|
Name |
Accession |
Description |
Interval |
E-value |
| Endostatin |
pfam06482 |
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ... |
1197-1361 |
3.73e-111 |
|
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: 346.74 E-value: 3.73e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 1197 LHLVALNTPVAGDIR----ADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFGLPIVNLKGQVLFNNWDSIFSG 1272
Cdd:pfam06482 1 LHLIALNTPQSGDMRgirgADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 1273 DGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCANRL 1352
Cdd:pfam06482 81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160
|
....*....
gi 134288882 1353 IVLCIENSF 1361
Cdd:pfam06482 161 IVLCIENSY 169
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
42-228 |
1.61e-43 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
:
Pssm-ID: 214560 Cd Length: 184 Bit Score: 156.75 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 42 DLTVLIGVPLPSSVSFTTGY-GGFPAYSFGPGANVGRPARTLIPPTFFRDFAIGVAVKPNSAQGGVLFAITDAfQKVIYL 120
Cdd:smart00210 4 LLQVFDLPSLSFAIRQVVGPePGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNVRQF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 121 GLRLssveDGRQRVILYYTEpGSHVSREAAVFS-VPVMTNRWNRFAVTVQGEEVALFMDCEEQSQVRFQRSSWPltFEPS 199
Cdd:smart00210 83 GLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP--PIDT 155
|
170 180
....*....|....*....|....*....
gi 134288882 200 AGIFVGNAGAMGLERFTGSIQQLTIYSDP 228
Cdd:smart00210 156 DGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| Collagen_trimer |
pfam20010 |
Collagen trimerization domain; This small domain mediate trimerization in various collagen ... |
1114-1160 |
4.43e-19 |
|
Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.
:
Pssm-ID: 466257 Cd Length: 49 Bit Score: 81.88 E-value: 4.43e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 134288882 1114 VTALSDMGDMLQKAHLVIEGTFIYLRDSGEFFIRVRDGWKKLQLGEL 1160
Cdd:pfam20010 1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGEL 47
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
637-912 |
1.11e-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.
The actual alignment was detected with superfamily member NF038329:
Pssm-ID: 468478 [Multi-domain] Cd Length: 440 Bit Score: 90.73 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 637 DGAPGEPGPQGPEGQpgldgaSGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGPPGKNGEVGTPgvmgppgppgppGPPG 716
Cdd:NF038329 116 DGEKGEPGPAGPAGP------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ------------GPAG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 717 PGCTTELgfeiegSGDVRLLSKPTISGPTSPSGPKGEKGEQGAKGERGADGtstmgppgprgppghvevlssslinitng 796
Cdd:NF038329 178 KDGEAGA------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAG----------------------------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 797 smnfsdiPELMGPPGPDGVPGLPGFPGPRGPKGDTGVPGFPGLKGEQGEKGEPGaiLTGDVPLEMMKGRKGEPGihgapg 876
Cdd:NF038329 223 -------EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG--PDGPDGKDGERGPVGPAG------ 287
|
250 260 270
....*....|....*....|....*....|....*.
