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Conserved domains on  [gi|624871|dbj|BAA07368|]
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a1(XIX) collagen chain precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-233 1.01e-56

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


:

Pssm-ID: 214560  Cd Length: 184  Bit Score: 194.11  E-value: 1.01e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871        50 NKLEVSGFDLGD-SFSLRRAFC-ESDKTCFKLGS-ALLIRDTIKIFPKGLPEEYSVAAMFRVRrnaKKERWFLWQVLNQQ 126
Cdd:smart00210    1 GQDLLQVFDLPSlSFAIRQVVGpEPGSPAYRLGDpALVPQPTRDLFPSGLPEDFSLLTTFRQT---PKSRGVLFAIYDAQ 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871       127 NIPQISIVVDGGKKVVEFMFQATEGDVLNYIFRNrelRPLFDRQWHKLGISIQSQVISLYMDCNLIARRQTDEKD--TVD 204
Cdd:smart00210   78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGqpPID 154

                           170       180
                    ....*....|....*....|....*....
gi 624871       205 FHGRTVIATRASDGKPVDIELHQLKIYCS 233
Cdd:smart00210  155 TDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 446-666 2.31e-29

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


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 122.71  E-value: 2.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     446 NKGNDEHEAGGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEKGDRGEPGVIGSQGVKGEPGDPGPPGLIGSPGLKG 525
Cdd:NF038329  107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     526 QQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEKgdPGGIIGPPGLPGPKGEAGPPGKSlpGEPGLDGNPGAPGPRGPK 605
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA--GEDGPAGPAGDGQQGPDGDPGPT--GEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624871     606 GERGLPGVHGSPGDIGPQG-IGIPGRTGAQGPAGEPGIQGPRGLPGLPGTPGTPGNDGVPGR 666
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGpVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 744-995 9.20e-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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 90.35  E-value: 9.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     744 GPKGSKGERGYPGIPGEKGDEGLQGIPGIPGAPGPTGPPGLMGRTGHPGPTGAKGEKGSDGPPGKPGppgppgipfnern 823
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG------------- 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     824 gmsslykikggvnvpsypgppgppgpkgdpgpvgEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGmSGKPGAPGPPGVPGE 903
Cdd:NF038329  187 ----------------------------------PAGEKGPQGPRGETGPAGEQGPAGPAGPDG-EAGPAGEDGPAGPAG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     904 PGERGPVGDIGFPGPEGPSGKPGINGKDGIPGAEGIMGKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMG 983
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                         250
                  ....*....|..
gi 624871     984 PPGNKGSMGSPG 995
Cdd:NF038329  312 LPGKDGKDGQPG 323
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 291-414 4.98e-07

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: 53.76  E-value: 4.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     291 KGEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQkGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKGVLGPHG 370
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 624871     371 PPGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKT 414
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD 319
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-233 1.01e-56

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 194.11  E-value: 1.01e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871        50 NKLEVSGFDLGD-SFSLRRAFC-ESDKTCFKLGS-ALLIRDTIKIFPKGLPEEYSVAAMFRVRrnaKKERWFLWQVLNQQ 126
Cdd:smart00210    1 GQDLLQVFDLPSlSFAIRQVVGpEPGSPAYRLGDpALVPQPTRDLFPSGLPEDFSLLTTFRQT---PKSRGVLFAIYDAQ 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871       127 NIPQISIVVDGGKKVVEFMFQATEGDVLNYIFRNrelRPLFDRQWHKLGISIQSQVISLYMDCNLIARRQTDEKD--TVD 204
Cdd:smart00210   78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGqpPID 154

