|
Name |
Accession |
Description |
Interval |
E-value |
| Endostatin |
pfam06482 |
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ... |
1175-1339 |
2.13e-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: 347.12 E-value: 2.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 1175 LHLVALNTPVAGDIR----ADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFSLPIVNLKGQVLFNNWDSIFSG 1250
Cdd:pfam06482 1 LHLIALNTPQSGDMRgirgADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 1251 DGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCANRL 1330
Cdd:pfam06482 81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160
|
....*....
gi 407228400 1331 IVLCIENSF 1339
Cdd:pfam06482 161 IVLCIENSY 169
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
40-228 |
7.19e-45 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
:
Pssm-ID: 214560 Cd Length: 184 Bit Score: 160.60 E-value: 7.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 40 HLDLTELIGVP-LPSSVSFVTGY-GGFPAYSFRPGANVGRPARTLIPSTFFRDFAIGVAVKPSSAQGGVLFAVTDAfQKV 117
Cdd:smart00210 1 GQDLLQVFDLPsLSFAIRQVVGPePGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 118 IYLGLRLsrveDGRQRVILYYTEpGSHVSQEAAAFS-VPVMTNRWNRFAVTVQGEEAVLFMDCEEHSQVLFQRSSRPltF 196
Cdd:smart00210 80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP--P 152
|
170 180 190
....*....|....*....|....*....|..
gi 407228400 197 EPSAGIFVGNAGATGLERFTGSIQQLIIYSDP 228
Cdd:smart00210 153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| Collagen_trimer |
pfam20010 |
Collagen trimerization domain; This small domain mediate trimerization in various collagen ... |
1092-1138 |
7.31e-19 |
|
Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.
:
Pssm-ID: 466257 Cd Length: 49 Bit Score: 81.11 E-value: 7.31e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 407228400 1092 VTALSDMGDMLQKAHLVIEGTFIYLRESGEFFLRVRDGWKKLQLGEL 1138
Cdd:pfam20010 1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGEL 47
|
|
| gly_rich_SclB super family |
cl45768 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
579-890 |
9.55e-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: 87.65 E-value: 9.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 579 DLLRGPPGPpgppgspgipgkpgtdvfVGPPGSPGEDGAPGEPGPQGPEGQPGLDGASGQPGMKGEKGARGPNGSVGEKG 658
Cdd:NF038329 116 DGEKGEPGP------------------AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 659 DPGSRGLPGPPGKNGEVGIPGAMGPPGPPGPPGPPGPgcttklgfeiEGSGDTQLLSKPRISGPSSPSGPKGEKGEQGAK 738
Cdd:NF038329 178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP----------DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 739 GERGTDGIstmgppgprgppgrvevlssslinitngsmnfsdipelmgppgpdgvpglpgfPGPRGPKGDTGVPGFPGLK 818
Cdd:NF038329 248 GPQGPDGP-----------------------------------------------------AGKDGPRGDRGEAGPDGPD 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407228400 819 GEQGEKGEPGAiltgdiplemvKGRKGEpgvhgapgpmgpkgppghKGEFGLPGRPGRPGLNGLKGAKGDRG 890
Cdd:NF038329 275 GKDGERGPVGP-----------AGKDGQ------------------NGKDGLPGKDGKDGQNGKDGLPGKDG 317
|
|
| Herpes_BLLF1 super family |
cl37540 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
265-546 |
7.82e-05 |
|
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: 47.22 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 265 TQAPPKEAHVDPISMPPTSSSPTEDTELSGEPVPEGTPGTDLSITGHSSP-EQGSGEILNDTLEVRTVDGNPSTDGGSGD 343
Cdd:pfam05109 445 TTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPrDNGTESKAPDMTSPTSAVTTPTPNATSPT 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 344 GALLNVTdgqglsATATGETRVPVTTALEVENGSMPTGSPTLAMFTQSfrevdmldlENLTTASGDGEVPTS-TDVDTEA 422
Cdd:pfam05109 525 PAVTTPT------PNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT---------PNATIPTLGKTSPTSaVTTPTPN 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 423 GTLPTGGPTlKPREEATLGSLGEEWSTTVVSKVPLNAFE-----EEEASGTAIDSLdAFTPTVVLEQASGTPTDiqaalT 497
Cdd:pfam05109 590 ATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPKNATSavttgQHNITSSSTSSM-SLRPSSISETLSPSTSD-----N 662
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 407228400 498 TTVAPEQVFTAAPTDGEDLVTSTEESDEEGSGSTlpiGPPLSKPTVTPE 546
Cdd:pfam05109 663 STSHMPLLTSAHPTGGENITQVTPASTSTHHVST---SSPAPRPGTTSQ 708
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Endostatin |
pfam06482 |
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ... |
1175-1339 |
2.13e-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: 347.12 E-value: 2.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 1175 LHLVALNTPVAGDIR----ADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFSLPIVNLKGQVLFNNWDSIFSG 1250
Cdd:pfam06482 1 LHLIALNTPQSGDMRgirgADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 1251 DGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCANRL 1330
Cdd:pfam06482 81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160
|
....*....