gi 134288882 877 pmgpkgPPGHKGEFGLPGRPGRPGLNGLKGAKGDRG 912
Cdd:NF038329 288 ------KDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
|
|
| Herpes_BLLF1 super family |
cl37540 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
265-541 |
5.24e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
The actual alignment was detected with superfamily member pfam05109:
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 41.44 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 265 TQAPPKESHVDPISVPPTSSSPAEDSELSGEPVPEGTPETNLSIIGHSSPEqgsgeilndtlevhamdgDPGTDDGSGDg 344
Cdd:pfam05109 445 TTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPR------------------DNGTESKAPD- 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 345 allnVTDGQGLSATATGEASVPVTTVLE-AENGSMPT---GSPTLAMFTQS------IREVDTPDPeNLTTTASGDGEVP 414
Cdd:pfam05109 506 ----MTSPTSAVTTPTPNATSPTPAVTTpTPNATSPTlgkTSPTSAVTTPTpnatspTPAVTTPTP-NATIPTLGKTSPT 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 415 TSTDGDTEADSSPTGGPTlKPREEATLGSHGEEWLTPAVSKMP---LKAFEEEEASGTAIDSLDVIFTPTVVLEQVSRRP 491
Cdd:pfam05109 581 SAVTTPTPNATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPknaTSAVTTGQHNITSSSTSSMSLRPSSISETLSPST 659
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 134288882 492 TDIQATFTPTVVLEETSG---------APTDTQDALTPTVAPEQMFTAEPTDGGDLVAS 541
Cdd:pfam05109 660 SDNSTSHMPLLTSAHPTGgenitqvtpASTSTHHVSTSSPAPRPGTTSQASGPGNSSTS 718
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Endostatin |
pfam06482 |
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ... |
1197-1361 |
3.73e-111 |
|
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: 346.74 E-value: 3.73e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 1197 LHLVALNTPVAGDIR----ADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFGLPIVNLKGQVLFNNWDSIFSG 1272
Cdd:pfam06482 1 LHLIALNTPQSGDMRgirgADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 1273 DGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCANRL 1352
Cdd:pfam06482 81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160
|
....*....
gi 134288882 1353 IVLCIENSF 1361
Cdd:pfam06482 161 IVLCIENSY 169
|
|
| Endostatin-like |
cd00247 |
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ... |
1194-1360 |
5.74e-111 |
|
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: 346.24 E-value: 5.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 1194 RPVLHLVALNTPVAGDIR----ADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFGLPIVNLKGQVLFNNWDSI 1269
Cdd:cd00247 1 QPVLHLVALNTPLSGDMRgirgADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 1270 FSGDGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCA 1349
Cdd:cd00247 81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160
|
170
....*....|.
gi 134288882 1350 NRLIVLCIENS 1360
Cdd:cd00247 161 NKLIVLCIENS 171
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
42-228 |
1.61e-43 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 156.75 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 42 DLTVLIGVPLPSSVSFTTGY-GGFPAYSFGPGANVGRPARTLIPPTFFRDFAIGVAVKPNSAQGGVLFAITDAfQKVIYL 120
Cdd:smart00210 4 LLQVFDLPSLSFAIRQVVGPePGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNVRQF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 121 GLRLssveDGRQRVILYYTEpGSHVSREAAVFS-VPVMTNRWNRFAVTVQGEEVALFMDCEEQSQVRFQRSSWPltFEPS 199
Cdd:smart00210 83 GLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP--PIDT 155
|
170 180
....*....|....*....|....*....
gi 134288882 200 AGIFVGNAGAMGLERFTGSIQQLTIYSDP 228
Cdd:smart00210 156 DGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| Collagen_trimer |
pfam20010 |
Collagen trimerization domain; This small domain mediate trimerization in various collagen ... |
1114-1160 |
4.43e-19 |
|
Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.
Pssm-ID: 466257 Cd Length: 49 Bit Score: 81.88 E-value: 4.43e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 134288882 1114 VTALSDMGDMLQKAHLVIEGTFIYLRDSGEFFIRVRDGWKKLQLGEL 1160
Cdd:pfam20010 1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGEL 47
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
637-912 |
1.11e-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: 90.73 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 637 DGAPGEPGPQGPEGQpgldgaSGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGPPGKNGEVGTPgvmgppgppgppGPPG 716
Cdd:NF038329 116 DGEKGEPGPAGPAGP------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ------------GPAG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 717 PGCTTELgfeiegSGDVRLLSKPTISGPTSPSGPKGEKGEQGAKGERGADGtstmgppgprgppghvevlssslinitng 796
Cdd:NF038329 178 KDGEAGA------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAG----------------------------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 797 smnfsdiPELMGPPGPDGVPGLPGFPGPRGPKGDTGVPGFPGLKGEQGEKGEPGaiLTGDVPLEMMKGRKGEPGihgapg 876
Cdd:NF038329 223 -------EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG--PDGPDGKDGERGPVGPAG------ 287
|
250 260 270
....*....|....*....|....*....|....*.
