|
Name |
Accession |
Description |
Interval |
E-value |
| Endostatin-like |
cd00247 |
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ... |
1350-1520 |
6.39e-115 |
|
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of collagen XV/XVIII, a proteoglycan/collagen found in vessel walls and basement membranes; this domain has a compact globular fold similar to that of C-type lectins; endostatin XVIII is monomeric and contains a heparin-binding epitope and zinc binding sites while endostatin XV is trimeric and contains neither of these sites; the generation of endostatin or endostatin-like collagen XV/XVIII fragments is catalyzed by proteolytic enzymes within the protease-sensitive hinge region of the C-terminal domain; endostatin inhibits endothelial cell migration in vitro and appears to be highly effective in murine in vivo studies
:
Pssm-ID: 238151 Cd Length: 171 Bit Score: 358.57 E-value: 6.39e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1350 QPVLHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSL 1429
Cdd:cd00247 1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1430 FSGSQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCH 1509
Cdd:cd00247 81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160
|
170
....*....|.
gi 158508560 1510 NSYIVLCIENS 1520
Cdd:cd00247 161 NKLIVLCIENS 171
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
245-433 |
7.38e-51 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
:
Pssm-ID: 214560 Cd Length: 184 Bit Score: 177.93 E-value: 7.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 245 EVGLLQLLGDP-LPEKISQIDDPHVG-PAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDaAQVV 322
Cdd:smart00210 1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 323 VSLGVKLsevrDGQQNISLLYTEpGASQTQTGASFR-LPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQglEL 401
Cdd:smart00210 80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152
|
170 180 190
....*....|....*....|....*....|..
gi 158508560 402 ERGAGLFVGQAGTADPDKFQGMISELKVRKTP 433
Cdd:smart00210 153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| DUF959 super family |
cl25749 |
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' ... |
37-218 |
4.11e-48 |
|
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' isoform of Collagen A.
The actual alignment was detected with superfamily member pfam06121:
Pssm-ID: 399255 [Multi-domain] Cd Length: 192 Bit Score: 170.40 E-value: 4.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 37 LVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASselppEEEEEEDQKAGQGGSPATPAVPIP 116
Cdd:pfam06121 16 LDLLWFLDIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAAS-----PELPLEELEAAPGRAPGAPISAAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 117 LVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSS 196
Cdd:pfam06121 91 PAALAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPHR 170
|
170 180
....*....|....*....|..
gi 158508560 197 AIPSSPDAQTTEAGTLAVPTQL 218
Cdd:pfam06121 171 GALSSLDTPRAESGTLAVPTQL 192
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
819-1075 |
1.01e-24 |
|
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: 109.22 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 819 GLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPP 898
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 899 gpviyvssedKAIVSTPGPEGKPGYAGFPGPAGPKGDlGSKGEQGLPGPKGEKGEPGtifsPDGRALGHPQKGAKGEPGf 978
Cdd:NF038329 206 ----------QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQG----PDGPAGKDGPRGDRGEAG- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 979 rgppgpygRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASlgfsMRGlpgppgppgppgppgmpiydsnafvESGRPGL 1058
Cdd:NF038329 270 --------PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG----KDG-------------------------QNGKDGL 312
|
250
....*....|....*..
gi 158508560 1059 PGQQGVQGPSGPKGDKG 1075
Cdd:NF038329 313 PGKDGKDGQPGKDGLPG 329
|
|
| Collagen_trimer |
pfam20010 |
Collagen trimerization domain; This small domain mediate trimerization in various collagen ... |
1216-1263 |
9.66e-17 |
|
Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.