gi 407228400 1331 IVLCIENSF 1339
Cdd:pfam06482 161 IVLCIENSY 169
|
|
| Endostatin-like |
cd00247 |
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ... |
1172-1338 |
2.73e-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: 346.63 E-value: 2.73e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 1172 RPVLHLVALNTPVAGDIR----ADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFSLPIVNLKGQVLFNNWDSI 1247
Cdd:cd00247 1 QPVLHLVALNTPLSGDMRgirgADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 1248 FSGDGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCA 1327
Cdd:cd00247 81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160
|
170
....*....|.
gi 407228400 1328 NRLIVLCIENS 1338
Cdd:cd00247 161 NKLIVLCIENS 171
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
40-228 |
7.19e-45 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 160.60 E-value: 7.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 40 HLDLTELIGVP-LPSSVSFVTGY-GGFPAYSFRPGANVGRPARTLIPSTFFRDFAIGVAVKPSSAQGGVLFAVTDAfQKV 117
Cdd:smart00210 1 GQDLLQVFDLPsLSFAIRQVVGPePGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 118 IYLGLRLsrveDGRQRVILYYTEpGSHVSQEAAAFS-VPVMTNRWNRFAVTVQGEEAVLFMDCEEHSQVLFQRSSRPltF 196
Cdd:smart00210 80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP--P 152
|
170 180 190
....*....|....*....|....*....|..
gi 407228400 197 EPSAGIFVGNAGATGLERFTGSIQQLIIYSDP 228
Cdd:smart00210 153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| Collagen_trimer |
pfam20010 |
Collagen trimerization domain; This small domain mediate trimerization in various collagen ... |
1092-1138 |
7.31e-19 |
|
Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.
Pssm-ID: 466257 Cd Length: 49 Bit Score: 81.11 E-value: 7.31e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 407228400 1092 VTALSDMGDMLQKAHLVIEGTFIYLRESGEFFLRVRDGWKKLQLGEL 1138
Cdd:pfam20010 1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGEL 47
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
579-890 |
9.55e-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: 87.65 E-value: 9.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 579 DLLRGPPGPpgppgspgipgkpgtdvfVGPPGSPGEDGAPGEPGPQGPEGQPGLDGASGQPGMKGEKGARGPNGSVGEKG 658
Cdd:NF038329 116 DGEKGEPGP------------------AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 659 DPGSRGLPGPPGKNGEVGIPGAMGPPGPPGPPGPPGPgcttklgfeiEGSGDTQLLSKPRISGPSSPSGPKGEKGEQGAK 738
Cdd:NF038329 178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP----------DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 739 GERGTDGIstmgppgprgppgrvevlssslinitngsmnfsdipelmgppgpdgvpglpgfPGPRGPKGDTGVPGFPGLK 818
Cdd:NF038329 248 GPQGPDGP-----------------------------------------------------AGKDGPRGDRGEAGPDGPD 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407228400 819 GEQGEKGEPGAiltgdiplemvKGRKGEpgvhgapgpmgpkgppghKGEFGLPGRPGRPGLNGLKGAKGDRG 890
Cdd:NF038329 275 GKDGERGPVGP-----------AGKDGQ------------------NGKDGLPGKDGKDGQNGKDGLPGKDG 317
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
619-669 |
1.33e-11 |
|
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: 60.59 E-value: 1.33e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 407228400 619 GEPGPQGPEGQPGLDGASGQPGMKGEKGARGPNGSVGEKGDPGSRGLPGPP 669
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