gi 134288882 877 pmgpkgPPGHKGEFGLPGRPGRPGLNGLKGAKGDRG 912
Cdd:NF038329 288 ------KDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
641-690 |
2.52e-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: 57.12 E-value: 2.52e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 134288882 641 GEPGPQGPEGQPGLDGASGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGP 690
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
582-696 |
1.86e-08 |
|
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: 58.38 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 582 GPVGGLDEGSGSGDIVGNEDLLRGPPGPPGPPGSPGIPGKPgtdvfmGPPGSPGEDGAPGEPGPQGPEGQ------PGLD 655
Cdd:NF038329 213 GPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD------GPAGKDGPRGDRGEAGPDGPDGKdgergpVGPA 286
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 134288882 656 GASGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGPPGKNGE 696
Cdd:NF038329 287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
752-997 |
8.20e-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: 53.37 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 752 GEKGEQGAKGERGAdgtstmgppgpRGPpghvevlssslinitngsmnfsdipelmgppgpdgvpglpgfPGPRGPKGDT 831
Cdd:NF038329 117 GEKGEPGPAGPAGP-----------AGE------------------------------------------QGPRGDRGET 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 832 GVPGFPGLKGEQGEKGEPGAiltgdvplemmKGRKGEPgihgapgpmgpkgppghkGEFGLPGRPGRPGLNGLKGAKGDR 911
Cdd:NF038329 144 GPAGPAGPPGPQGERGEKGP-----------AGPQGEA------------------GPQGPAGKDGEAGAKGPAGEKGPQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 912 GVTLPGPPGLPGPPGPPGPPGAVVNIKGAvfPIPARPHCKTPVGTAHPGDPElvtfhGVKGEKGSWGLPGSKGEKGDQGA 991
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGE--DGPAGPAGDGQQGPDGDPGPT-----GEDGPQGPDGPAGKDGPRGDRGE 267
|
....*.
gi 134288882 992 QGPPGP 997
Cdd:NF038329 268 AGPDGP 273
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
72-224 |
4.79e-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: 47.80 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 72 GANVGRPARTLIPPTFF--RDFAIGVAVKPNSAQGgVLFAITDAFQKViYLGLRLssvEDGRqrVILYYtepgsHVSREA 149
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAprTRLSISFSFRTTSPNG-LLLYAGSQNGGD-FLALEL---EDGR--LVLRY-----DLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 150 AVFS--VPVMTNRWNRFAVTVQGEEVALFMDCEeqSQVRFQRSSWPLTFEPSAGIFVGNAGAMGL-------ERFTGSIQ 220
Cdd:cd00110 69 LVLSskTPLNDGQWHSVSVERNGRSVTLSVDGE--RVVESGSPGGSALLNLDGPLYLGGLPEDLKspglpvsPGFVGCIR 146
|
....
gi 134288882 221 QLTI 224
Cdd:cd00110 147 DLKV 150
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
90-235 |
2.28e-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: 45.84 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 90 DFAIGVAVKPNSAQGGVLFAITDAFQKVIYLGLRlssvEDGRQRVILYytepGSHVSREAAVFSVPVMTNRWNRFAVTVQ 169
Cdd:pfam13385 18 DFTVSAWVKPDSLPGWARAIISSSGGGGYSLGLD----GDGRLRFAVN----GGNGGWDTVTSGASVPLGQWTHVAVTYD 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134288882 170 GEEVALFMDCEEQSQVRFqrsSWPLTFEPSAGIFVGNAGAmGLERFTGSIQQLTIYSDPRTPEELC 235
Cdd:pfam13385 90 GGTLRLYVNGVLVGSSTL---TGGPPPGTGGPLYIGRSPG-GDDYFNGLIDEVRIYDRALSAAEIA 151
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
265-541 |
5.24e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 41.44 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 265 TQAPPKESHVDPISVPPTSSSPAEDSELSGEPVPEGTPETNLSIIGHSSPEqgsgeilndtlevhamdgDPGTDDGSGDg 344
Cdd:pfam05109 445 TTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPR------------------DNGTESKAPD- 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 345 allnVTDGQGLSATATGEASVPVTTVLE-AENGSMPT---GSPTLAMFTQS------IREVDTPDPeNLTTTASGDGEVP 414
Cdd:pfam05109 506 ----MTSPTSAVTTPTPNATSPTPAVTTpTPNATSPTlgkTSPTSAVTTPTpnatspTPAVTTPTP-NATIPTLGKTSPT 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 415 TSTDGDTEADSSPTGGPTlKPREEATLGSHGEEWLTPAVSKMP---LKAFEEEEASGTAIDSLDVIFTPTVVLEQVSRRP 491
Cdd:pfam05109 581 SAVTTPTPNATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPknaTSAVTTGQHNITSSSTSSMSLRPSSISETLSPST 659
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 134288882 492 TDIQATFTPTVVLEETSG---------APTDTQDALTPTVAPEQMFTAEPTDGGDLVAS 541