:
Pssm-ID: 466257 Cd Length: 49 Bit Score: 75.33 E-value: 9.66e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 158508560 1216 VRIWATYQTMLDKIREVPEGWLIFVAEREELYVRVRNGFRKVLLEART 1263
Cdd:pfam20010 1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELI 48
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
589-883 |
6.90e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 69.55 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 589 KDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGEKGDPGIGPRGPPGPPGPPGpsfrqdkltfidmegsGFSGD 668
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR----------------GETGP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 669 ieslRGPRGFPGPPGPPGVPGLPGEPGRFGINGSYAPGPAGLPGvpgkegppgfpgppgppgppgkegppgVAGQKGSVG 748
Cdd:NF038329 203 ----AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG---------------------------PTGEDGPQG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 749 DVGIPGPKGSKGDLGPIGMPGKSGlagspgpvgppgppgppgppgpgfaagfddmegsgiplwttarsSDGLQGPPGSPG 828
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDG--------------------------------------------KDGERGPVGPAG 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158508560 829 LKGDPGVAGLPGAKGEvgaDGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGK 883
Cdd:NF038329 288 KDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Endostatin-like |
cd00247 |
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ... |
1350-1520 |
6.39e-115 |
|
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of collagen XV/XVIII, a proteoglycan/collagen found in vessel walls and basement membranes; this domain has a compact globular fold similar to that of C-type lectins; endostatin XVIII is monomeric and contains a heparin-binding epitope and zinc binding sites while endostatin XV is trimeric and contains neither of these sites; the generation of endostatin or endostatin-like collagen XV/XVIII fragments is catalyzed by proteolytic enzymes within the protease-sensitive hinge region of the C-terminal domain; endostatin inhibits endothelial cell migration in vitro and appears to be highly effective in murine in vivo studies
Pssm-ID: 238151 Cd Length: 171 Bit Score: 358.57 E-value: 6.39e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1350 QPVLHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSL 1429
Cdd:cd00247 1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1430 FSGSQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCH 1509
Cdd:cd00247 81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160
|
170
....*....|.
gi 158508560 1510 NSYIVLCIENS 1520
Cdd:cd00247 161 NKLIVLCIENS 171
|
|
| Endostatin |
pfam06482 |
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ... |
1353-1521 |
1.27e-112 |
|
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss:P39059. A mutation in this region in Swiss:P39060 is associated with an increased risk of prostrate cancer. This domain is cleaved from the precursor and forms endostatin. Endostatin is a key tumour suppressor and has been used highly successfully to treat cancer. It is a potent angiogenesis inhibitor. Endostatin also binds a zinc ion near the N-terminus; this is likely to be of structural rather than functional importance according to.
Pssm-ID: 461931 Cd Length: 169 Bit Score: 352.13 E-value: 1.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1353 LHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSLFSG 1432
Cdd:pfam06482 1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1433 SQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCHNSY 1512
Cdd:pfam06482 81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160
|
....*....
gi 158508560 1513 IVLCIENSF 1521
Cdd:pfam06482 161 IVLCIENSY 169
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
245-433 |
7.38e-51 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 177.93 E-value: 7.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 245 EVGLLQLLGDP-LPEKISQIDDPHVG-PAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDaAQVV 322
Cdd:smart00210 1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 323 VSLGVKLsevrDGQQNISLLYTEpGASQTQTGASFR-LPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQglEL 401
Cdd:smart00210 80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152
|
170 180 190
....*....|....*....|....*....|..
gi 158508560 402 ERGAGLFVGQAGTADPDKFQGMISELKVRKTP 433
Cdd:smart00210 153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| DUF959 |
pfam06121 |
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' ... |
37-218 |
4.11e-48 |
|
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' isoform of Collagen A.
Pssm-ID: 399255 [Multi-domain] Cd Length: 192 Bit Score: 170.40 E-value: 4.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 37 LVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASselppEEEEEEDQKAGQGGSPATPAVPIP 116
Cdd:pfam06121 16 LDLLWFLDIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAAS-----PELPLEELEAAPGRAPGAPISAAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 117 LVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSS 196
Cdd:pfam06121 91 PAALAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPHR 170
|
170 180
....*....|....*....|..
gi 158508560 197 AIPSSPDAQTTEAGTLAVPTQL 218
Cdd:pfam06121 171 GALSSLDTPRAESGTLAVPTQL 192
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
819-1075 |
1.01e-24 |
|
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: 109.22 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 819 GLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPP 898
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 899 gpviyvssedKAIVSTPGPEGKPGYAGFPGPAGPKGDlGSKGEQGLPGPKGEKGEPGtifsPDGRALGHPQKGAKGEPGf 978
Cdd:NF038329 206 ----------QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQG----PDGPAGKDGPRGDRGEAG- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 979 rgppgpygRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASlgfsMRGlpgppgppgppgppgmpiydsnafvESGRPGL 1058
Cdd:NF038329 270 --------PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG----KDG-------------------------QNGKDGL 312
|
250
....*....|....*..