578-745 |
2.28e-11 |
|
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: 67.62 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 578 EDLLRGPPGPPGPPGSPGIPGKPGTDVFVGPPGSPGEDGAPGEPGPQGPEG--QPGLDGASGQPGMKGEKGARGPNGSVG 655
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 656 EKGDPGSRGLPGPPGKNGEVGIPGamgppgppgppgppgpgcttKLGFEIEGSGDtqllskprisGPSSPSGPKGEKGEQ 735
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVG--------------------PAGKDGQNGKD----------GLPGKDGKDGQNGKD 310
|
170
....*....|
gi 407228400 736 GAKGERGTDG 745
Cdd:NF038329 311 GLPGKDGKDG 320
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
615-976 |
8.32e-10 |
|
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: 62.62 E-value: 8.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 615 DGAPGEPGPQGPEGQpgldgaSGQPGMKGEKGARGPNGSVGEKGDPGSRGLPGPPGKNGevgipgamgppgppgppgppg 694
Cdd:NF038329 116 DGEKGEPGPAGPAGP------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG--------------------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 695 pgcttklgfeiegsgdtqllskprisgpssPSGPKGEKGEQgakgergtdgistmgppgprgppgrvevlssslinitng 774
Cdd:NF038329 169 ------------------------------EAGPQGPAGKD--------------------------------------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 775 smnfsdipelmgppgpdGVPGLPgfpGPRGPKGDTGVPGFPGLKGEQGEKGEPGAilTGDIPLEMVKGRKGEPGvhgapg 854
Cdd:NF038329 180 -----------------GEAGAK---GPAGEKGPQGPRGETGPAGEQGPAGPAGP--DGEAGPAGEDGPAGPAG------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 855 pMGPKGPPGHKGEFGLPGRPGRPGLNGLKGAKGDRGImlpgppglpgppgppgppgavvnikgavfPIPARPHCKT---- 930
Cdd:NF038329 232 -DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE-----------------------------AGPDGPDGKDgerg 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 407228400 931 PVGTA----HPGDPELVTFHGVKGEKGSWGLPGTKGEKGDQGAQGPPGPP 976
Cdd:NF038329 282 PVGPAgkdgQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD 331
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
265-546 |
7.82e-05 |
|
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: 47.22 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 265 TQAPPKEAHVDPISMPPTSSSPTEDTELSGEPVPEGTPGTDLSITGHSSP-EQGSGEILNDTLEVRTVDGNPSTDGGSGD 343
Cdd:pfam05109 445 TTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPrDNGTESKAPDMTSPTSAVTTPTPNATSPT 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 344 GALLNVTdgqglsATATGETRVPVTTALEVENGSMPTGSPTLAMFTQSfrevdmldlENLTTASGDGEVPTS-TDVDTEA 422
Cdd:pfam05109 525 PAVTTPT------PNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT---------PNATIPTLGKTSPTSaVTTPTPN 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 423 GTLPTGGPTlKPREEATLGSLGEEWSTTVVSKVPLNAFE-----EEEASGTAIDSLdAFTPTVVLEQASGTPTDiqaalT 497
Cdd:pfam05109 590 ATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPKNATSavttgQHNITSSSTSSM-SLRPSSISETLSPSTSD-----N 662
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 407228400 498 TTVAPEQVFTAAPTDGEDLVTSTEESDEEGSGSTlpiGPPLSKPTVTPE 546
Cdd:pfam05109 663 STSHMPLLTSAHPTGGENITQVTPASTSTHHVST---SSPAPRPGTTSQ 708
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
84-224 |
1.94e-04 |
|
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: 43.18 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 84 PSTFFRDFAIGVAVKPSSAQGgVLFAVTDAFQKViYLGLRLsrvEDGRqrVILYY-TEPGSHVSQeaaaFSVPVMTNRWN 162