Cdd:pfam05109 660 SDNSTSHMPLLTSAHPTGgenitqvtpASTSTHHVSTSSPAPRPGTTSQASGPGNSSTS 718
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
629-696 |
9.26e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.95 E-value: 9.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134288882 629 GPPGSPGEDGAPGEPGPQGPEGQPGLDGASGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGPPGKNGE 696
Cdd:PHA03169 135 SPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSP 202
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Endostatin |
pfam06482 |
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ... |
1197-1361 |
3.73e-111 |
|
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: 346.74 E-value: 3.73e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 1197 LHLVALNTPVAGDIR----ADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFGLPIVNLKGQVLFNNWDSIFSG 1272
Cdd:pfam06482 1 LHLIALNTPQSGDMRgirgADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 1273 DGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCANRL 1352
Cdd:pfam06482 81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160
|
....*....
gi 134288882 1353 IVLCIENSF 1361
Cdd:pfam06482 161 IVLCIENSY 169
|
|
| Endostatin-like |
cd00247 |
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ... |
1194-1360 |
5.74e-111 |
|
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: 346.24 E-value: 5.74e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 1194 RPVLHLVALNTPVAGDIR----ADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFGLPIVNLKGQVLFNNWDSI 1269
Cdd:cd00247 1 QPVLHLVALNTPLSGDMRgirgADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 1270 FSGDGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCA 1349
Cdd:cd00247 81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160
|
170
....*....|.
gi 134288882 1350 NRLIVLCIENS 1360
Cdd:cd00247 161 NKLIVLCIENS 171
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
42-228 |
1.61e-43 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 156.75 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 42 DLTVLIGVPLPSSVSFTTGY-GGFPAYSFGPGANVGRPARTLIPPTFFRDFAIGVAVKPNSAQGGVLFAITDAfQKVIYL 120
Cdd:smart00210 4 LLQVFDLPSLSFAIRQVVGPePGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNVRQF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 121 GLRLssveDGRQRVILYYTEpGSHVSREAAVFS-VPVMTNRWNRFAVTVQGEEVALFMDCEEQSQVRFQRSSWPltFEPS 199
Cdd:smart00210 83 GLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP--PIDT 155
|
170 180
....*....|....*....|....*....
gi 134288882 200 AGIFVGNAGAMGLERFTGSIQQLTIYSDP 228
Cdd:smart00210 156 DGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| Collagen_trimer |
pfam20010 |
Collagen trimerization domain; This small domain mediate trimerization in various collagen ... |
1114-1160 |
4.43e-19 |
|
Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.
Pssm-ID: 466257 Cd Length: 49 Bit Score: 81.88 E-value: 4.43e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 134288882 1114 VTALSDMGDMLQKAHLVIEGTFIYLRDSGEFFIRVRDGWKKLQLGEL 1160
Cdd:pfam20010 1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGEL 47
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
637-912 |
1.11e-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: 90.73 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 637 DGAPGEPGPQGPEGQpgldgaSGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGPPGKNGEVGTPgvmgppgppgppGPPG 716
Cdd:NF038329 116 DGEKGEPGPAGPAGP------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQ------------GPAG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 717 PGCTTELgfeiegSGDVRLLSKPTISGPTSPSGPKGEKGEQGAKGERGADGtstmgppgprgppghvevlssslinitng 796
Cdd:NF038329 178 KDGEAGA------KGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAG----------------------------- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 797 smnfsdiPELMGPPGPDGVPGLPGFPGPRGPKGDTGVPGFPGLKGEQGEKGEPGaiLTGDVPLEMMKGRKGEPGihgapg 876
Cdd:NF038329 223 -------EDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAG--PDGPDGKDGERGPVGPAG------ 287
|
250 260 270
....*....|....*....|....*....|....*.