gi 158508560 1059 PGQQGVQGPSGPKGDKG 1075
Cdd:NF038329 313 PGKDGKDGQPGKDGLPG 329
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
741-1016 |
1.24e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 106.14 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 741 AGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGspgpvgppgppgppgppgpgfaagfddmegsgiplwttarsSDGL 820
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG-----------------------------------------PAGP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 821 QGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPpgppgp 900
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD------ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 901 viyvssedkaivstPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGtifsPDGRALGHPQKGAKGEPGFRG 980
Cdd:NF038329 241 --------------PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG----PVGPAGKDGQNGKDGLPGKDG 302
|
250 260 270
....*....|....*....|....*....|....*.
gi 158508560 981 PPGPYGRPGHKGEIGFPGRPGRPGTNGLKGEKGEPG 1016
Cdd:NF038329 303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
705-955 |
1.43e-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: 93.43 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 705 PGPAGLPGVPGKEGPPGFPGPPGPPGPPGKEGPPGVAGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGspgpvgppg 784
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG--------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 785 PPGPPGPPGPGFAAGFDDMEGSGIPLWTTARSSDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAG 864
Cdd:NF038329 199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 865 SPGPKGEKGMPGEKGNPGkdgvgrpglpgppgppgpviyvssedkaivsTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGL 944
Cdd:NF038329 279 ERGPVGPAGKDGQNGKDG-------------------------------LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
250
....*....|.
gi 158508560 945 PGPKGEKGEPG 955
Cdd:NF038329 328 PGKDGKDGQPG 338
|
|
| Collagen_trimer |
pfam20010 |
Collagen trimerization domain; This small domain mediate trimerization in various collagen ... |
1216-1263 |
9.66e-17 |
|
Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.
Pssm-ID: 466257 Cd Length: 49 Bit Score: 75.33 E-value: 9.66e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 158508560 1216 VRIWATYQTMLDKIREVPEGWLIFVAEREELYVRVRNGFRKVLLEART 1263
Cdd:pfam20010 1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELI 48
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
876-1120 |
1.29e-13 |
|
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: 74.94 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 876 GEKGNPGkdgvgrpglpgPPGPPGPviyvssedkaivstPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPG 955
Cdd:NF038329 117 GEKGEPG-----------PAGPAGP--------------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 956 tifsPDGRALGHPQKGAKGEPGFRGPPGPYGRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASLGfsmrglpgppgppg 1035
Cdd:NF038329 172 ----PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG-------------- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1036 ppgppgmpiydsnafvESGRPGLPGQQGVQGPSGPKGDKGEVGPpgppgqfpidlfhleaemKGDKGDRGDAGQKGERGE 1115
Cdd:NF038329 234 ----------------QQGPDGDPGPTGEDGPQGPDGPAGKDGP------------------RGDRGEAGPDGPDGKDGE 279
|
....*
gi 158508560 1116 PGAPG 1120
Cdd:NF038329 280 RGPVG 284
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
589-883 |
6.90e-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: 69.55 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 589 KDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGEKGDPGIGPRGPPGPPGPPGpsfrqdkltfidmegsGFSGD 668
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR----------------GETGP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 669 ieslRGPRGFPGPPGPPGVPGLPGEPGRFGINGSYAPGPAGLPGvpgkegppgfpgppgppgppgkegppgVAGQKGSVG 748
Cdd:NF038329 203 ----AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG---------------------------PTGEDGPQG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 749 DVGIPGPKGSKGDLGPIGMPGKSGlagspgpvgppgppgppgppgpgfaagfddmegsgiplwttarsSDGLQGPPGSPG 828
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDG--------------------------------------------KDGERGPVGPAG 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158508560 829 LKGDPGVAGLPGAKGEvgaDGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGK 883
Cdd:NF038329 288 KDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
825-881 |
9.30e-10 |
|
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: 55.58 E-value: 9.30e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 158508560 825 GSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNP 881
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
281-429 |
