|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
196-395 |
4.19e-99 |
|
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 306.92 E-value: 4.19e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 196 RYVELYVVADSQEFQKLGT-REAVRQRVLEVVNHVDKLYRELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 274 LLGRHPHDNVQLITGVDFIGTTVGLAKVSALCSR-HSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDENIPGCYCPipr 352
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564331627 353 EGGGCIMTESIGSKFPKTFSRCSQVDLESFVTNHQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
196-393 |
9.19e-81 |
|
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 258.31 E-value: 9.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 196 RYVELYVVADSQEFQKLG-TREAVRQRVLEVVNHVDKLYRELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 274 LLGRHPHDNVQLITGVDFIGTTVGLAKVSALCSR-HSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDEniPGCYCPipr 352
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCG--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564331627 353 eGGGCIMTESIGSkFPKTFSRCSQVDLESFVTNHQTGCLTN 393
Cdd:cd04269 156 -RSTCIMAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
412-486 |
3.91e-35 |
|
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.
Pssm-ID: 214490 Cd Length: 75 Bit Score: 127.81 E-value: 3.91e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564331627 412 ERGEQCDCGTPQDCQNPCCNATTCQLAKGAECAHGACCHECKVKPAGELCRPMKDKCDLEEFCDGQKPTCPEDAF 486
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
51-152 |
8.09e-35 |
|
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
Pssm-ID: 460254 Cd Length: 128 Bit Score: 128.97 E-value: 8.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 51 YPESLSYALGTSEQVFTLHLRKNRDLLGSSYTETYSAANGSEVKEQLHEQDHCLYQGHVEGYEGSAASISTCAGLSGFFR 130
Cdd:pfam01562 23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
|
90 100
....*....|....*....|....*.
gi 564331627 131 VGSTVHLIEPL---DADEEGQ-HAVY 152
Cdd:pfam01562 103 TENEEYLIEPLekySREEGGHpHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
412-484 |
2.11e-33 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 122.73 E-value: 2.11e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564331627 412 ERGEQCDCGTPQDCQ-NPCCNATTCQLAKGAECAHGACCHECKVKPAGELCRPMKDKCDLEEFCDGQKPTCPED 484
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
488-607 |
4.31e-31 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 118.62 E-value: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 488 QNGTPCPG--GYCFDGSCPTLAQQCQALWGPGARAASDSCFAFSIPQG-----C---YGSMYP--SRINRCGVLFCEGGQ 555
Cdd:smart00608 1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIPcaPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 564331627 556 KP--LERSSCTFSSHHG--LCQALQTDSNTNT-YEFVLQGTKCEEGKVCMDGNCQDL 607
Cdd:smart00608 81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
489-526 |
3.25e-13 |
|
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 66.48 E-value: 3.25e-13
10 20 30 40
....*....|....*....|....*....|....*....|
gi 564331627 489 NGTPCPG--GYCFDGSCPTLAQQCQALWGPGARAASDSCF 526
Cdd:pfam08516 1 DGTPCNNgqAYCYNGRCRDRDQQCQELFGKGAKSAPDACY 40
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
736-867 |
4.50e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 736 VAPKPTSGLSNPLFYTGDSSLPA---KSRPPDPPEMVSTNQPPRPIVKPKRPPpappgAMSSPPLPVPVYAPKAPNQLRP 812
Cdd:PHA03247 2837 TAPPPPPGPPPPSLPLGGSVAPGgdvRRRPPSRSPAAKPAAPARPPVRRLARP-----AVSRSTESFALPPDQPERPPQP 2911
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564331627 813 DPPTKPLPKLK-PKQVKPTFAPPTP-----PVKP-----GTGGTVPGVTQGAGGSKVALKVPIQKR 867
Cdd:PHA03247 2912 QAPPPPQPQPQpPPPPQPQPPPPPPprpqpPLAPttdpaGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
757-849 |
5.41e-04 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 43.60 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 757 PAKSRPPDP-PEMVSTNQPPRPIVkpkrpppappgamssPPLPVPVYAPKAPNQLRPDPPTKPLPKLKPKQVKPTFAPPT 835
Cdd:NF033839 287 PGNKKPSAPkPGMQPSPQPEKKEV---------------KPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPK 351
|
90
....*....|....
gi 564331627 836 PPVKPGTGGTVPGV 849
Cdd:NF033839 352 PEVKPQPEKPKPEV 365
|
|
| FAP |
pfam07174 |
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ... |
755-855 |
8.68e-04 |
|
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.