Cdd:cd00110 15 LPAPRTRLSISFSFRTTSPNG-LLLYAGSQNGGD-FLALEL---EDGR--LVLRYdLGSGSLVLS----SKTPLNDGQWH 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407228400 163 RFAVTVQGEEAVLFMDCEEHSQVLFQRSSRPLtfEPSAGIFVGNA-------GATGLERFTGSIQQLII 224
Cdd:cd00110 84 SVSVERNGRSVTLSVDGERVVESGSPGGSALL--NLDGPLYLGGLpedlkspGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
90-235 |
7.59e-04 |
|
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: 41.60 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 90 DFAIGVAVKPSSAQGGVLFAVTDAFQKVIYLGLRlsrvEDGRQRVILYytepGSHVSQEAAAFSVPVMTNRWNRFAVTVQ 169
Cdd:pfam13385 18 DFTVSAWVKPDSLPGWARAIISSSGGGGYSLGLD----GDGRLRFAVN----GGNGGWDTVTSGASVPLGQWTHVAVTYD 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407228400 170 GEEAVLFMDCEEhsqvlfqRSSRPLTFEP---SAGIFVGNAGATGLERFTGSIQQLIIYSDPRTPEELC 235
Cdd:pfam13385 90 GGTLRLYVNGVL-------VGSSTLTGGPppgTGGPLYIGRSPGGDDYFNGLIDEVRIYDRALSAAEIA 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Endostatin |
pfam06482 |
Collagenase NC10 and Endostatin; NC10 stands for Non-helical region 10 and is taken from Swiss: ... |
1175-1339 |
2.13e-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: 347.12 E-value: 2.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 1175 LHLVALNTPVAGDIR----ADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFSLPIVNLKGQVLFNNWDSIFSG 1250
Cdd:pfam06482 1 LHLIALNTPQSGDMRgirgADFLCFQQARAAGLKGTFRAFLSSRLQDLYSIVRKADRENVPIVNLKDEVLFDSWESIFSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 1251 DGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCANRL 1330
Cdd:pfam06482 81 SGGQMKPNVPIYSFDGRDVLRDPAWPQKMVWHGSTSKGHRLTDNYCEAWRTGDQAVTGQASSLQSGKLLQQSPSSCSNSY 160
|
....*....
gi 407228400 1331 IVLCIENSF 1339
Cdd:pfam06482 161 IVLCIENSY 169
|
|
| Endostatin-like |
cd00247 |
Endostatin-like domain; the angiogenesis inhibitor endostatin is a C-terminal fragment of ... |
1172-1338 |
2.73e-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: 346.63 E-value: 2.73e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 1172 RPVLHLVALNTPVAGDIR----ADFQCFQQARAAGLLSTFRAFLSSHLQDLSTVVRKAERFSLPIVNLKGQVLFNNWDSI 1247
Cdd:cd00247 1 QPVLHLVALNTPLSGDMRgirgADFQCFQQARAAGLKGTFRAFLSSRLQDLYSIVRRADRDSLPIVNLKGEVLFNSWESL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 1248 FSGDGGQFNTHIPIYSFDGRDVMTDPSWPQKVVWHGSNPHGVRLVDKYCEAWRTTDMAVTGFASPLSTGKILDQKAYSCA 1327
Cdd:cd00247 81 FSGSGGQFNPGARIYSFDGRDVLTDPAWPQKMVWHGSDPNGRRLTDSYCEAWRTGDSAVTGQASSLSSGKLLEQKAYSCE 160
|
170
....*....|.
gi 407228400 1328 NRLIVLCIENS 1338
Cdd:cd00247 161 NKLIVLCIENS 171
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
40-228 |
7.19e-45 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 160.60 E-value: 7.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 40 HLDLTELIGVP-LPSSVSFVTGY-GGFPAYSFRPGANVGRPARTLIPSTFFRDFAIGVAVKPSSAQGGVLFAVTDAfQKV 117
Cdd:smart00210 1 GQDLLQVFDLPsLSFAIRQVVGPePGSPAYRLGDPALVPQPTRDLFPSGLPEDFSLLTTFRQTPKSRGVLFAIYDA-QNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 118 IYLGLRLsrveDGRQRVILYYTEpGSHVSQEAAAFS-VPVMTNRWNRFAVTVQGEEAVLFMDCEEHSQVLFQRSSRPltF 196
Cdd:smart00210 80 RQFGLEV----DGRANTLLLRYQ-GVDGKQHTVSFRnLPLADGQWHKLALSVSGSSATLYVDCNEIDSRPLDRPGQP--P 152
|
170 180 190
....*....|....*....|....*....|..