3.78e-06 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 48.18 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 281 GQVAQYHFPKLFFRDFSLLFHVRPaTEAAGVLFAITDAAQV-VVSLgvklsEVRDGQqnISLLYTEPGASqtqtgASFRL 359
Cdd:cd00110 7 SSYVRLPTLPAPRTRLSISFSFRT-TSPNGLLLYAGSQNGGdFLAL-----ELEDGR--LVLRYDLGSGS-----LVLSS 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158508560 360 PAFV--GQWTHFALSVDGGSVALYVDCEEFQRVPFARASQGLELErgAGLFVG-------QAGTADPDKFQGMISELKV 429
Cdd:cd00110 74 KTPLndGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD--GPLYLGglpedlkSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
295-429 |
2.22e-05 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 46.22 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 295 DFSLLFHVRP--ATEAAGVLFAITDAAQVVVSLGvklsevRDGQQNISLLYTEPGASQTQTGASFRLpafvGQWTHFALS 372
Cdd:pfam13385 18 DFTVSAWVKPdsLPGWARAIISSSGGGGYSLGLD------GDGRLRFAVNGGNGGWDTVTSGASVPL----GQWTHVAVT 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 158508560 373 VDGGSVALYVDCEEFQRVPfarASQGLELERGAGLFVGQAGTADPDkFQGMISELKV 429
Cdd:pfam13385 88 YDGGTLRLYVNGVLVGSST---LTGGPPPGTGGPLYIGRSPGGDDY-FNGLIDEVRI 140
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
742-960 |
3.69e-05 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 48.10 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 742 GQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGSPGPVGPPGPPGPPGPPGPGFAAGFDDMEGSGIPLWTTARSSDGLQ 821
Cdd:COG5164 61 GGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 822 GP-PGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPgREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPpgp 900
Cdd:COG5164 141 GStPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPP-DDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNG--- 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 901 viyvssedkaivSTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGTIFSP 960
Cdd:COG5164 217 ------------KGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
593-628 |
1.39e-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: 38.24 E-value: 1.39e-03
10 20 30
....*....|....*....|....*....|....*.
gi 158508560 593 PGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGE 628
Cdd:pfam01391 21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| MJ1470 |
COG5306 |
Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type ... |
306-383 |
4.69e-03 |
|
Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type IV pili-like system [General function prediction only];
Pssm-ID: 444105 [Multi-domain] Cd Length: 529 Bit Score: 41.43 E-value: 4.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158508560 306 TEAAGVLFAITDAAQVVVSLGVKLSEVRDGQQNISLlytePGASQTQTGASFRLPAfvGQWTHFALSVDGGSVALYVD 383
Cdd:COG5306 200 TFSAWIKPAQLDGNAVLYSRRDGANGLDNGAPFVEV----GGAGGTRSAAGAPLAA--GTWHHLAVVADAGKVTLYVN 271
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Endostatin-like |
cd00247 |
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ... |
1350-1520 |
6.39e-115 |
|
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of collagen XV/XVIII, a proteoglycan/collagen found in vessel walls and basement membranes; this domain has a compact globular fold similar to that of C-type lectins; endostatin XVIII is monomeric and contains a heparin-binding epitope and zinc binding sites while endostatin XV is trimeric and contains neither of these sites; the generation of endostatin or endostatin-like collagen XV/XVIII fragments is catalyzed by proteolytic enzymes within the protease-sensitive hinge region of the C-terminal domain; endostatin inhibits endothelial cell migration in vitro and appears to be highly effective in murine in vivo studies
Pssm-ID: 238151 Cd Length: 171 Bit Score: 358.57 E-value: 6.39e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1350 QPVLHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSL 1429
Cdd:cd00247 1 QPVLHLVALNTPLSGDMRGIRGADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1430 FSGSQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCH 1509
Cdd:cd00247 81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160
|
170
....*....|.
gi 158508560 1510 NSYIVLCIENS 1520
Cdd:cd00247 161 NKLIVLCIENS 171
|
|
| Endostatin |
pfam06482 |
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ... |
1353-1521 |
1.27e-112 |
|
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss:P39059. A mutation in this region in Swiss:P39060 is associated with an increased risk of prostrate cancer. This domain is cleaved from the precursor and forms endostatin. Endostatin is a key tumour suppressor and has been used highly successfully to treat cancer. It is a potent angiogenesis inhibitor. Endostatin also binds a zinc ion near the N-terminus; this is likely to be of structural rather than functional importance according to.