Pssm-ID: 429334 Cd Length: 301 Bit Score: 42.22 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 755 SLPAKSR---PPDPPEMVSTNQPPRPivkpkrpppapPGAMSSPPLPVPVYAPKAPNQLRPDPPTKPLPKLKPKQVKPTf 831
Cdd:pfam07174 32 ALPAVAHadpEPAPPPPSTATAPPAP-----------PPPPPAPAAPAPPPPPAAPNAPNAPPPPADPNAPPPPPADPN- 99
|
90 100
....*....|....*....|....*
gi 564331627 832 APPTPPVKPgtGGTVPG-VTQGAGG 855
Cdd:pfam07174 100 APPPPAVDP--NAPEPGrIDNAVGG 122
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
757-840 |
7.71e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 39.75 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 757 PAKSRP---PDP----PEMVSTNQPPRPIVkpkrpppappgamsSPPLPVPVYAPKaPNQLRPDPPTKPLPKLKPKQVKP 829
Cdd:NF033839 402 PEKPKPevkPQPekpkPEVKPQPEKPKPEV--------------KPQPEKPKPEVK-PQPEKPKPEVKPQPETPKPEVKP 466
|
90
....*....|.
gi 564331627 830 TFAPPTPPVKP 840
Cdd:NF033839 467 QPEKPKPEVKP 477
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Reprolysin |
pfam01421 |
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that ... |
196-395 |
4.19e-99 |
|
Reprolysin (M12B) family zinc metalloprotease; The members of this family are enzymes that cleave peptides. These proteases require zinc for catalysis. Members of this family are also known as adamalysins. Most members of this family are snake venom endopeptidases, but there are also some mammalian proteins such as Swiss:P78325, and fertilin. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.
Pssm-ID: 426256 [Multi-domain] Cd Length: 200 Bit Score: 306.92 E-value: 4.19e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 196 RYVELYVVADSQEFQKLGT-REAVRQRVLEVVNHVDKLYRELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:pfam01421 1 KYIELFIVVDKQLFQKMGSdTTVVRQRVFQVVNLVNSIYKELNIRVVLVGLEIWTdEDKIDVSGDANDTLRNFLKWRQEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 274 LLGRHPHDNVQLITGVDFIGTTVGLAKVSALCSR-HSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDENIPGCYCPipr 352
Cdd:pfam01421 81 LKKRKPHDVAQLLSGVEFGGTTVGAAYVGGMCSLeYSGGVNEDHSKNLESFAVTMAHELGHNLGMQHDDFNGGCKCP--- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564331627 353 EGGGCIMTESIGSKFPKTFSRCSQVDLESFVTNHQTGCLTNVP 395
Cdd:pfam01421 158 PGGGCIMNPSAGSSFPRKFSNCSQEDFEQFLTKQKGACLFNKP 200
|
|
| ZnMc_adamalysin_II_like |
cd04269 |
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom ... |
196-393 |
9.19e-81 |
|
Zinc-dependent metalloprotease; adamalysin_II_like subfamily. Adamalysin II is a snake venom zinc endopeptidase. This subfamily contains other snake venom metalloproteinases, as well as membrane-anchored metalloproteases belonging to the ADAM family. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239797 [Multi-domain] Cd Length: 194 Bit Score: 258.31 E-value: 9.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 196 RYVELYVVADSQEFQKLG-TREAVRQRVLEVVNHVDKLYRELSFRVVLVGLEIWN-KDKFYISRYANVTLENFLSWREQN 273
Cdd:cd04269 1 KYVELVVVVDNSLYKKYGsNLSKVRQRVIEIVNIVDSIYRPLNIRVVLVGLEIWTdKDKISVSGDAGETLNRFLDWKRSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 274 LLGRHPHDNVQLITGVDFIGTTVGLAKVSALCSR-HSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDEniPGCYCPipr 352
Cdd:cd04269 81 LLPRKPHDNAQLLTGRDFDGNTVGLAYVGGMCSPkYSGGVVQDHSRNLLLFAVTMAHELGHNLGMEHDD--GGCTCG--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 564331627 353 eGGGCIMTESIGSkFPKTFSRCSQVDLESFVTNHQTGCLTN 393
Cdd:cd04269 156 -RSTCIMAPSPSS-LTDAFSNCSYEDYQKFLSRGGGQCLLN 194
|
|
| ZnMc_ADAMTS_like |
cd04273 |
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) ... |
196-391 |
2.88e-38 |
|
Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that combine ADAM-like metalloproteinases with thrombospondin type-1 repeats. ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) proteinases are inhibited by TIMPs (tissue inhibitors of metalloproteinases), and they play roles in coagulation, angiogenesis, development and progression of arthritis. They hydrolyze the von Willebrand factor precursor and various components of the extracellular matrix.