gi 134288882 877 pmgpkgPPGHKGEFGLPGRPGRPGLNGLKGAKGDRG 912
Cdd:NF038329 288 ------KDGQNGKDGLPGKDGKDGQNGKDGLPGKDG 317
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
641-690 |
2.52e-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: 57.12 E-value: 2.52e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 134288882 641 GEPGPQGPEGQPGLDGASGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGP 690
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGA 50
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
631-673 |
1.06e-08 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 52.50 E-value: 1.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 134288882 631 PGSPGEDGAPGEPGPQGPEGQPGLDGASGQQGMKGEKGARGPN 673
Cdd:pfam01391 15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
582-696 |
1.86e-08 |
|
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: 58.38 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 582 GPVGGLDEGSGSGDIVGNEDLLRGPPGPPGPPGSPGIPGKPgtdvfmGPPGSPGEDGAPGEPGPQGPEGQ------PGLD 655
Cdd:NF038329 213 GPDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPD------GPAGKDGPRGDRGEAGPDGPDGKdgergpVGPA 286
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 134288882 656 GASGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGPPGKNGE 696
Cdd:NF038329 287 GKDGQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGL 327
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
752-997 |
8.20e-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: 53.37 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 752 GEKGEQGAKGERGAdgtstmgppgpRGPpghvevlssslinitngsmnfsdipelmgppgpdgvpglpgfPGPRGPKGDT 831
Cdd:NF038329 117 GEKGEPGPAGPAGP-----------AGE------------------------------------------QGPRGDRGET 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 832 GVPGFPGLKGEQGEKGEPGAiltgdvplemmKGRKGEPgihgapgpmgpkgppghkGEFGLPGRPGRPGLNGLKGAKGDR 911
Cdd:NF038329 144 GPAGPAGPPGPQGERGEKGP-----------AGPQGEA------------------GPQGPAGKDGEAGAKGPAGEKGPQ 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 912 GVTLPGPPGLPGPPGPPGPPGAVVNIKGAvfPIPARPHCKTPVGTAHPGDPElvtfhGVKGEKGSWGLPGSKGEKGDQGA 991
Cdd:NF038329 195 GPRGETGPAGEQGPAGPAGPDGEAGPAGE--DGPAGPAGDGQQGPDGDPGPT-----GEDGPQGPDGPAGKDGPRGDRGE 267
|
....*.
gi 134288882 992 QGPPGP 997
Cdd:NF038329 268 AGPDGP 273
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
72-224 |
4.79e-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: 47.80 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 72 GANVGRPARTLIPPTFF--RDFAIGVAVKPNSAQGgVLFAITDAFQKViYLGLRLssvEDGRqrVILYYtepgsHVSREA 149
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAprTRLSISFSFRTTSPNG-LLLYAGSQNGGD-FLALEL---EDGR--LVLRY-----DLGSGS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 150 AVFS--VPVMTNRWNRFAVTVQGEEVALFMDCEeqSQVRFQRSSWPLTFEPSAGIFVGNAGAMGL-------ERFTGSIQ 220
Cdd:cd00110 69 LVLSskTPLNDGQWHSVSVERNGRSVTLSVDGE--RVVESGSPGGSALLNLDGPLYLGGLPEDLKspglpvsPGFVGCIR 146
|
....