Pssm-ID: 461931 Cd Length: 169 Bit Score: 352.13 E-value: 1.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1353 LHLVALNTPLSGGMRGIRGADFQCFQQARAVGLSGTFRAFLSSRLQDLYSIVRRADRGSVPIVNLKDEVLSPSWDSLFSG 1432
Cdd:pfam06482 1 LHLIALNTPQSGDMRGIRGADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1433 SQGQLQPGARIFSFDGRDVLRHPAWPQKSVWHGSDPSGRRLMESYCETWRTETTGATGQASSLLSGRLLEQKAASCHNSY 1512
Cdd:pfam06482 81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160
|
....*....
gi 158508560 1513 IVLCIENSF 1521
Cdd:pfam06482 161 IVLCIENSY 169
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
245-433 |
7.38e-51 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 177.93 E-value: 7.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 245 EVGLLQLLGDP-LPEKISQIDDPHVG-PAYIFGPDSNSGQVAQYHFPKLFFRDFSLLFHVRPATEAAGVLFAITDaAQVV 322
Cdd:smart00210 1 GQDLLQVFDLPsLSFAIRQVVGPEPGsPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYD-AQNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 323 VSLGVKLsevrDGQQNISLLYTEpGASQTQTGASFR-LPAFVGQWTHFALSVDGGSVALYVDCEEFQRVPFARASQglEL 401
Cdd:smart00210 80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQ--PP 152
|
170 180 190
....*....|....*....|....*....|..
gi 158508560 402 ERGAGLFVGQAGTADPDKFQGMISELKVRKTP 433
Cdd:smart00210 153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| DUF959 |
pfam06121 |
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' ... |
37-218 |
4.11e-48 |
|
Domain of Unknown Function (DUF959); This N-terminal domain is not expressed in the 'Short' isoform of Collagen A.
Pssm-ID: 399255 [Multi-domain] Cd Length: 192 Bit Score: 170.40 E-value: 4.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 37 LVWLWPPKTSDSLEGPVSKPQNSSPVQSTENPTTHVVPQDGLTEQQTTPASselppEEEEEEDQKAGQGGSPATPAVPIP 116
Cdd:pfam06121 16 LDLLWFLDIADPEDTLASEPQGGLAVQPAAAPATHVAPQDDPAEQATAAAS-----PELPLEELEAAPGRAPGAPISAAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 117 LVAPAASPDMKEENVAGVGAKILNVAQGIRSFVQLWDEDSTIGHSAGTEVPDSSIPTVLPSPAELSSAPQGSKTTLWLSS 196
Cdd:pfam06121 91 PAALAARPDMREENVAGVGAKILNIAQGIQSFIQLWNDAAPTESPAGAGTLAASAPTDPLALAEPSGPAAESGTALGPHR 170
|
170 180
....*....|....*....|..
gi 158508560 197 AIPSSPDAQTTEAGTLAVPTQL 218
Cdd:pfam06121 171 GALSSLDTPRAESGTLAVPTQL 192
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
819-1075 |
1.01e-24 |
|
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: 109.22 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 819 GLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPP 898
Cdd:NF038329 126 GPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGE 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 899 gpviyvssedKAIVSTPGPEGKPGYAGFPGPAGPKGDlGSKGEQGLPGPKGEKGEPGtifsPDGRALGHPQKGAKGEPGf 978
Cdd:NF038329 206 ----------QGPAGPAGPDGEAGPAGEDGPAGPAGD-GQQGPDGDPGPTGEDGPQG----PDGPAGKDGPRGDRGEAG- 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 979 rgppgpygRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASlgfsMRGlpgppgppgppgppgmpiydsnafvESGRPGL 1058
Cdd:NF038329 270 --------PDGPDGKDGERGPVGPAGKDGQNGKDGLPGKDG----KDG-------------------------QNGKDGL 312
|
250
....*....|....*..