Pssm-ID: 239801 Cd Length: 207 Bit Score: 141.61 E-value: 2.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 196 RYVELYVVADSQEFQKLGtREAVRQRVLEVVNHVDKLYRELS----FRVVLVGLEIWNKDKF--YISRYANVTLENFLSW 269
Cdd:cd04273 1 RYVETLVVADSKMVEFHH-GEDLEHYILTLMNIVASLYKDPSlgnsINIVVVRLIVLEDEESglLISGNAQKSLKSFCRW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 270 --REQNLLGRHP--HDNVQLITGVDF-----IGTTVGLAKVSALCSRH-SGAVNQDHtrsAIGVASTMAHELGHNLGMNH 339
Cdd:cd04273 80 qkKLNPPNDSDPehHDHAILLTRQDIcrsngNCDTLGLAPVGGMCSPSrSCSINEDT---GLSSAFTIAHELGHVLGMPH 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564331627 340 DENIPGCycpIPREGGGCIMTESIGSKF-PKTFSRCSQVDLESFVTNHQTGCL 391
Cdd:cd04273 157 DGDGNSC---GPEGKDGHIMSPTLGANTgPFTWSKCSRRYLTSFLDTGDGNCL 206
|
|
| DISIN |
smart00050 |
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to ... |
412-486 |
3.91e-35 |
|
Homologues of snake disintegrins; Snake disintegrins inhibit the binding of ligands to integrin receptors. They contain a 'RGD' sequence, identical to the recognition site of many adhesion proteins. Molecules containing both disintegrin and metalloprotease domains are known as ADAMs.
Pssm-ID: 214490 Cd Length: 75 Bit Score: 127.81 E-value: 3.91e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564331627 412 ERGEQCDCGTPQDCQNPCCNATTCQLAKGAECAHGACCHECKVKPAGELCRPMKDKCDLEEFCDGQKPTCPEDAF 486
Cdd:smart00050 1 EEGEECDCGSPKECTDPCCDPATCKLKPGAQCASGPCCDNCKFKPAGTLCRPSVDECDLPEYCNGTSADCPPDPY 75
|
|
| Pep_M12B_propep |
pfam01562 |
Reprolysin family propeptide; This region is the propeptide for members of peptidase family ... |
51-152 |
8.09e-35 |
|
Reprolysin family propeptide; This region is the propeptide for members of peptidase family M12B. The propeptide contains a sequence motif similar to the "cysteine switch" of the matrixins. This motif is found at the C terminus of the alignment but is not well aligned.
Pssm-ID: 460254 Cd Length: 128 Bit Score: 128.97 E-value: 8.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 51 YPESLSYALGTSEQVFTLHLRKNRDLLGSSYTETYSAANGSEVKEQLHEQDHCLYQGHVEGYEGSAASISTCAGLSGFFR 130
Cdd:pfam01562 23 YLDTLSYRLAAFGKKFHLHLTPNRLLLAPGFTVTYYLDGGTGVESPPVQTDHCYYQGHVEGHPDSSVALSTCSGLRGFIR 102
|
90 100
....*....|....*....|....*.
gi 564331627 131 VGSTVHLIEPL---DADEEGQ-HAVY 152
Cdd:pfam01562 103 TENEEYLIEPLekySREEGGHpHVVY 128
|
|
| Disintegrin |
pfam00200 |
Disintegrin; |
412-484 |
2.11e-33 |
|
Disintegrin;
Pssm-ID: 459709 Cd Length: 74 Bit Score: 122.73 E-value: 2.11e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564331627 412 ERGEQCDCGTPQDCQ-NPCCNATTCQLAKGAECAHGACCHECKVKPAGELCRPMKDKCDLEEFCDGQKPTCPED 484
Cdd:pfam00200 1 EEGEECDCGSLEECTnDPCCDAKTCKLKPGAQCSSGPCCTNCQFKPAGTVCRPSKDECDLPEYCNGTSAECPPD 74
|
|
| ZnMc_ADAM_like |
cd04267 |
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ... |
196-376 |
1.28e-32 |
|
Zinc-dependent metalloprotease, ADAM_like or reprolysin_like subgroup. The adamalysin_like or ADAM family of metalloproteases contains proteolytic domains from snake venoms, proteases from the mammalian reproductive tract, and the tumor necrosis factor alpha convertase, TACE. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions.