gi 134288882 221 QLTI 224
Cdd:cd00110 147 DLKV 150
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
90-235 |
2.28e-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: 45.84 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 90 DFAIGVAVKPNSAQGGVLFAITDAFQKVIYLGLRlssvEDGRQRVILYytepGSHVSREAAVFSVPVMTNRWNRFAVTVQ 169
Cdd:pfam13385 18 DFTVSAWVKPDSLPGWARAIISSSGGGGYSLGLD----GDGRLRFAVN----GGNGGWDTVTSGASVPLGQWTHVAVTYD 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 134288882 170 GEEVALFMDCEEQSQVRFqrsSWPLTFEPSAGIFVGNAGAmGLERFTGSIQQLTIYSDPRTPEELC 235
Cdd:pfam13385 90 GGTLRLYVNGVLVGSSTL---TGGPPPGTGGPLYIGRSPG-GDDYFNGLIDEVRIYDRALSAAEIA 151
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
653-763 |
3.13e-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: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 653 GLDGASGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGPPGkngevgtpgvmgppgppgppgppgpgcttelgfeiegsgd 732
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG---------------------------------------- 40
|
90 100 110
....*....|....*....|....*....|.
gi 134288882 733 vrllskptisgptsPSGPKGEKGEQGAKGER 763
Cdd:pfam01391 41 --------------PPGPPGPPGAPGAPGPP 57
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
823-912 |
1.34e-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: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 823 GPRGPKGDTGVPGFPGLKGEQGEKGEPgailtgdvplemmkgrkgepgihgapgpmgpkgppGHKGEFGLPGRPGRPGLN 902
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPP-----------------------------------GPPGEPGPPGPPGPPGPP 45
|
90
....*....|
gi 134288882 903 GLKGAKGDRG 912
Cdd:pfam01391 46 GPPGAPGAPG 55
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
822-852 |
4.55e-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: 36.70 E-value: 4.55e-03
10 20 30
....*....|....*....|....*....|.
gi 134288882 822 PGPRGPKGDTGVPGFPGLKGEQGEKGEPGAI 852
Cdd:pfam01391 21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
265-541 |
5.24e-03 |
|
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.
Pssm-ID: 282904 [Multi-domain] Cd Length: 886 Bit Score: 41.44 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 265 TQAPPKESHVDPISVPPTSSSPAEDSELSGEPVPEGTPETNLSIIGHSSPEqgsgeilndtlevhamdgDPGTDDGSGDg 344
Cdd:pfam05109 445 TTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPR------------------DNGTESKAPD- 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 345 allnVTDGQGLSATATGEASVPVTTVLE-AENGSMPT---GSPTLAMFTQS------IREVDTPDPeNLTTTASGDGEVP 414
Cdd:pfam05109 506 ----MTSPTSAVTTPTPNATSPTPAVTTpTPNATSPTlgkTSPTSAVTTPTpnatspTPAVTTPTP-NATIPTLGKTSPT 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134288882 415 TSTDGDTEADSSPTGGPTlKPREEATLGSHGEEWLTPAVSKMP---LKAFEEEEASGTAIDSLDVIFTPTVVLEQVSRRP 491
Cdd:pfam05109 581 SAVTTPTPNATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPknaTSAVTTGQHNITSSSTSSMSLRPSSISETLSPST 659
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 134288882 492 TDIQATFTPTVVLEETSG---------APTDTQDALTPTVAPEQMFTAEPTDGGDLVAS 541
Cdd:pfam05109 660 SDNSTSHMPLLTSAHPTGgenitqvtpASTSTHHVSTSSPAPRPGTTSQASGPGNSSTS 718
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
821-870 |
9.25e-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: 35.93 E-value: 9.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 134288882 821 FPGPRGPKGDTGVPGFPGLKGEQGEKGEPGAiltgdvplemmKGRKGEPG 870
Cdd:pfam01391 17 PPGPPGPPGPPGPPGEPGPPGPPGPPGPPGP-----------PGAPGAPG 55
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
629-696 |
9.26e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 39.95 E-value: 9.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 134288882 629 GPPGSPGEDGAPGEPGPQGPEGQPGLDGASGQQGMKGEKGARGPNGSAGEKGDPGNRGLPGPPGKNGE 696
Cdd:PHA03169 135 SPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSP 202
|
|
| |