                           170       180
                    ....*....|....*....|....*....
gi 624871       205 FHGRTVIATRASDGKPVDIELHQLKIYCS 233
Cdd:smart00210  155 TDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 446-666 2.31e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 122.71  E-value: 2.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     446 NKGNDEHEAGGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEKGDRGEPGVIGSQGVKGEPGDPGPPGLIGSPGLKG 525
Cdd:NF038329  107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     526 QQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEKgdPGGIIGPPGLPGPKGEAGPPGKSlpGEPGLDGNPGAPGPRGPK 605
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA--GEDGPAGPAGDGQQGPDGDPGPT--GEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624871     606 GERGLPGVHGSPGDIGPQG-IGIPGRTGAQGPAGEPGIQGPRGLPGLPGTPGTPGNDGVPGR 666
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGpVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 332-666 2.90e-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: 98.05  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     332 FEGSKGETGEKGEQGEKGDPalaglngenglkgvlgphgppGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRr 411
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQ---------------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP- 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     412 gktgppgkpgppgppgppgiqgihQTLGGDDNKDnkgndeheagGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEK 491
Cdd:NF038329  173 ------------------------QGPAGKDGEA----------GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     492 GDRGEPGVIGSQGVKGEpgdpgppgliGSPGLKGQQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEkgdpggiigppg 571
Cdd:NF038329  219 GPAGEDGPAGPAGDGQQ----------GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK------------ 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     572 lpgpKGEAGPPGKslPGEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDIGPQGI-GIPGRTGAQGPAGEPGIQGPRgLPG 650
Cdd:NF038329  277 ----DGERGPVGP--AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKdGLPGKDGKDGQPGKPAPKTPE-VPQ 349

                         330
                  ....*....|....*..
gi 624871     651 LPGT-PGTPGNDGVPGR 666
Cdd:NF038329  350 KPDTaPHTPKTPQIPGQ 366
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 744-995 9.20e-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: 90.35  E-value: 9.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     744 GPKGSKGERGYPGIPGEKGDEGLQGIPGIPGAPGPTGPPGLMGRTGHPGPTGAKGEKGSDGPPGKPGppgppgipfnern 823
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG------------- 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     824 gmsslykikggvnvpsypgppgppgpkgdpgpvgEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGmSGKPGAPGPPGVPGE 903
Cdd:NF038329  187 ----------------------------------PAGEKGPQGPRGETGPAGEQGPAGPAGPDG-EAGPAGEDGPAGPAG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     904 PGERGPVGDIGFPGPEGPSGKPGINGKDGIPGAEGIMGKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMG 983
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                         250
                  ....*....|..
gi 624871     984 PPGNKGSMGSPG 995
Cdd:NF038329  312 LPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 870-1098 3.32e-18

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: 88.81  E-value: 3.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     870 FPGVKGDRGPAGPPGIAGmsgkpgapgppgvpgepgERGPVGDIGFPGPEGPSGKPGINGKDGIPGAEGIMGKPGDRGPK 949
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAG------------------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     950 GERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPGHQGPPGSPGIPGIPADAvsfeeikkyinqevlri 1029
Cdd:NF038329  177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG----------------- 239

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 624871    1030 feermavflsqlkLPAAMLAAQAYGRPGPPGKDGLPGPPGDPGPQGYRGQKGERGEPGI----GLPGSPGLPG 1098
Cdd:NF038329  240 -------------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPagkdGQNGKDGLPG 299
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 858-1101 1.61e-12

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: 71.09  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     858 EPGAMGLPGLEGFPGVKGDRGPAGPPGIAGMSGKPGAPGPPGVPGEPGERGPVG---------DIGFPGPEGPSGKPGIN 928
Cdd:NF038329  121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGpagkdgeagAKGPAGEKGPQGPRGET 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     929 GKDGIPGAEGIMGKPGDRGPKGERGDQGIPGDrGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPGhqGPPGSPGIPGI 1008
Cdd:NF038329  201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG--EAGPDGPDGKD 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    1009 PADAVSFEEIKKYINQEVlrifeermavflsqlklpaaMLAAQAyGRPGPPGKDGLPgppgdpgpqgyrGQKGERGEPG- 1087
Cdd:NF038329  278 GERGPVGPAGKDGQNGKD--------------------GLPGKD-GKDGQNGKDGLP------------GKDGKDGQPGk 324

                         250
                  ....*....|....*..
gi 624871    1088 ---IGLPGSPGLPGTSA 1101
Cdd:NF038329  325 dglPGKDGKDGQPGKPA 341
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 291-414 4.98e-07