Pssm-ID: 239795 Cd Length: 192 Bit Score: 124.84 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 196 RYVELYVVADSQEFQKL-GTREAVRQRVLEVVNHVDKLYRELSF----RVVLVGLEIWNKDKFY--ISRYANVTLENFLS 268
Cdd:cd04267 1 REIELVVVADHRMVSYFnSDENILQAYITELINIANSIYRSTNLrlgiRISLEGLQILKGEQFAppIDSDASNTLNSFSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 269 WREQnllGRHPHDNVQLITGVDFI-GTTVGLAKVSALC-SRHSGAVNQDHTrSAIGVASTMAHELGHNLGMNHDENipGC 346
Cdd:cd04267 81 WRAE---GPIRHDNAVLLTAQDFIeGDILGLAYVGSMCnPYSSVGVVEDTG-FTLLTALTMAHELGHNLGAEHDGG--DE 154
|
170 180 190
....*....|....*....|....*....|
gi 564331627 347 YCPIPREGGGCIMTESIGSKFPKTFSRCSQ 376
Cdd:cd04267 155 LAFECDGGGNYIMAPVDSGLNSYRFSQCSI 184
|
|
| ACR |
smart00608 |
ADAM Cysteine-Rich Domain; |
488-607 |
4.31e-31 |
|
ADAM Cysteine-Rich Domain;
Pssm-ID: 214743 Cd Length: 137 Bit Score: 118.62 E-value: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 488 QNGTPCPG--GYCFDGSCPTLAQQCQALWGPGARAASDSCFAFSIPQG-----C---YGSMYP--SRINRCGVLFCEGGQ 555
Cdd:smart00608 1 QDGTPCDNgqGYCYNGRCPTRDNQCQALFGPGAKVAPDSCYEELNTKGdrfgnCgreNGTYIPcaPEDVKCGKLQCTNVS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 564331627 556 KP--LERSSCTFSSHHG--LCQALQTDSNTNT-YEFVLQGTKCEEGKVCMDGNCQDL 607
Cdd:smart00608 81 ELplLGEHATVIYSNIGglVCWSLDYHLGTDPdIGMVKDGTKCGPGKVCINGQCVDV 137
|
|
| ZnMc_salivary_gland_MPs |
cd04272 |
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary ... |
197-392 |
5.82e-19 |
|
Zinc-dependent metalloprotease, salivary_gland_MPs. Metalloproteases secreted by the salivary glands of arthropods.
Pssm-ID: 239800 Cd Length: 220 Bit Score: 86.64 E-value: 5.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 197 YVELYVVADSQEFQKLGTREAVRQRVLEVVNHVDKLYRELS---FRVVLVGLEIwNKDKFYISRYAN---------VTLE 264
Cdd:cd04272 2 YPELFVVVDYDHQSEFFSNEQLIRYLAVMVNAANLRYRDLKsprIRLLLVGITI-SKDPDFEPYIHPinygyidaaETLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 265 NFLSW-REQNLLGRHphDNVQLITGVDFIGT--------TVGLAKVSALCSRHSGAVNQDhTRSAIGVASTMAHELGHNL 335
Cdd:cd04272 81 NFNEYvKKKRDYFNP--DVVFLVTGLDMSTYsggslqtgTGGYAYVGGACTENRVAMGED-TPGSYYGVYTMTHELAHLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564331627 336 GMNHDENIPGCYCPIPREGGGC------IMTESIGSKFPKTFSRCSQVDLESFVTNHQTGCLT 392
Cdd:cd04272 158 GAPHDGSPPPSWVKGHPGSLDCpwddgyIMSYVVNGERQYRFSQCSQRQIRNVFRRLGASCLH 220
|
|
| Reprolysin_5 |
pfam13688 |
Metallo-peptidase family M12; |
196-365 |
5.87e-17 |
|
Metallo-peptidase family M12;
Pssm-ID: 372673 Cd Length: 191 Bit Score: 79.77 E-value: 5.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 196 RYVELYVVADsQEFQKLGTREAVRQRVLEVVNHVDKL-YRELSFRVVLVGLEIWNKDKFYISRYANV-----TLENFLSW 269
Cdd:pfam13688 3 RTVALLVAAD-CSYVAAFGGDAAQANIINMVNTASNVyERDFNISLGLVNLTISDSTCPYTPPACSTgdssdRLSEFQDF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 270 REQNllGRHPHDNVQLITGVDFigTTVGLAKVSALCSRHS-GAVNQDHTRSAIGVAS-----TMAHELGHNLGMNHD--- 340
Cdd:pfam13688 82 SAWR--GTQNDDLAYLFLMTNC--SGGGLAWLGQLCNSGSaGSVSTRVSGNNVVVSTatewqVFAHEIGHNFGAVHDcds 157
|
170 180 190
....*....|....*....|....*....|.
