 5.77e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  167 PSGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDgQPGTTYFPGQAGQPGEPGWLGEPGLPGQHGEPGKDGEEGPQGAPGTP 246
Cdd:PRK07764 588 VGPAPGAAGGEGPPAPASSGPPEEAARPAAPA-APAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  247 GNAGHDAFPGTPGQAGKPGAPGkdanycPCPQRQDDRTPPSSGTSAPQPPPRGSTAAPGTRAPPATRAPPATRAPPATTR 326
Cdd:PRK07764 667 DGWPAKAGGAAPAAPPPAPAPA------APAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVP 740

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 17551258  327 APPATTRPAPASQPPVREPETPDSGYPSPAPQEPA 361
Cdd:PRK07764 741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPP 775
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 160-216 7.21e-05

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 40.17  E-value: 7.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17551258   160 GLQGQSGPSGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDGQPGTTYFPGQAGQPGEP 216
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 190-246 2.02e-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: 39.01  E-value: 2.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17551258   190 GYDGTDGPDGQPGTTYFPGQAGQPGEPGWLGEPGLPGQHGEPGKDGEEGPQGAPGTP 246
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 220-270 7.87e-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: 7.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 17551258   220 GEPGLPGQHGEPGKDGEEGPQGAPGTPGNAGHDAFPGTPGQAGKPGAPGKD 270
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
PHA03169 PHA03169
hypothetical protein; Provisional
 154-301 1.12e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 41.11  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  154 GPEGFPGLQGQSGPSGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDGQPGTTYFPGQAGQPGEPGWLG-------EPGLPG 226
Cdd:PHA03169 102 SPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQpshedspEEPEPP 181

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17551258  227 QhGEPGKDGEEGPQGAPGTPGNAGHDAfpgtPGQAGKPGAPGKDANYCPCPQRQDDRTPPSSGTSAPQPPPRGST 301
Cdd:PHA03169 182 T-SEPEPDSPGPPQSETPTSSPPPQSP----PDEPGEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHR 251
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 193-249 2.11e-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: 36.32  E-value: 2.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17551258   193 GTDGPDGQPGTTYFPGQAGQPGEPGWLGEPGLPGQHGEPGKDGEEGPQGAPGTPGNA 249
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
PHA03169 PHA03169
hypothetical protein; Provisional
 162-296 2.69e-03

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 39.95  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  162 QGQSGPSGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDGQPGTTYFPGQAGQPGEPGWLGEPGLPGQHGEPGKDGEEGPQG 241
Cdd:PHA03169  89 QGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQ 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 17551258  242 APGTPGNAGHDAFPGTPGQAGKPGAPGKDANYCPCPQRQDDRTPPSSGTSAPQPP 296
Cdd:PHA03169 169 PSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAP 223
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 196-250 5.59e-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: 5.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 17551258   196 GPDGQPGTTYFPGQAGQPGEPGWLGEPGLPGQHGEPGKDGEEGPQGAPGTPGNAG 250
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 154-202 6.35e-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: 6.35e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17551258   154 GPEGFPGLQGQSGPSGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDGQPG 202
Cdd:pfam01391   7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
236-424 6.86e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 38.70  E-value: 6.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  236 EEGPQGAPGTPGNAGHDAFPgTPGQAGKPGAPGKDANYCPCPQRQDDRTPPSSGTSAPQPPPrgsTAAPGTRAPPATRAP 315
Cdd:PRK12323 396 APAPAAPPAAPAAAPAAAAA-ARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAA---APAAAARPAAAGPRP 471

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  316 PATRAPPATTRAPPATTRPAPASQPPVREPETPDSGYPSPAPQEPAHPSPSYPSPSYPSPSYPSPSYPSPSYPSPSYPAE 395
Cdd:PRK12323 472 VAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAP 551

                        170       180       190
                 ....*....|....*....|....*....|
gi 17551258  396 -PAYSVPPPAKPEQPSGGYDAPSPPQTGSY 424
Cdd:PRK12323 552 rAAAATEPVVAPRPPRASASGLPDMFDGDW 581
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 207-418 6.87e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.81  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  207 PGQAGQPGEPGWLGEPGLPGQHGEP-GKDGEEGPQGAPGTPGNAGHDAFPGTPGQAGKPGAPGKDANYCPCPQRQDDRTP 285
Cdd:PRK07764 591 APGAAGGEGPPAPASSGPPEEAARPaAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWP 670

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  286 PSSGTSAPQPPPRGstAAPGTRAPPATRAPPATRAPPATTRAPPATTRPAPASQPPVREPETPDSGYPSPAPQEPAHPSP 365
Cdd:PRK07764 671 AKAGGAAPAAPPPA--PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDP 748

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17551258  366 SYPSPSYPSPSYPSPSYPSPSYPSPSYPAEPAYSVPPPAKPEQPSGGYDAPSP 418
Cdd:PRK07764 749 PDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDA 801
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 238-420 7.62e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.81  E-value: 7.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  238 GPQGAPGTPGNAGHDAFPGTPGQAGKPGAPGKDAnycpcpqrqdDRTPPSSGTSAPQPPPRGSTAAPGTRAPPATRAPPA 317
Cdd:PRK07764 589 GPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPA----------APAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVA 658

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258  318 TRAPPATTRAPPATTRPAPASQPPVREPETPDSGyPSPAPQEPAHPSPSYPSPSYPSPSYPSPSYPSPSYPSPSYPAEPA 397
Cdd:PRK07764 659 VPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAA-PAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADD 737

                        170       180
                 ....*....|....*....|...
gi 17551258  398 ySVPPPAKPEQPSGGYDAPSPPQ 420
Cdd:PRK07764 738 -PVPLPPEPDDPPDPAGAPAQPP 759
PHA03247 PHA03247
large tegument protein UL36; Provisional
 159-416 9.81e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 38.38  E-value: 9.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258   159 PGLQGQSGP-SGEDGAPGQEGAPGDQGEQGPKGYDGTDGPDGQPGTTYFPGQAGQPGEPGWLGEPGLPGqhgEPGKDGEE 237
Cdd:PHA03247 2717 SATPLPPGPaAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTR---PAVASLSE 2793

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258   238 GPQGAPGTPGNAGHDAfPGTPGQAGKPGAPGKDANYCPCPQRQDDRTPPSSGTSAPQPPPRGSTAaPGTRAPPATRAPPA 317
Cdd:PHA03247 2794 SRESLPSPWDPADPPA-AVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVA-PGGDVRRRPPSRSP 2871

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551258   318 TRAPPATTRAPPATTRPAPASQPPVREPETPDSGYPSPAPQEPAhpspsypsPSYPSPSYPSPSYPSPSYPSPSYPAEPA 397
Cdd:PHA03247 2872 AAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPP--------PPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943

                         250
                  ....*....|....*....
gi 17551258   398 YSVPPPAKPEQPSGGYDAP 416
Cdd:PHA03247 2944 APTTDPAGAGEPSGAVPQP 2962
 
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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