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: 53.76  E-value: 4.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     291 KGEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQkGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKGVLGPHG 370
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 624871     371 PPGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKT 414
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD 319
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 292-423 1.16e-06

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: 52.60  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     292 GEAGLPGAPGSPGQKGHKGEPGENGlHGAPGFPGQKGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKGVLGPHGP 371
Cdd:NF038329  207 GPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 624871     372 PGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKTGPPGKPGPP 423
Cdd:NF038329  286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 292-344 1.18e-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: 46.72  E-value: 1.18e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 624871      292 GEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGFEGSKGETGEKGE 344
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 941-995 1.36e-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: 46.33  E-value: 1.36e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 624871      941 GKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPG 995
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 578-640 1.22e-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: 40.94  E-value: 1.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 624871      578 EAGPPGKslPGEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDigpqgigiPGRTGAQGPAGEP 640
Cdd:pfam01391    5 PPGPPGP--PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP--------PGPPGAPGAPGPP 57
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
396-657 1.33e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.71  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    396 QGPQGPPGKEGQRGRRGKTGPPGKPGPPGPpgppgiQGIHQTLGGDDNKDNKGndeheAGGLKGDKGETGLPGFPGSVGP 475
Cdd:COG5164   51 QGSTTPAGNTGGTRPAGNQGATGPAQNQGG------TTPAQNQGGTRPAGNTG-----GTTPAGDGGATGPPDDGGATGP 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    476 KGQKGEPGEPFT--KGEKGDRGE-PGVIGSQGVKGEPGDPGPPGLIGSPGLKGQQGSAGSMGPRGPP--GDVGLPGEHGI 550
Cdd:COG5164  120 PDDGGSTTPPSGgsTTPPGDGGStPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGG 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    551 PGKQGIKGEKGDPGGIIGPPGLPGPKGEAGPPGKSLPGEPgldgnpgaPGPRGPKGERGLPGVHGSPGDIGPQGIGIPGR 630
Cdd:COG5164  200 TPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNP--------IERRGPERPEAAALPAELTALEAENRAANPEP 271

                        250       260
                 ....*....|....*....|....*..
gi 624871    631 TGAQGPAGEPGIQGPRGLPGLPGTPGT 657
Cdd:COG5164  272 ATKTIPETTTVKDLATVLGKKGSDLVT 298
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 581-664 8.89e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.99  E-value: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     581 PPGKSLPgEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDIGPQGIGIPGRTGAQGPAGEPgiQGPRGLPGLPGTPGTPGN 660
Cdd:PHA03264  277 PPGDDRP-EAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDADRP--EGWPSLEAITFPPPTPAT 353


                  ....
gi 624871     661 DGVP 664
Cdd:PHA03264  354 PAVP 357
 
Name Accession Description Interval E-value
TSPN smart00210
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ...
 50-233 1.01e-56

Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin


Pssm-ID: 214560  Cd Length: 184  Bit Score: 194.11  E-value: 1.01e-56
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871        50 NKLEVSGFDLGD-SFSLRRAFC-ESDKTCFKLGS-ALLIRDTIKIFPKGLPEEYSVAAMFRVRrnaKKERWFLWQVLNQQ 126
Cdd:smart00210    1 GQDLLQVFDLPSlSFAIRQVVGpEPGSPAYRLGDpALVPQPTRDLFPSGLPEDFSLLTTFRQT---PKSRGVLFAIYDAQ 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871       127 NIPQISIVVDGGKKVVEFMFQATEGDVLNYIFRNrelRPLFDRQWHKLGISIQSQVISLYMDCNLIARRQTDEKD--TVD 204
Cdd:smart00210   78 NVRQFGLEVDGRANTLLLRYQGVDGKQHTVSFRN---LPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGqpPID 154

                           170       180
                    ....*....|....*....|....*....
gi 624871       205 FHGRTVIATRASDGKPVDIELHQLKIYCS 233
Cdd:smart00210  155 TDGIEVRGAQAADRKPFQGDLQQLKIVCD 183
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 446-666 2.31e-29