gi 564331627 341 -ENIPGC-----YCPIpreGGGCIMTESIGS 365
Cdd:pfam13688 158 sTSSQCCppsnsTCPA---GGRYIMNPSSSP 185
|
|
| Reprolysin_3 |
pfam13582 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
221-340 |
8.11e-15 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 463926 [Multi-domain] Cd Length: 122 Bit Score: 71.63 E-value: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 221 RVLEVVNHVDKLY-RELSFRVVLVGLEIWNKDKF-YISRYANVTLENFLswreQNLLGRHPHDN---VQLITGVDFIGTT 295
Cdd:pfam13582 2 RIVSLVNRANTIYeRDLGIRLQLAAIIITTSADTpYTSSDALEILDELQ----EVNDTRIGQYGydlGHLFTGRDGGGGG 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 564331627 296 vGLAKVSALC-SRHSGAVNQDHTRSAIGVASTMAHELGHNLGMNHD 340
Cdd:pfam13582 78 -GIAYVGGVCnSGSKFGVNSGSGPVGDTGADTFAHEIGHNFGLNHT 122
|
|
| ADAM_CR |
pfam08516 |
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell ... |
489-526 |
3.25e-13 |
|
ADAM cysteine-rich; ADAMs are membrane-anchored proteases that proteolytically modify cell surface and extracellular matrix (ECM) in order to alter cell behaviour. It has been shown that the cysteine-rich domain of ADAM13 regulates the protein's metalloprotease activity.
Pssm-ID: 462504 Cd Length: 105 Bit Score: 66.48 E-value: 3.25e-13
10 20 30 40
....*....|....*....|....*....|....*....|
gi 564331627 489 NGTPCPG--GYCFDGSCPTLAQQCQALWGPGARAASDSCF 526
Cdd:pfam08516 1 DGTPCNNgqAYCYNGRCRDRDQQCQELFGKGAKSAPDACY 40
|
|
| ZnMc |
cd00203 |
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major ... |
196-382 |
2.18e-12 |
|
Zinc-dependent metalloprotease. This super-family of metalloproteases contains two major branches, the astacin-like proteases and the adamalysin/reprolysin-like proteases. Both branches have wide phylogenetic distribution, and contain sub-families, which are involved in vertebrate development and disease.
Pssm-ID: 238124 [Multi-domain] Cd Length: 167 Bit Score: 66.01 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 196 RYVELYVVADSQEFQKLGTREAVRQRVLevvnhvdklyrelsfrvvlVGLEIWNKdkfyisrYANVTLenFLSwreqnLL 275
Cdd:cd00203 1 KVIPYVVVADDRDVEEENLSAQIQSLIL-------------------IAMQIWRD-------YLNIRF--VLV-----GV 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 276 GRHPHDNVQLITGVDFIGTTVGLAKVSALC-SRHSGAVNQDHTRSAIGVASTMAHELGHNLGMNHD------ENIPGCYC 348
Cdd:cd00203 48 EIDKADIAILVTRQDFDGGTGGWAYLGRVCdSLRGVGVLQDNQSGTKEGAQTIAHELGHALGFYHDhdrkdrDDYPTIDD 127
|
170 180 190
....*....|....*....|....*....|....*....
gi 564331627 349 PIPRE--GGGCIMTESIGSKFP---KTFSRCSQVDLESF 382
Cdd:cd00203 128 TLNAEddDYYSVMSYTKGSFSDgqrKDFSQCDIDQINKL 166
|
|
| ZnMc_TACE_like |
cd04270 |
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha ... |
200-375 |
1.16e-11 |
|
Zinc-dependent metalloprotease; TACE_like subfamily. TACE, the tumor-necrosis factor-alpha converting enzyme, releases soluble TNF-alpha from transmembrane pro-TNF-alpha.
Pssm-ID: 239798 [Multi-domain] Cd Length: 244 Bit Score: 65.86 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 200 LYVVADSQEFQKLGT--REAVRQRVLEVVNHVDKLYRELSFRVVL---VGLEIW----NKD--------KFYISRYANVT 262
Cdd:cd04270 5 LLLVADHRFYKYMGRgeEETTINYLISHIDRVDDIYRNTDWDGGGfkgIGFQIKririHTTpdevdpgnKFYNKSFPNWG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 263 LENFLswrEQNLLGRHPHDN--VQLITGVDFIGTTVGLAKVSALCSRHSGAVNQDHTRSAIGVAS--------------- 325
Cdd:cd04270 85 VEKFL---VKLLLEQFSDDVclAHLFTYRDFDMGTLGLAYVGSPRDNSAGGICEKAYYYSNGKKKylntgltttvnygkr 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564331627 326 --------TMAHELGHNLGMNHDENIPGCyCPIPREGGGCIMTESIGS---KFPKTFSRCS 375
Cdd:cd04270 162 vptkesdlVTAHELGHNFGSPHDPDIAEC-APGESQGGNYIMYARATSgdkENNKKFSPCS 221
|
|
| Reprolysin_2 |
pfam13574 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
217-349 |
1.51e-08 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 372637 Cd Length: 193 Bit Score: 55.33 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 217 AVRQRVLEVVNHVDKLYR--ELSFRVVLVG---LEI-------WNKDKFyiSRYANVTLENFLSwreqNLLGRHPHDNVQ 284
Cdd:pfam13574 2 NVTENLVNVVNRVNQIYEpdDININGGLVNpgeIPAttsasdsGNNYCN--SPTTIVRRLNFLS----QWRGEQDYCLAH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 285 LITGVDFIGTTVGLAKVSALCSRHSGAVnqdhtRSAIGVAST---------------MAHELGHNLGMNHDENIPGCYCP 349
Cdd:pfam13574 76 LVTMGTFSGGELGLAYVGQICQKGASSP-----KTNTGLSTTtnygsfnyptqewdvVAHEVGHNFGATHDCDGSQYASS 150
|
|
| ZnMc_ADAM_fungal |
cd04271 |
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A ... |
202-392 |
3.07e-08 |
|
Zinc-dependent metalloprotease, ADAM_fungal subgroup. The adamalysin_like or ADAM (A Disintegrin And Metalloprotease) family of metalloproteases are integral membrane proteases acting on a variety of extracellular targets. They are involved in shedding soluble peptides or proteins from the cell surface. This subfamily contains fungal ADAMs, whose precise function has yet to be determined.