gi 407228400 197 EPSAGIFVGNAGATGLERFTGSIQQLIIYSDP 228
Cdd:smart00210 153 IDTDGIEVRGAQAADRKPFQGDLQQLKIVCDP 184
|
|
| Collagen_trimer |
pfam20010 |
Collagen trimerization domain; This small domain mediate trimerization in various collagen ... |
1092-1138 |
7.31e-19 |
|
Collagen trimerization domain; This small domain mediate trimerization in various collagen proteins.
Pssm-ID: 466257 Cd Length: 49 Bit Score: 81.11 E-value: 7.31e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 407228400 1092 VTALSDMGDMLQKAHLVIEGTFIYLRESGEFFLRVRDGWKKLQLGEL 1138
Cdd:pfam20010 1 VTVFQNYDTMLQKTHRVPEGTLVYVREREELYIRVRNGWRKIQLGEL 47
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
579-890 |
9.55e-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: 87.65 E-value: 9.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 579 DLLRGPPGPpgppgspgipgkpgtdvfVGPPGSPGEDGAPGEPGPQGPEGQPGLDGASGQPGMKGEKGARGPNGSVGEKG 658
Cdd:NF038329 116 DGEKGEPGP------------------AGPAGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 659 DPGSRGLPGPPGKNGEVGIPGAMGPPGPPGPPGPPGPgcttklgfeiEGSGDTQLLSKPRISGPSSPSGPKGEKGEQGAK 738
Cdd:NF038329 178 KDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGP----------DGEAGPAGEDGPAGPAGDGQQGPDGDPGPTGED 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 739 GERGTDGIstmgppgprgppgrvevlssslinitngsmnfsdipelmgppgpdgvpglpgfPGPRGPKGDTGVPGFPGLK 818
Cdd:NF038329 248 GPQGPDGP-----------------------------------------------------AGKDGPRGDRGEAGPDGPD 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407228400 819 GEQGEKGEPGAiltgdiplemvKGRKGEpgvhgapgpmgpkgppghKGEFGLPGRPGRPGLNGLKGAKGDRG 890
Cdd:NF038329 275 GKDGERGPVGP-----------AGKDGQ------------------NGKDGLPGKDGKDGQNGKDGLPGKDG 317
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
619-669 |
1.33e-11 |
|
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: 60.59 E-value: 1.33e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 407228400 619 GEPGPQGPEGQPGLDGASGQPGMKGEKGARGPNGSVGEKGDPGSRGLPGPP 669
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
578-745 |
2.28e-11 |
|
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: 67.62 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 578 EDLLRGPPGPPGPPGSPGIPGKPGTDVFVGPPGSPGEDGAPGEPGPQGPEG--QPGLDGASGQPGMKGEKGARGPNGSVG 655
Cdd:NF038329 181 EAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAGdgQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 656 EKGDPGSRGLPGPPGKNGEVGIPGamgppgppgppgppgpgcttKLGFEIEGSGDtqllskprisGPSSPSGPKGEKGEQ 735
Cdd:NF038329 261 PRGDRGEAGPDGPDGKDGERGPVG--------------------PAGKDGQNGKD----------GLPGKDGKDGQNGKD 310
|
170
....*....|
gi 407228400 736 GAKGERGTDG 745
Cdd:NF038329 311 GLPGKDGKDG 320
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
616-674 |
2.56e-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: 2.56e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 407228400 616 GAPGEPGPQGPEGQPGLDGASGQPGMKGEKGARGPngsvgekgdPGSRGLPGPPGKNGE 674
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGP---------PGPPGPPGPPGPPGA 50
|
|
| gly_rich_SclB |
NF038329 |
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ... |
615-976 |
8.32e-10 |
|