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


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 122.71  E-value: 2.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     446 NKGNDEHEAGGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEKGDRGEPGVIGSQGVKGEPGDPGPPGLIGSPGLKG 525
Cdd:NF038329  107 DEGLQQLKGDGEKGEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     526 QQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEKgdPGGIIGPPGLPGPKGEAGPPGKSlpGEPGLDGNPGAPGPRGPK 605
Cdd:NF038329  187 PAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPA--GEDGPAGPAGDGQQGPDGDPGPT--GEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624871     606 GERGLPGVHGSPGDIGPQG-IGIPGRTGAQGPAGEPGIQGPRGLPGLPGTPGTPGNDGVPGR 666
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGpVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGK 324
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 332-666 2.90e-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: 98.05  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     332 FEGSKGETGEKGEQGEKGDPalaglngenglkgvlgphgppGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRr 411
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQ---------------------GPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGP- 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     412 gktgppgkpgppgppgppgiqgihQTLGGDDNKDnkgndeheagGLKGDKGETGLPGFPGSVGPKGQKGEPGEPFTKGEK 491
Cdd:NF038329  173 ------------------------QGPAGKDGEA----------GAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEA 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     492 GDRGEPGVIGSQGVKGEpgdpgppgliGSPGLKGQQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKGEkgdpggiigppg 571
Cdd:NF038329  219 GPAGEDGPAGPAGDGQQ----------GPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGK------------ 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     572 lpgpKGEAGPPGKslPGEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDIGPQGI-GIPGRTGAQGPAGEPGIQGPRgLPG 650
Cdd:NF038329  277 ----DGERGPVGP--AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKdGLPGKDGKDGQPGKPAPKTPE-VPQ 349

                         330
                  ....*....|....*..
gi 624871     651 LPGT-PGTPGNDGVPGR 666
Cdd:NF038329  350 KPDTaPHTPKTPQIPGQ 366
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 744-995 9.20e-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: 90.35  E-value: 9.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     744 GPKGSKGERGYPGIPGEKGDEGLQGIPGIPGAPGPTGPPGLMGRTGHPGPTGAKGEKGSDGPPGKPGppgppgipfnern 823
Cdd:NF038329  120 GEPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKG------------- 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     824 gmsslykikggvnvpsypgppgppgpkgdpgpvgEPGAMGLPGLEGFPGVKGDRGPAGPPGIAGmSGKPGAPGPPGVPGE 903
Cdd:NF038329  187 ----------------------------------PAGEKGPQGPRGETGPAGEQGPAGPAGPDG-EAGPAGEDGPAGPAG 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     904 PGERGPVGDIGFPGPEGPSGKPGINGKDGIPGAEGIMGKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMG 983
Cdd:NF038329  232 DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDG 311

                         250
                  ....*....|..
gi 624871     984 PPGNKGSMGSPG 995
Cdd:NF038329  312 LPGKDGKDGQPG 323
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 870-1098 3.32e-18

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: 88.81  E-value: 3.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     870 FPGVKGDRGPAGPPGIAGmsgkpgapgppgvpgepgERGPVGDIGFPGPEGPSGKPGINGKDGIPGAEGIMGKPGDRGPK 949
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAG------------------EQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPA 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     950 GERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPGHQGPPGSPGIPGIPADAvsfeeikkyinqevlri 1029
Cdd:NF038329  177 GKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDG----------------- 239

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 624871    1030 feermavflsqlkLPAAMLAAQAYGRPGPPGKDGLPGPPGDPGPQGYRGQKGERGEPGI----GLPGSPGLPG 1098
Cdd:NF038329  240 -------------DPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGPagkdGQNGKDGLPG 299
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 858-1101 1.61e-12

