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Conserved domains on  [gi|77404252|ref|NP_001029211.1|]
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collagen alpha-1(I) chain precursor [Bos taurus]

Protein Classification

VWC and COLFI domain-containing protein (domain architecture ID 11985870)

protein containing domains VWC, Collagen, DNA_pol3_gamma3, and COLFI

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1229-1462 8.47e-155

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


:

Pssm-ID: 307527  Cd Length: 230  Bit Score: 471.42  E-value: 8.47e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   1229 EVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQ 1308
Cdd:pfam01410    1 EVFASLKSLNQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCAKDAIKVFCNFETGETCIYPDPASIPR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   1309 KNWYISKNpkeKRHVWYGESMTGGFQFEYGGqGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALL 1388
Cdd:pfam01410   81 KNWWTKEN---KKHVWFGEFMNGGSQFSYVD-DSGPAVGVVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALR 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77404252   1389 LQGSNEIEIRAEGNSRFTYSVTYDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPACF 1462
Cdd:pfam01410  157 LLGSNDEELRAEGNSRFTYTVLEDGCSKRTGQWGKTVIEYRTQKTSRLPIVDIAPMDIGGADQEFGVEVGPVCF 230
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
40-95 1.45e-20

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


:

Pssm-ID: 278520  Cd Length: 57  Bit Score: 89.41  E-value: 1.45e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404252     40 CVQNGLRYHDRDVWKPVPCQICVCDNGNVLCDDVICDELkDCPNAK--VPTDECCPVC 95
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPPL-DCPNPRleIPPGECCPVC 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
235-294 6.94e-09

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: 189968  Cd Length: 60  Bit Score: 55.57  E-value: 6.94e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252    235 GKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGEN 294
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
DNA_pol3_gamma3 super family cl26386
DNA polymerase III subunits gamma and tau domain III; This domain family is found in bacteria, ...
448-639 7.72e-07

DNA polymerase III subunits gamma and tau domain III; This domain family is found in bacteria, and is approximately 110 amino acids in length. The family is found in association with pfam00004. Domains I-III are shared between the tau and the gamma subunits, while most of the DnaB-binding Domain IV and all of the alpha-interacting Domain V are unique to tau.


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 331207  Cd Length: 824  Bit Score: 53.84  E-value: 7.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   448 GEPGPTGIQGPPGPAGEEGKRGARGEPGPAGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGAPGPAGPKGSPGEAGR 527
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   528 PGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMgfPGPKGAAGEPGKAGERGVPGPPGAVG 607
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP--PQAAQGASAPSPAADDPVPLPPEPDD 747
                         170       180       190
                  ....*....|....*....|....*....|..
gi 77404252   608 PAGKDGEAGAQGPPGPAGPAGERGEQGPAGSP 639
Cdd:PRK07764  748 PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
700-758 1.81e-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: 189968  Cd Length: 60  Bit Score: 48.25  E-value: 1.81e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 77404252    700 GAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGAPGK 758
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
271-323 6.69e-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: 189968  Cd Length: 60  Bit Score: 43.63  E-value: 6.69e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 77404252    271 GLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGN 323
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGA 53
Rho super family cl28310
Transcription termination factor Rho [Transcription];
904-1110 8.79e-04

Transcription termination factor Rho [Transcription];


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 333130  Cd Length: 672  Bit Score: 43.74  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   904 GSKGPRGETGPAGRPGEVGPPGPPGPAGEKGAPGADGPAG-APGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPG 982
Cdd:PRK12678   61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAkAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRG 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   983 KQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKS 1062
Cdd:PRK12678  141 AARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGR 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 77404252  1063 GDRGETGPAGPAGPIGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHR 1110
Cdd:PRK12678  221 RDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD 268
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1229-1462 8.47e-155