gi 158508560 1059 PGQQGVQGPSGPKGDKG 1075
Cdd:NF038329 313 PGKDGKDGQPGKDGLPG 329
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
741-1016 |
1.24e-23 |
|
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 106.14 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 741 AGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGspgpvgppgppgppgppgpgfaagfddmegsgiplwttarsSDGL 820
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKG-----------------------------------------PAGP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 821 QGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPpgppgp 900
Cdd:NF038329 167 QGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGD------ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 901 viyvssedkaivstPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGtifsPDGRALGHPQKGAKGEPGFRG 980
Cdd:NF038329 241 --------------PGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDGERG----PVGPAGKDGQNGKDGLPGKDG 302
|
250 260 270
....*....|....*....|....*....|....*.
gi 158508560 981 PPGPYGRPGHKGEIGFPGRPGRPGTNGLKGEKGEPG 1016
Cdd:NF038329 303 KDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
705-955 |
1.43e-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: 93.43 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 705 PGPAGLPGVPGKEGPPGFPGPPGPPGPPGKEGPPGVAGQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGspgpvgppg 784
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRG--------- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 785 PPGPPGPPGPGFAAGFDDMEGSGIPLWTTARSSDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAG 864
Cdd:NF038329 199 ETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPDGPDGKDG 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 865 SPGPKGEKGMPGEKGNPGkdgvgrpglpgppgppgpviyvssedkaivsTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGL 944
Cdd:NF038329 279 ERGPVGPAGKDGQNGKDG-------------------------------LPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
250
....*....|.
gi 158508560 945 PGPKGEKGEPG 955
Cdd:NF038329 328 PGKDGKDGQPG 338
|
|
| Collagen_trimer |
pfam20010 |
Collagen trimerization domain; This small domain mediate trimerization in various collagen ... |
1216-1263 |
9.66e-17 |
|
Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.
Pssm-ID: 466257 Cd Length: 49 Bit Score: 75.33 E-value: 9.66e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 158508560 1216 VRIWATYQTMLDKIREVPEGWLIFVAEREELYVRVRNGFRKVLLEART 1263
Cdd:pfam20010 1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGELI 48
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
876-1120 |
1.29e-13 |
|
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: 74.94 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 876 GEKGNPGkdgvgrpglpgPPGPPGPviyvssedkaivstPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPG 955
Cdd:NF038329 117 GEKGEPG-----------PAGPAGP--------------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 956 tifsPDGRALGHPQKGAKGEPGFRGPPGPYGRPGHKGEIGFPGRPGRPGTNGLKGEKGEPGDASLGfsmrglpgppgppg 1035
Cdd:NF038329 172 ----PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGDG-------------- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 1036 ppgppgmpiydsnafvESGRPGLPGQQGVQGPSGPKGDKGEVGPpgppgqfpidlfhleaemKGDKGDRGDAGQKGERGE 1115
Cdd:NF038329 234 ----------------QQGPDGDPGPTGEDGPQGPDGPAGKDGP------------------RGDRGEAGPDGPDGKDGE 279
|
....*
gi 158508560 1116 PGAPG 1120
Cdd:NF038329 280 RGPVG 284
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
589-883 |
6.90e-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: 69.55 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 589 KDGTPGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGEKGDPGIGPRGPPGPPGPPGpsfrqdkltfidmegsGFSGD 668