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: 62.62 E-value: 8.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 615 DGAPGEPGPQGPEGQpgldgaSGQPGMKGEKGARGPNGSVGEKGDPGSRGLPGPPGKNGevgipgamgppgppgppgppg 694
Cdd:NF038329 116 DGEKGEPGPAGPAGP------AGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQG--------------------- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 695 pgcttklgfeiegsgdtqllskprisgpssPSGPKGEKGEQgakgergtdgistmgppgprgppgrvevlssslinitng 774
Cdd:NF038329 169 ------------------------------EAGPQGPAGKD--------------------------------------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 775 smnfsdipelmgppgpdGVPGLPgfpGPRGPKGDTGVPGFPGLKGEQGEKGEPGAilTGDIPLEMVKGRKGEPGvhgapg 854
Cdd:NF038329 180 -----------------GEAGAK---GPAGEKGPQGPRGETGPAGEQGPAGPAGP--DGEAGPAGEDGPAGPAG------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 855 pMGPKGPPGHKGEFGLPGRPGRPGLNGLKGAKGDRGImlpgppglpgppgppgppgavvnikgavfPIPARPHCKT---- 930
Cdd:NF038329 232 -DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGE-----------------------------AGPDGPDGKDgerg 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 407228400 931 PVGTA----HPGDPELVTFHGVKGEKGSWGLPGTKGEKGDQGAQGPPGPP 976
Cdd:NF038329 282 PVGPAgkdgQNGKDGLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKD 331
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
609-651 |
1.94e-09 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 54.81 E-value: 1.94e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 407228400 609 PGSPGEDGAPGEPGPQGPEGQPGLDGASGQPGMKGEKGARGPN 651
Cdd:pfam01391 15 PGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
|
|
| Herpes_BLLF1 |
pfam05109 |
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ... |
265-546 |
7.82e-05 |
|
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: 47.22 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 265 TQAPPKEAHVDPISMPPTSSSPTEDTELSGEPVPEGTPGTDLSITGHSSP-EQGSGEILNDTLEVRTVDGNPSTDGGSGD 343
Cdd:pfam05109 445 TTGLPSSTHVPTNLTAPASTGPTVSTADVTSPTPAGTTSGASPVTPSPSPrDNGTESKAPDMTSPTSAVTTPTPNATSPT 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 344 GALLNVTdgqglsATATGETRVPVTTALEVENGSMPTGSPTLAMFTQSfrevdmldlENLTTASGDGEVPTS-TDVDTEA 422
Cdd:pfam05109 525 PAVTTPT------PNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT---------PNATIPTLGKTSPTSaVTTPTPN 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 423 GTLPTGGPTlKPREEATLGSLGEEWSTTVVSKVPLNAFE-----EEEASGTAIDSLdAFTPTVVLEQASGTPTDiqaalT 497
Cdd:pfam05109 590 ATSPTVGET-SPQANTTNHTLGGTSSTPVVTSPPKNATSavttgQHNITSSSTSSM-SLRPSSISETLSPSTSD-----N 662
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 407228400 498 TTVAPEQVFTAAPTDGEDLVTSTEESDEEGSGSTlpiGPPLSKPTVTPE 546
Cdd:pfam05109 663 STSHMPLLTSAHPTGGENITQVTPASTSTHHVST---SSPAPRPGTTSQ 708
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
801-890 |
1.05e-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: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 801 GPRGPKGDTGVPGFPGLKGEQGEKGEPgailtgdiplemvkgrkgepgvhgapgpmgpkgppGHKGEFGLPGRPGRPGLN 880
Cdd:pfam01391 1 GPPGPPGPPGPPGPPGPPGPPGPPGPP-----------------------------------GPPGEPGPPGPPGPPGPP 45
|
90
....*....|
gi 407228400 881 GLKGAKGDRG 890
Cdd:pfam01391 46 GPPGAPGAPG 55
|
|
| DUF5585 |
pfam17823 |