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 307527  Cd Length: 230  Bit Score: 471.42  E-value: 8.47e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   1229 EVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQ 1308
Cdd:pfam01410    1 EVFASLKSLNQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCAKDAIKVFCNFETGETCIYPDPASIPR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   1309 KNWYISKNpkeKRHVWYGESMTGGFQFEYGGqGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALL 1388
Cdd:pfam01410   81 KNWWTKEN---KKHVWFGEFMNGGSQFSYVD-DSGPAVGVVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALR 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77404252   1389 LQGSNEIEIRAEGNSRFTYSVTYDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPACF 1462
Cdd:pfam01410  157 LLGSNDEELRAEGNSRFTYTVLEDGCSKRTGQWGKTVIEYRTQKTSRLPIVDIAPMDIGGADQEFGVEVGPVCF 230
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1227-1463 5.25e-136

Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 197483  Cd Length: 232  Bit Score: 421.11  E-value: 5.25e-136
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252    1227 DLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSV 1306
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252    1307 AQKNWYISKNPkekrHVWYGESMTGGFQFEYGGQGSDPaDVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKA 1386
Cdd:smart00038   81 PRKTWYSGKSK----HVWFGETMNGGFKFSYGDSEGPP-VGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKA 155
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77404252    1387 LLLQGSNEIEIRAEGNSRFTYSVTYDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPACFL 1463
Cdd:smart00038  156 LRLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
40-95 1.45e-20

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 89.41  E-value: 1.45e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404252     40 CVQNGLRYHDRDVWKPVPCQICVCDNGNVLCDDVICDELkDCPNAK--VPTDECCPVC 95
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPPL-DCPNPRleIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
40-95 4.62e-19

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 84.88  E-value: 4.62e-19
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 77404252      40 CVQNGLRYHDRDVWKPVPCQICVCDNG-NVLCDDVICDELKDCPNA--KVPTDECCPVC 95
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGtTVLCDPVECPPPPDCPNPerVKPPGECCPRC 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
235-294 6.94e-09

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: 189968  Cd Length: 60  Bit Score: 55.57  E-value: 6.94e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252    235 GKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGEN 294
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
448-639 7.72e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090  Cd Length: 824  Bit Score: 53.84  E-value: 7.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   448 GEPGPTGIQGPPGPAGEEGKRGARGEPGPAGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGAPGPAGPKGSPGEAGR 527
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   528 PGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMgfPGPKGAAGEPGKAGERGVPGPPGAVG 607
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP--PQAAQGASAPSPAADDPVPLPPEPDD 747
                         170       180       190
                  ....*....|....*....|....*....|..
gi 77404252   608 PAGKDGEAGAQGPPGPAGPAGERGEQGPAGSP 639
Cdd:PRK07764  748 PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
700-758 1.81e-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: 189968  Cd Length: 60  Bit Score: 48.25  E-value: 1.81e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 77404252    700 GAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGAPGK 758
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
508-561 5.52e-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: 189968  Cd Length: 60  Bit Score: 47.10  E-value: 5.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 77404252    508 GERGAPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQD 561
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAP 54
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
271-323 6.69e-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: 189968  Cd Length: 60  Bit Score: 43.63  E-value: 6.69e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 77404252    271 GLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGN 323
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGA 53
PRK12678 PRK12678
transcription termination factor Rho; Provisional
904-1110 8.79e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171  Cd Length: 672  Bit Score: 43.74  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   904 GSKGPRGETGPAGRPGEVGPPGPPGPAGEKGAPGADGPAG-APGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPG 982
Cdd:PRK12678   61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAkAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRG 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   983 KQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKS 1062
Cdd:PRK12678  141 AARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGR 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 77404252  1063 GDRGETGPAGPAGPIGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHR 1110
Cdd:PRK12678  221 RDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD 268
 
Name Accession Description Interval E-value
COLFI pfam01410
Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1229-1462 8.47e-155