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: 71.09  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     858 EPGAMGLPGLEGFPGVKGDRGPAGPPGIAGMSGKPGAPGPPGVPGEPGERGPVG---------DIGFPGPEGPSGKPGIN 928
Cdd:NF038329  121 EPGPAGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGpagkdgeagAKGPAGEKGPQGPRGET 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     929 GKDGIPGAEGIMGKPGDRGPKGERGDQGIPGDrGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPGhqGPPGSPGIPGI 1008
Cdd:NF038329  201 GPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRG--EAGPDGPDGKD 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    1009 PADAVSFEEIKKYINQEVlrifeermavflsqlklpaaMLAAQAyGRPGPPGKDGLPgppgdpgpqgyrGQKGERGEPG- 1087
Cdd:NF038329  278 GERGPVGPAGKDGQNGKD--------------------GLPGKD-GKDGQNGKDGLP------------GKDGKDGQPGk 324

                         250
                  ....*....|....*..
gi 624871    1088 ---IGLPGSPGLPGTSA 1101
Cdd:NF038329  325 dglPGKDGKDGQPGKPA 341
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 291-414 4.98e-07

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: 53.76  E-value: 4.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     291 KGEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQkGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKGVLGPHG 370
Cdd:NF038329  197 RGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDG 275

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 624871     371 PPGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKT 414
Cdd:NF038329  276 KDGERGPVGPAGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKD 319
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 292-423 1.16e-06

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: 52.60  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     292 GEAGLPGAPGSPGQKGHKGEPGENGlHGAPGFPGQKGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKGVLGPHGP 371
Cdd:NF038329  207 GPAGPAGPDGEAGPAGEDGPAGPAG-DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERGPVGP 285

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 624871     372 PGPKGEKGDTGPPGPPALPGSLGIQGPQGPPGKEGQRGRRGKTGPPGKPGPP 423
Cdd:NF038329  286 AGKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQP 337
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 292-344 1.18e-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: 46.72  E-value: 1.18e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 624871      292 GEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGFEGSKGETGEKGE 344
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 941-995 1.36e-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: 46.33  E-value: 1.36e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 624871      941 GKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPPGNKGSMGSPG 995
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 929-985 1.08e-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: 44.02  E-value: 1.08e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 624871      929 GKDGIPGAEGIMGKPGDRGPKGERGDQGIPGDRGSQGERGKPGLTGMKGAIGPMGPP 985
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 310-364 2.44e-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: 42.87  E-value: 2.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 624871      310 GEPGENGLHGAPGFPGQKGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKG 364
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 292-347 3.03e-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: 42.48  E-value: 3.03e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 624871      292 GEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGFEGSKGETGEKGEQGE 347
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 578-640 1.22e-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: 40.94  E-value: 1.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 624871      578 EAGPPGKslPGEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDigpqgigiPGRTGAQGPAGEP 640
Cdd:pfam01391    5 PPGPPGP--PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGP--------PGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 291-334 1.53e-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: 40.55  E-value: 1.53e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 624871      291 KGEAGLPGAPGSPGQKGHKGEPGENGLHGAPGFPGQKGEQGFEG 334
Cdd:pfam01391   12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 908-956 9.18e-04

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


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 38.24  E-value: 9.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 624871      908 GPVGDIGFPGPEGPSGKPGINGKDGIPGAEGIMGKPGDRGPKGERGDQG 956
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
396-657 1.33e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 42.71  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    396 QGPQGPPGKEGQRGRRGKTGPPGKPGPPGPpgppgiQGIHQTLGGDDNKDNKGndeheAGGLKGDKGETGLPGFPGSVGP 475
Cdd:COG5164   51 QGSTTPAGNTGGTRPAGNQGATGPAQNQGG------TTPAQNQGGTRPAGNTG-----GTTPAGDGGATGPPDDGGATGP 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    476 KGQKGEPGEPFT--KGEKGDRGE-PGVIGSQGVKGEPGDPGPPGLIGSPGLKGQQGSAGSMGPRGPP--GDVGLPGEHGI 550
Cdd:COG5164  120 PDDGGSTTPPSGgsTTPPGDGGStPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPnkGETGTDIPTGG 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    551 PGKQGIKGEKGDPGGIIGPPGLPGPKGEAGPPGKSLPGEPgldgnpgaPGPRGPKGERGLPGVHGSPGDIGPQGIGIPGR 630
Cdd:COG5164  200 TPRQGPDGPVKKDDKNGKGNPPDDRGGKTGPKDQRPKTNP--------IERRGPERPEAAALPAELTALEAENRAANPEP 271