Pssm-ID: 239799 [Multi-domain] Cd Length: 228 Bit Score: 55.12 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 202 VVADSQEFQKLGTREAVRQRVLEVVNHVDKLYRElSFRVVL--VGLEI--------------WN---KDKFYISRyanvT 262
Cdd:cd04271 7 VAADCSYTKSFGSVEEARRNILNNVNSASQLYES-SFNISLglRNLTIsdascpstavdsapWNlpcNSRIDIDD----R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 263 LENFLSWREQnllgRHPHDNV--QLITGVDfIGTTVGLAKVSALC-SRHSGAVNQDHTrSAIGVAST------MAHELGH 333
Cdd:cd04271 82 LSIFSQWRGQ----QPDDGNAfwTLMTACP-SGSEVGVAWLGQLCrTGASDQGNETVA-GTNVVVRTsnewqvFAHEIGH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564331627 334 NLGMNHDENIPGCY---------CPIPRE----GGGCIMTESIGSKFpKTFSRCSQVDLESFV--TNHQTGCLT 392
Cdd:cd04271 156 TFGAVHDCTSGTCSdgsvgsqqcCPLSTStcdaNGQYIMNPSSSSGI-TEFSPCTIGNICSLLgrNPVRTSCLS 228
|
|
| Reprolysin_4 |
pfam13583 |
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the ... |
196-346 |
4.70e-07 |
|
Metallo-peptidase family M12B Reprolysin-like; This zinc-binding metallo-peptidase has the characteriztic binding motif HExxGHxxGxxH of Reprolysin-like peptidases of family M12B.
Pssm-ID: 404471 Cd Length: 203 Bit Score: 51.47 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 196 RYVELYVVADSQEFQKLGTREAVRQRVLEVVNHVDKLY-RELSFRVVLVG----------LEIWNKDKFyISRYANVTLE 264
Cdd:pfam13583 3 RVYRVAVATDCTYSASFGSVDELRANINATVTTANEVYgRDFNVSLALISdrdviytdssTDSFNADCS-GGDLGNWRLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 265 NFLSWReqnllGRHPHDNVQLITGVDFIGTTVGLAKVSALCSRHSGAVNQDHTRSAIGVASTMAHELGHNLGMNHDENIP 344
Cdd:pfam13583 82 TLTSWR-----DSLNYDLAYLTLMTGPSGQNVGVAWVGALCSSARQNAKASGVARSRDEWDIFAHEIGHTFGAVHDCSSQ 156
|
..