Family of unknown function (DUF5585); This is a family of unknown function found in chordata. |
253-550 |
1.28e-04 |
|
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
Pssm-ID: 465521 [Multi-domain] Cd Length: 506 Bit Score: 46.11 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 253 DEVAEIMEAVTYTQAPPKEAHVDP--ISMPPTSSSPTEDTELSGEP--VPEGTPGTDLSITGHSSPEQGSGEILNDTLEV 328
Cdd:pfam17823 108 DGAASRALAAAASSSPSSAAQSLPaaIAALPSEAFSAPRAAACRANasAAPRAAIAAASAPHAASPAPRTAASSTTAASS 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 329 RTVDGNPSTDGGSGDGALLNVTDGQGLSATATGetrvpvTTALEVENGSMPTGSPTLAMFTQSFREVDMLDLENLTTASG 408
Cdd:pfam17823 188 TTAASSAPTTAASSAPATLTPARGISTAATATG------HPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAG 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 409 dgevptstDVDTEAGTLPTGGPTlkpreeATLGSLGEEWSTTVVSKVPLnAFEEEEASGTAID-SLDafTPTVvleqaSG 487
Cdd:pfam17823 262 --------TVASAAGTINMGDPH------ARRLSPAKHMPSDTMARNPA-APMGAQAQGPIIQvSTD--QPVH-----NT 319
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407228400 488 TPTDIQAALTTTVAPEQVFTAAPTDGEdLVTSTEESDEEGSGSTLPIgPPLSKptvTPERQVT 550
Cdd:pfam17823 320 AGEPTPSPSNTTLEPNTPKSVASTNLA-VVTTTKAQAKEPSASPVPV-LHTSM---IPEVEAT 377
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
800-829 |
1.79e-04 |
|
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.
Pssm-ID: 460189 [Multi-domain] Cd Length: 57 Bit Score: 40.55 E-value: 1.79e-04
10 20 30
....*....|....*....|....*....|
gi 407228400 800 PGPRGPKGDTGVPGFPGLKGEQGEKGEPGA 829
Cdd:pfam01391 9 PGPPGPPGPPGPPGPPGPPGPPGEPGPPGP 38
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| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
84-224 |
1.94e-04 |
|
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: 43.18 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 84 PSTFFRDFAIGVAVKPSSAQGgVLFAVTDAFQKViYLGLRLsrvEDGRqrVILYY-TEPGSHVSQeaaaFSVPVMTNRWN 162
Cdd:cd00110 15 LPAPRTRLSISFSFRTTSPNG-LLLYAGSQNGGD-FLALEL---EDGR--LVLRYdLGSGSLVLS----SKTPLNDGQWH 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407228400 163 RFAVTVQGEEAVLFMDCEEHSQVLFQRSSRPLtfEPSAGIFVGNA-------GATGLERFTGSIQQLII 224
Cdd:cd00110 84 SVSVERNGRSVTLSVDGERVVESGSPGGSALL--NLDGPLYLGGLpedlkspGLPVSPGFVGCIRDLKV 150
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
90-235 |
7.59e-04 |
|
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: 41.60 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407228400 90 DFAIGVAVKPSSAQGGVLFAVTDAFQKVIYLGLRlsrvEDGRQRVILYytepGSHVSQEAAAFSVPVMTNRWNRFAVTVQ 169
Cdd:pfam13385 18 DFTVSAWVKPDSLPGWARAIISSSGGGGYSLGLD----GDGRLRFAVN----GGNGGWDTVTSGASVPLGQWTHVAVTYD 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407228400 170 GEEAVLFMDCEEhsqvlfqRSSRPLTFEP---SAGIFVGNAGATGLERFTGSIQQLIIYSDPRTPEELC 235
Cdd:pfam13385 90 GGTLRLYVNGVL-------VGSSTLTGGPppgTGGPLYIGRSPGGDDYFNGLIDEVRIYDRALSAAEIA 151
|
|
| Collagen |
pfam01391 |
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ... |
800-830 |
3.90e-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: 3.90e-03
10 20 30
....*....|....*....|....*....|.
gi 407228400 800 PGPRGPKGDTGVPGFPGLKGEQGEKGEPGAI 830
Cdd:pfam01391 21 PGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
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