Cdd:NF038329 139 DRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPR----------------GETGP 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 669 ieslRGPRGFPGPPGPPGVPGLPGEPGRFGINGSYAPGPAGLPGvpgkegppgfpgppgppgppgkegppgVAGQKGSVG 748
Cdd:NF038329 203 ----AGEQGPAGPAGPDGEAGPAGEDGPAGPAGDGQQGPDGDPG---------------------------PTGEDGPQG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 749 DVGIPGPKGSKGDLGPIGMPGKSGlagspgpvgppgppgppgppgpgfaagfddmegsgiplwttarsSDGLQGPPGSPG 828
Cdd:NF038329 252 PDGPAGKDGPRGDRGEAGPDGPDG--------------------------------------------KDGERGPVGPAG 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158508560 829 LKGDPGVAGLPGAKGEvgaDGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPGK 883
Cdd:NF038329 288 KDGQNGKDGLPGKDGK---DGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPGK 339
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
825-881 |
9.30e-10 |
|
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: 55.58 E-value: 9.30e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 158508560 825 GSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNP 881
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
817-868 |
4.04e-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: 460189 [Multi-domain] Cd Length: 57 Bit Score: 54.04 E-value: 4.04e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 158508560 817 SDGLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGP 868
Cdd:pfam01391 5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
819-875 |
4.28e-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: 460189 [Multi-domain] Cd Length: 57 Bit Score: 53.65 E-value: 4.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 158508560 819 GLQGPPGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMP 875
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
831-882 |
5.16e-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: 460189 [Multi-domain] Cd Length: 57 Bit Score: 53.65 E-value: 5.16e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 158508560 831 GDPGVAGLPGAKGEVGADGAQGIPGPPGREGAAGSPGPKGEKGMPGEKGNPG 882
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
281-429 |
3.78e-06 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 48.18 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 281 GQVAQYHFPKLFFRDFSLLFHVRPaTEAAGVLFAITDAAQV-VVSLgvklsEVRDGQqnISLLYTEPGASqtqtgASFRL 359
Cdd:cd00110 7 SSYVRLPTLPAPRTRLSISFSFRT-TSPNGLLLYAGSQNGGdFLAL-----ELEDGR--LVLRYDLGSGS-----LVLSS 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158508560 360 PAFV--GQWTHFALSVDGGSVALYVDCEEFQRVPFARASQGLELErgAGLFVG-------QAGTADPDKFQGMISELKV 429
Cdd:cd00110 74 KTPLndGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD--GPLYLGglpedlkSPGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
295-429 |
2.22e-05 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 46.22 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 295 DFSLLFHVRP--ATEAAGVLFAITDAAQVVVSLGvklsevRDGQQNISLLYTEPGASQTQTGASFRLpafvGQWTHFALS 372
Cdd:pfam13385 18 DFTVSAWVKPdsLPGWARAIISSSGGGGYSLGLD------GDGRLRFAVNGGNGGWDTVTSGASVPL----GQWTHVAVT 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 158508560 373 VDGGSVALYVDCEEFQRVPfarASQGLELERGAGLFVGQAGTADPDkFQGMISELKV 429
Cdd:pfam13385 88 YDGGTLRLYVNGVLVGSST---LTGGPPPGTGGPLYIGRSPGGDDY-FNGLIDEVRI 140
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
915-955 |
2.41e-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: 43.25 E-value: 2.41e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 158508560 915 PGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPG 955
Cdd:pfam01391 12 PGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
|
|
| LamG |
smart00282 |
Laminin G domain; |
297-429 |
3.07e-05 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 45.02 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 297 SLLFHVRPaTEAAGVLFAITDAAQV-VVSLgvklsEVRDGQqnISLLYTEPGASQTQTGASFRLPAfvGQWTHFALSVDG 375