Fibrillar collagen C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1 alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 307527  Cd Length: 230  Bit Score: 471.42  E-value: 8.47e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   1229 EVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQ 1308
Cdd:pfam01410    1 EVFASLKSLNQQIENIRSPDGSKKNPARTCRDLKLCHPDWKSGEYWIDPNQGCAKDAIKVFCNFETGETCIYPDPASIPR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   1309 KNWYISKNpkeKRHVWYGESMTGGFQFEYGGqGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALL 1388
Cdd:pfam01410   81 KNWWTKEN---KKHVWFGEFMNGGSQFSYVD-DSGPAVGVVQLTFLRLLSTEASQNITYHCKNSVAYMDQATGNLKKALR 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77404252   1389 LQGSNEIEIRAEGNSRFTYSVTYDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPACF 1462
Cdd:pfam01410  157 LLGSNDEELRAEGNSRFTYTVLEDGCSKRTGQWGKTVIEYRTQKTSRLPIVDIAPMDIGGADQEFGVEVGPVCF 230
COLFI smart00038
Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia ...
1227-1463 5.25e-136

Fibrillar collagens C-terminal domain; Found at C-termini of fibrillar collagens: Ephydatia muelleri procollagen EMF1alpha, vertebrate collagens alpha(1)III, alpha(1)II, alpha(2)V etc.


Pssm-ID: 197483  Cd Length: 232  Bit Score: 421.11  E-value: 5.25e-136
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252    1227 DLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSV 1306
Cdd:smart00038    1 DEEVFASLKSLNNQIEQLKSPTGSRKNPARTCKDLKLCHPEWKSGEYWVDPNQGCIRDAIKVFCNFETGETCVSPSPSSI 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252    1307 AQKNWYISKNPkekrHVWYGESMTGGFQFEYGGQGSDPaDVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKA 1386
Cdd:smart00038   81 PRKTWYSGKSK----HVWFGETMNGGFKFSYGDSEGPP-VGVVQLTFLRLLSTEAHQNITYHCKNSVAYMDEATGNLKKA 155
                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77404252    1387 LLLQGSNEIEIRAEGNSRFTYSVTYDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPACFL 1463
Cdd:smart00038  156 LRLRGSNDVELSAEGNSKFTYEVLEDGCQKRTGKWGKTVIEYRTKKTERLPIVDIAPSDIGGPDQEFGVEIGPVCFS 232
VWC pfam00093
von Willebrand factor type C domain; The high cutoff was used to prevent overlap with ...
40-95 1.45e-20

von Willebrand factor type C domain; The high cutoff was used to prevent overlap with pfam00094.


Pssm-ID: 278520  Cd Length: 57  Bit Score: 89.41  E-value: 1.45e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 77404252     40 CVQNGLRYHDRDVWKPVPCQICVCDNGNVLCDDVICDELkDCPNAK--VPTDECCPVC 95
Cdd:pfam00093    1 CVQNGVVYENGETWKPDLCTICTCDDGKVLCDKIICPPL-DCPNPRleIPPGECCPVC 57
VWC smart00214
von Willebrand factor (vWF) type C domain;
40-95 4.62e-19

von Willebrand factor (vWF) type C domain;


Pssm-ID: 214564  Cd Length: 59  Bit Score: 84.88  E-value: 4.62e-19
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*....
gi 77404252      40 CVQNGLRYHDRDVWKPVPCQICVCDNG-NVLCDDVICDELKDCPNA--KVPTDECCPVC 95
Cdd:smart00214    1 CVHNGRVYNDGETWKPDPCQICTCLDGtTVLCDPVECPPPPDCPNPerVKPPGECCPRC 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
235-294 6.94e-09