                        250       260
                 ....*....|....*....|....*..
gi 624871    631 TGAQGPAGEPGIQGPRGLPGLPGTPGT 657
Cdd:COG5164  272 ATKTIPETTTVKDLATVLGKKGSDLVT 298
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 908-962 2.12e-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: 37.47  E-value: 2.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 624871      908 GPVGDIGFPGPEGPSGKPGINGKDGIPGAEGIMGKPGDRGPKGERGDQGIPGDRG 962
Cdd:pfam01391    1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
SPT5 COG5164
Transcription elongation factor SPT5 [Transcription];
319-657 2.76e-03

Transcription elongation factor SPT5 [Transcription];


Pssm-ID: 444063 [Multi-domain]  Cd Length: 495  Bit Score: 41.55  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    319 GAPGFPGQKGEQGFEGSKGETGEKGEQGEKGDPALAGLNGENGLKGVLGPHGPPGPKGEKGDTGPPGPPALPGSLGIQGP 398
Cdd:COG5164    7 GKTGPSDPGGVTTPAGSQGSTKPAQNQGSTRPAGNTGGTRPAQNQGSTTPAGNTGGTRPAGNQGATGPAQNQGGTTPAQN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    399 QGPPGKEGQRGRRGKTGPPGKPGPPGPPGPPGIQGIHQTLGGDDNKdnkgndeheAGGLKGDKGETglPGFPGSVGPKGQ 478
Cdd:COG5164   87 QGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGG---------STTPPGDGGST--PPGPGSTGPGGS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    479 KGEPGEPFTKGEKGDRGEPGVIGSQGVKGEPGDpgppgliGSPGLKGQQGSAGSMGPRGPPGDVGLPGEHGIPGKQGIKG 558
Cdd:COG5164  156 TTPPGDGGSTTPPGPGGSTTPPDDGGSTTPPNK-------GETGTDIPTGGTPRQGPDGPVKKDDKNGKGNPPDDRGGKT 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871    559 EKGDPGGIIGPPGLPGPKGEAGPPGKSLP---GEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDIGPQGIGIPGRTGAQG 635
Cdd:COG5164  229 GPKDQRPKTNPIERRGPERPEAAALPAELtalEAENRAANPEPATKTIPETTTVKDLATVLGKKGSDLVTNLMKKGKGTN 308

                        330       340
                 ....*....|....*....|..
gi 624871    636 PAGEPGIQGPRGLPgLPGTPGT 657
Cdd:COG5164  309 INAALDFETAATIA-LEGNVIT 329
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 626-665 5.46e-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: 5.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 624871      626 GIPGRTGAQGPAGEPGIQGPRGLPGLPGTPGTPGNDGVPG 665
Cdd:pfam01391    7 GPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPG 46
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 626-665 8.59e-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: 35.55  E-value: 8.59e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 624871      626 GIPGRTGAQGPAGEPGIQGPRGLPGLPGTPGTPGNDGVPG 665
Cdd:pfam01391    4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPG 43
PHA03264 PHA03264
envelope glycoprotein D; Provisional
 581-664 8.89e-03

envelope glycoprotein D; Provisional


Pssm-ID: 223029 [Multi-domain]  Cd Length: 416  Bit Score: 39.99  E-value: 8.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624871     581 PPGKSLPgEPGLDGNPGAPGPRGPKGERGLPGVHGSPGDIGPQGIGIPGRTGAQGPAGEPgiQGPRGLPGLPGTPGTPGN 660
Cdd:PHA03264  277 PPGDDRP-EAKPEPGPVEDGAPGRETGGEGEGPEPAGRDGAAGGEPKPGPPRPAPDADRP--EGWPSLEAITFPPPTPAT 353


                  ....
gi 624871     661 DGVP 664
Cdd:PHA03264  354 PAVP 357
 
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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