gi 564331627 345 GC 346
Cdd:pfam13583 157 GE 158
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
736-867 |
4.50e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 50.71 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 736 VAPKPTSGLSNPLFYTGDSSLPA---KSRPPDPPEMVSTNQPPRPIVKPKRPPpappgAMSSPPLPVPVYAPKAPNQLRP 812
Cdd:PHA03247 2837 TAPPPPPGPPPPSLPLGGSVAPGgdvRRRPPSRSPAAKPAAPARPPVRRLARP-----AVSRSTESFALPPDQPERPPQP 2911
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564331627 813 DPPTKPLPKLK-PKQVKPTFAPPTP-----PVKP-----GTGGTVPGVTQGAGGSKVALKVPIQKR 867
Cdd:PHA03247 2912 QAPPPPQPQPQpPPPPQPQPPPPPPprpqpPLAPttdpaGAGEPSGAVPQPWLGALVPGRVAVPRF 2977
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
736-848 |
6.67e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 736 VAPKPTSGLSNPLFYTGDSSLPAKSRP--PDPPEMVSTNQPPRPIVKPKRPPPAPPGAMSSP------PLPVPVYAPKAP 807
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPPTTAGPpaPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPwdpadpPAAVLAPAAALP 2819
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 564331627 808 NQLRPDPPTKPLPKLKPKQVKPTFAPPTPPVKPGtGGTVPG 848
Cdd:PHA03247 2820 PAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG-GSVAPG 2859
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
638-848 |
8.24e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.47 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 638 APPYCAQLLADVPVVTeSAAVHSTTASGNWRGLNSGTVGLGLATTTSSNPLLESQKSWSSESLPVSVVVVLVILVAAVVI 717
Cdd:PHA03247 2774 APAAGPPRRLTRPAVA-SLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL 2852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 718 GAGIV----IYRKAPKqiqrRSVAPKPT-------SGLSNPLFYTGDSSLPaksRPPDPPEMVSTNQPPRPivkpkrppp 786
Cdd:PHA03247 2853 GGSVApggdVRRRPPS----RSPAAKPAaparppvRRLARPAVSRSTESFA---LPPDQPERPPQPQAPPP--------- 2916
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564331627 787 appgAMSSPPLPVPVY-APKAPNQLRPDPPTKPLPKLKPkQVKPTFAPPTPPVkpgtGGTVPG 848
Cdd:PHA03247 2917 ----PQPQPQPPPPPQpQPPPPPPPRPQPPLAPTTDPAG-AGEPSGAVPQPWL----GALVPG 2970
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
757-840 |
1.27e-04 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 44.67 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 757 PAKSRPPDPPEMVSTNQPPRPIvkpkrpppappgamSSPPLPVPVYAPKapnqlrPDPPTKPLPKLKPKQVKPTFAPPTP 836
Cdd:PRK10819 60 PPQAVQPPPEPVVEPEPEPEPI--------------PEPPKEAPVVIPK------PEPKPKPKPKPKPKPVKKVEEQPKR 119
|
....
gi 564331627 837 PVKP 840
Cdd:PRK10819 120 EVKP 123
|
|
| PTZ00449 |
PTZ00449 |
104 kDa microneme/rhoptry antigen; Provisional |
726-840 |
2.83e-04 |
|
104 kDa microneme/rhoptry antigen; Provisional
Pssm-ID: 185628 [Multi-domain] Cd Length: 943 Bit Score: 44.68 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 726 KAPKQIQRRSVAPKPTSGL----SNPLFYTGDSSLPAKSRPP-DPPEMVSTNQPPRPIVKPKRPPPAPPGAMSSPPLPVP 800
Cdd:PTZ00449 547 GKPGETKEGEVGKKPGPAKehkpSKIPTLSKKPEFPKDPKHPkDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKR 626
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 564331627 801 VYAPKAPNqlRPDPPTKPLPKLKP---KQVKPTFAP--PTPPVKP 840
Cdd:PTZ00449 627 PESPKSPK--RPPPPQRPSSPERPegpKIIKSPKPPksPKPPFDP 669
|
|
| PRK11633 |
PRK11633 |
cell division protein DedD; Provisional |
738-840 |
4.19e-04 |
|
cell division protein DedD; Provisional
Pssm-ID: 236940 [Multi-domain] Cd Length: 226 Bit Score: 42.68 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 738 PKPtsglsnplfytGDS----SLPA--KSRPPDPPE----MVSTNQPPRPIVKPkrpppappgAMSSPPLPVPVYAPKAP 807
Cdd:PRK11633 45 PKP-----------GDRdepdMMPAatQALPTQPPEgaaeAVRAGDAAAPSLDP---------ATVAPPNTPVEPEPAPV 104
|
90 100 110
....*....|....*....|....*....|...
gi 564331627 808 NQLRPDPPTKPLPKLKPKQVKPTFAPPTPPVKP 840
Cdd:PRK11633 105 EPPKPKPVEKPKPKPKPQQKVEAPPAPKPEPKP 137
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
733-860 |
5.07e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 733 RRSVAPKPTSglsnPLFYTGDSSLPAKSRPPDP-PEMVSTNQPPRPIVKPKRPPPAPPGAMSSPPLPVPVYAP------- 804
Cdd:PHA03247 2588 RPDAPPQSAR----PRAPVDDRGDPRGPAPPSPlPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPapgrvsr 2663
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564331627 805 --KAPNQLRPDPPTKPLPKLKPKQVKPTFAP-------------PTPPVKPGTGGT-VPGVTQGAGGSKVAL 860
Cdd:PHA03247 2664 prRARRLGRAAQASSPPQRPRRRAARPTVGSltsladpppppptPEPAPHALVSATpLPPGPAAARQASPAL 2735
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
757-849 |
5.41e-04 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 43.60 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 757 PAKSRPPDP-PEMVSTNQPPRPIVkpkrpppappgamssPPLPVPVYAPKAPNQLRPDPPTKPLPKLKPKQVKPTFAPPT 835
Cdd:NF033839 287 PGNKKPSAPkPGMQPSPQPEKKEV---------------KPEPETPKPEVKPQLEKPKPEVKPQPEKPKPEVKPQLETPK 351
|
90
....*....|....
gi 564331627 836 PPVKPGTGGTVPGV 849
Cdd:NF033839 352 PEVKPQPEKPKPEV 365
|
|
| FAP |
pfam07174 |
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment ... |
755-855 |
8.68e-04 |
|
Fibronectin-attachment protein (FAP); This family contains bacterial fibronectin-attachment proteins (FAP). Family members are rich in alanine and proline, are approximately 300 long, and seem to be restricted to mycobacteria. These proteins contain a fibronectin-binding motif that allows mycobacteria to bind to fibronectin in the extracellular matrix.