Cdd:smart00282 1 SISFSFRT-TSPNGLLLYAGSKGGGdYLAL-----ELRDGR--LVLRYDLGSGPARLTSDPTPLND--GQWHRVAVERNG 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158508560 376 GSVALYVDCEEFQRVPFARASQGLELErgAGLFVG-------QAGTADPDKFQGMISELKV 429
Cdd:smart00282 71 RSVTLSVDGGNRVSGESPGGLTILNLD--GPLYLGglpedlkLPPLPVTPGFRGCIRNLKV 129
|
|
| SPT5 |
COG5164 |
Transcription elongation factor SPT5 [Transcription]; |
742-960 |
3.69e-05 |
|
Transcription elongation factor SPT5 [Transcription];
Pssm-ID: 444063 [Multi-domain] Cd Length: 495 Bit Score: 48.10 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 742 GQKGSVGDVGIPGPKGSKGDLGPIGMPGKSGLAGSPGPVGPPGPPGPPGPPGPGFAAGFDDMEGSGIPLWTTARSSDGLQ 821
Cdd:COG5164 61 GGTRPAGNQGATGPAQNQGGTTPAQNQGGTRPAGNTGGTTPAGDGGATGPPDDGGATGPPDDGGSTTPPSGGSTTPPGDG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 822 GP-PGSPGLKGDPGVAGLPGAKGEVGADGAQGIPGPPgREGAAGSPGPKGEKGMPGEKGNPGKDGVGRPGLPGPPGPpgp 900
Cdd:COG5164 141 GStPPGPGSTGPGGSTTPPGDGGSTTPPGPGGSTTPP-DDGGSTTPPNKGETGTDIPTGGTPRQGPDGPVKKDDKNG--- 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 901 viyvssedkaivSTPGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPGTIFSP 960
Cdd:COG5164 217 ------------KGNPPDDRGGKTGPKDQRPKTNPIERRGPERPEAAALPAELTALEAEN 264
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
864-950 |
5.45e-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: 42.10 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 864 GSPGPKGEKGMPGEKGNPGKdgvgrpglpgppgppgpviyvssedkaivstPGPEGKPGYAGFPGPAGPKGDLGSKGEQG 943
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGP-------------------------------PGPPGPPGPPGEPGPPGPPGPPGPPGPPG 49
|
....*..
gi 158508560 944 LPGPKGE 950
Cdd:pfam01391 50 APGAPGP 56
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
915-955 |
7.25e-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: 41.71 E-value: 7.25e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 158508560 915 PGPEGKPGYAGFPGPAGPKGDLGSKGEQGLPGPKGEKGEPG 955
Cdd:pfam01391 15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
937-1018 |
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: 41.33 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 937 GSKGEQGLPGPKGEKGEPGtifspdgralghpQKGAKGEPGfrgppgpygrpgHKGEIGFPGRPGRPGTNGLKGEKGEPG 1016
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPG-------------PPGPPGPPG------------PPGEPGPPGPPGPPGPPGPPGAPGAPG 55
|
..
gi 158508560 1017 DA 1018
Cdd:pfam01391 56 PP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
593-628 |
1.39e-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: 38.24 E-value: 1.39e-03
10 20 30
....*....|....*....|....*....|....*.
gi 158508560 593 PGRDGEPGDPGEDGRPGDTGPQGFPGTPGDVGPKGE 628
Cdd:pfam01391 21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
|
|
| MJ1470 |
COG5306 |
Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type ... |
306-383 |
4.69e-03 |
|
Uncharacterized conserved protein MJ1470, contains DUF2341 domain, predicted component of type IV pili-like system [General function prediction only];
Pssm-ID: 444105 [Multi-domain] Cd Length: 529 Bit Score: 41.43 E-value: 4.69e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158508560 306 TEAAGVLFAITDAAQVVVSLGVKLSEVRDGQQNISLlytePGASQTQTGASFRLPAfvGQWTHFALSVDGGSVALYVD 383
Cdd:COG5306 200 TFSAWIKPAQLDGNAVLYSRRDGANGLDNGAPFVEV----GGAGGTRSAAGAPLAA--GTWHHLAVVADAGKVTLYVN 271
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
306-429 |
9.29e-03 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 37.78 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158508560 306 TEAAGVLFAITDAAQVVVSLgvklsEVRDGQqnISLLYTEPGASQTQTGASFRLPAfvGQWTHFALSVDGGSVALYVDCE 385
Cdd:pfam02210 4 RQPNGLLLYAGGGGSDFLAL-----ELVNGR--LVLRYDLGSGPESLLSSGKNLND--GQWHSVRVERNGNTLTLSVDGQ 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 158508560 386 EFQRVPFARASQGLELERgaGLFVGQAGTADPDK-------FQGMISELKV 429
Cdd:pfam02210 75 TVVSSLPPGESLLLNLNG--PLYLGGLPPLLLLPalpvragFVGCIRDVRV 123
|
|
| |