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: 189968  Cd Length: 60  Bit Score: 55.57  E-value: 6.94e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252    235 GKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGEN 294
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
448-639 7.72e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090  Cd Length: 824  Bit Score: 53.84  E-value: 7.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   448 GEPGPTGIQGPPGPAGEEGKRGARGEPGPAGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGAPGPAGPKGSPGEAGR 527
Cdd:PRK07764  590 PAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGW 669
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   528 PGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMgfPGPKGAAGEPGKAGERGVPGPPGAVG 607
Cdd:PRK07764  670 PAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQP--PQAAQGASAPSPAADDPVPLPPEPDD 747
                         170       180       190
                  ....*....|....*....|....*....|..
gi 77404252   608 PAGKDGEAGAQGPPGPAGPAGERGEQGPAGSP 639
Cdd:PRK07764  748 PPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
700-758 1.81e-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: 189968  Cd Length: 60  Bit Score: 48.25  E-value: 1.81e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 77404252    700 GAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGAPGK 758
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
244-303 1.90e-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: 189968  Cd Length: 60  Bit Score: 48.25  E-value: 1.90e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252    244 GPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPR 303
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
508-561 5.52e-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: 189968  Cd Length: 60  Bit Score: 47.10  E-value: 5.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 77404252    508 GERGAPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQD 561
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAP 54
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
403-609 3.20e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090  Cd Length: 824  Bit Score: 48.44  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   403 GIAGAPGFPGARGPSGPQGPSGPPGPKGNSGEPGAPGSKGDTgakgePGPTGIQGPPGPAGEEgkrGARGEPGPAGLPGP 482
Cdd:PRK07764  583 QVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAP-----AAPAPAGAAAAPAEAS---AAPAPGVAAPEHHP 654
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   483 PGERGGPGSRGFPGADGVAGPKGPAGERGAPGPAGPKGSPGEAGRPGEAGLPgakglTGSPGSPGPDGKTGPPGPAGQDG 562
Cdd:PRK07764  655 KHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPA-----ATPPAGQADDPAAQPPQAAQGAS 729
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 77404252   563 RPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPA 609
Cdd:PRK07764  730 APSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPP 776
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
715-765 4.97e-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: 189968  Cd Length: 60  Bit Score: 44.02  E-value: 4.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 77404252    715 GAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGAPGKDGVRGLT 765
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPP 51
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
271-323 6.69e-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: 189968  Cd Length: 60  Bit Score: 43.63  E-value: 6.69e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 77404252    271 GLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGN 323
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGA 53
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
500-684 1.60e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090  Cd Length: 824  Bit Score: 46.13  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   500 VAGPKGPAGERGAPGPAGPKGSPGEAGRPGEAGLPGAK-GLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGV 578
Cdd:PRK07764  587 VVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPaAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGG 666
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   579 MGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPG 658
Cdd:PRK07764  667 DGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPD 746
                         170       180
                  ....*....|....*....|....*.
gi 77404252   659 EQGVPGDLGAPGPSGARGERGFPGER 684
Cdd:PRK07764  747 DPPDPAGAPAQPPPPPAPAPAAAPAA 772
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
451-534 4.17e-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: 189968  Cd Length: 60  Bit Score: 41.32  E-value: 4.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252    451 GPTGIQGPPGPAGEEGKRGArgepgpaglpgppgerggpgsrgfPGADGVAGPKGPAGERGAPGPAGPKGSPGEAGRPGE 530
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGP------------------------PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGA 56

                   ....
gi 77404252    531 AGLP 534
Cdd:pfam01391   57 PGPP 60
PRK12678 PRK12678
transcription termination factor Rho; Provisional
904-1110 8.79e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171  Cd Length: 672  Bit Score: 43.74  E-value: 8.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   904 GSKGPRGETGPAGRPGEVGPPGPPGPAGEKGAPGADGPAG-APGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPG 982
Cdd:PRK12678   61 GGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAkAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRG 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252   983 KQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKS 1062
Cdd:PRK12678  141 AARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGR 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 77404252  1063 GDRGETGPAGPAGPIGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHR 1110
Cdd:PRK12678  221 RDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGRGGRRGRRFRD 268
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
535-594 3.62e-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: 189968  Cd Length: 60  Bit Score: 38.62  E-value: 3.62e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 77404252    535 GAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKA 594
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGPP 60
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
682-740 4.34e-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: 189968  Cd Length: 60  Bit Score: 38.24  E-value: 4.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 77404252    682 GERGVQGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGP 740
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
486-536 5.07e-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: 189968  Cd Length: 60  Bit Score: 37.85  E-value: 5.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 77404252    486 RGGPGSRGFPGADGVAGPKGPAGERGAPGPAGPKGSPGEAGRPGEAGLPGA 536
Cdd:pfam01391    9 PGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGAPGAPGP 59
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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