Pssm-ID: 429334 Cd Length: 301 Bit Score: 42.22 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 755 SLPAKSR---PPDPPEMVSTNQPPRPivkpkrpppapPGAMSSPPLPVPVYAPKAPNQLRPDPPTKPLPKLKPKQVKPTf 831
Cdd:pfam07174 32 ALPAVAHadpEPAPPPPSTATAPPAP-----------PPPPPAPAAPAPPPPPAAPNAPNAPPPPADPNAPPPPPADPN- 99
|
90 100
....*....|....*....|....*
gi 564331627 832 APPTPPVKPgtGGTVPG-VTQGAGG 855
Cdd:pfam07174 100 APPPPAVDP--NAPEPGrIDNAVGG 122
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
725-856 |
1.81e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 42.23 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 725 RKAPKQiQRRSVAPKPTSGLSNPLFYTGDSSLPAKSRPPDPPEmvSTNQPPRPIVKPKRPPPAPPGA-MSSPPLPVPVYA 803
Cdd:PHA03247 2665 RRARRL-GRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPP--TPEPAPHALVSATPLPPGPAAArQASPALPAAPAP 2741
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 564331627 804 PKAPNQlrPDPPTKPLPKLKPkQVKPTFAPPTPPVKPgTGGTVPGVTQGAGGS 856
Cdd:PHA03247 2742 PAVPAG--PATPGGPARPARP-PTTAGPPAPAPPAAP-AAGPPRRLTRPAVAS 2790
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
751-848 |
3.85e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.08 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 751 TGDSSLPAKSRPPDPPEMVSTNQPPRPIVKPKRPPPAPPGAMSSPPLPVPVYAPKAPNQLRPDPPTkPLPKLKPKQVKPT 830
Cdd:PHA03247 2563 APDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPP-PSPSPAANEPDPH 2641
|
90
....*....|....*...
gi 564331627 831 FAPPTPPVKPGTGGTVPG 848
Cdd:PHA03247 2642 PPPTVPPPERPRDDPAPG 2659
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
732-842 |
7.31e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 40.31 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 732 QRRSVAPKPTSGLSNPLFYTGDSS-------LPAKSRPPDPPEM----VSTNQPPRPIVKPKRPPPAPPGAMSSPP---L 797
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAarqaspaLPAAPAPPAVPAGpatpGGPARPARPPTTAGPPAPAPPAAPAAGPprrL 2783
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564331627 798 PVPVYAPKAPNQ----LRPDPPTKPLPKLKPKQVKPTFAPPTPPVKPGT 842
Cdd:PHA03247 2784 TRPAVASLSESReslpSPWDPADPPAAVLAPAAALPPAASPAGPLPPPT 2832
|
|
| PspC_subgroup_2 |
NF033839 |
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ... |
757-840 |
7.71e-03 |
|
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.
Pssm-ID: 468202 [Multi-domain] Cd Length: 557 Bit Score: 39.75 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 757 PAKSRP---PDP----PEMVSTNQPPRPIVkpkrpppappgamsSPPLPVPVYAPKaPNQLRPDPPTKPLPKLKPKQVKP 829
Cdd:NF033839 402 PEKPKPevkPQPekpkPEVKPQPEKPKPEV--------------KPQPEKPKPEVK-PQPEKPKPEVKPQPETPKPEVKP 466
|
90
....*....|.
gi 564331627 830 TFAPPTPPVKP 840
Cdd:NF033839 467 QPEKPKPEVKP 477
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
753-867 |
8.44e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 39.92 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564331627 753 DSSLPAKSRPPDPP-----EMVSTNQP-PRPIVKPKRPPPAPPGAmssPPLPVPVYAPKAPnqlrPDPPTKPLPklkpkq 826
Cdd:PHA03247 2547 DAGDPPPPLPPAAPpaapdRSVPPPRPaPRPSEPAVTSRARRPDA---PPQSARPRAPVDD----RGDPRGPAP------ 2613
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 564331627 827 vkPTFAPP-TPPVKPGTGGTVPGVTQGAGGSKVALKVPIQKR 867
Cdd:PHA03247 2614 --PSPLPPdTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPR 2653
|
|
| |
