|
Name |
Accession |
Description |
Interval |
E-value |
| COG4867 |
COG4867 |
Uncharacterized conserved protein, contains von Willebrand factor type A (vWFA) domain ... |
322-678 |
3.68e-137 |
|
Uncharacterized conserved protein, contains von Willebrand factor type A (vWFA) domain [Function unknown];
Pssm-ID: 443895 [Multi-domain] Cd Length: 371 Bit Score: 406.87 E-value: 3.68e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 322 DSLTMEQAMEMMRGLQELDQLEQSLQEAMRTGNMDDIDPDKLAELLGEEARKIYDELDRLRKLLQESGYV--TGDDKMDL 399
Cdd:COG4867 11 EPLGLGDATGAMQDLAELDALLEQLSQLLPGARLDDIDLDALDRQLGDTAAVDARTLRDLERELREQGYLrrEADGGLEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 400 TARGIRRIGQKALKEVFTHLKKDRIGNHMMDARGANGDLLGETKPYEFGDPFQVDLQATVRNAVLRGGPQVPVKLSPEDF 479
Cdd:COG4867 91 TPKAERRLGKSALRDIFGKLKKGRRGNHDTRRAGAGGELTGETRPWEFGDTLPLDVTRTLRNAVLRHGPGGPVRLDEEDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 480 EVFRNEHMTRSATVLLLDQSRSMGLFNNWQAAKKVTLALMALMRSQYPRDSLHIVGFSDYAREIKEEDLAKCTWnAWVSG 559
Cdd:COG4867 171 EVEETEYRTQAATVLMVDTSHSMILYGRWTPAKKVALALAHLIRTRFPGDTLDIIVFGNDAWEVEIKELPYLQW-VGPYG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 560 TNLHHALMLSRKLLSKEKGGNRQILVVTDGEPTAHLE--GDRSFFAYPPSHRTELETLKEVRRCTQEDIVINTFMLENNY 637
Cdd:COG4867 250 TNTHHGLLLARRLLRRHPNANKQILMITDGEPTAHLEpdGEYYKFSYPPDPETLAKTLAEVDRCRRLGIPITTFMLARDP 329
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1301426215 638 QLVNFVERMTRINSGRAFYSSAANLGEYLLVDYVTNRRKRV 678
Cdd:COG4867 330 YLARFVDEFTRRNGGRAYFPDLDGLGAYVVEDYLRNRRKRV 370
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
493-651 |
2.34e-13 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 68.36 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 493 VLLLDQSRSMGLfNNWQAAKKVTLALMALMRSQYPRDSLHIVGFSDYAREIKEEDLAKCTWN----------AWVSGTNL 562
Cdd:cd00198 4 VFLLDVSGSMGG-EKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADlleaidalkkGLGGGTNI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 563 HHALMLSRKLLSKEKGGNRQ--ILVVTDGEPTAHLEgdrsffayppshrtelETLKEVRRCTQEDIVINTFML---ENNY 637
Cdd:cd00198 83 GAALRLALELLKSAKRPNARrvIILLTDGEPNDGPE----------------LLAEAARELRKLGITVYTIGIgddANED 146
|
170
....*....|....
gi 1301426215 638 QLVNFVERMTRINS 651
Cdd:cd00198 147 ELKEIADKTTGGAV 160
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
493-658 |
8.82e-13 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 67.09 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 493 VLLLDQSRSMGLfNNWQAAKKVTLALMALMRSQYPRDSLHIVGFSDYAREIK-----------EEDLAKCTWNaWVSGTN 561
Cdd:smart00327 3 VFLLDGSGSMGG-NRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFplndsrskdalLEALASLSYK-LGGGTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 562 LHHAL-MLSRKLLSKEKGGNRQ----ILVVTDGEPTAHLEgdrsffayppshrtelETLKEVRRCTQEDIVINTFMLENN 636
Cdd:smart00327 81 LGAALqYALENLFSKSAGSRRGapkvVILITDGESNDGPK----------------DLLKAAKELKRSGVKVFVVGVGND 144
|
170 180
....*....|....*....|..
gi 1301426215 637 YqLVNFVERMTRINSGRAFYSS 658
Cdd:smart00327 145 V-DEEELKKLASAPGGVYVFLP 165
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
21-387 |
1.85e-06 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 51.14 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 21 DADQLMDLLSED--ILNHGDVMQALRDMlrqglqdRDGQQmpglrELMEQLKNQRRQqlqqhnmdsvvddlkERLEDIVQ 98
Cdd:pfam13779 464 ALDEVADLLWELalRIEDGDLSDAERRL-------RAAQE-----RLSEALERGASD---------------EEIAKLMQ 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 99 TERDGIKRRLDE-AREQVDAQADSQDGEDRAQMEGLLDLLQKRADnnrgklddlpespagQIKELLEYDFIDpEAQQkfq 177
Cdd:pfam13779 517 ELREALDDYMQAlAEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLD---------------RIEELARSGRRA-EAQQ--- 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 178 dLLDALkSQMAQNMGQQMMDQVKGMSEEDMaatREMMRQLNQMIKDKlagQEPDFDGF--MQQFGKMFGDNPPQSFDELM 255
Cdd:pfam13779 578 -MLSQL-QQMLENLQAGQPQQQQQQGQSEM---QQAMDELGDLLREQ---QQLLDETFrqLQQQGGQQQGQPGQQGQQGQ 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 256 EQMQQQLAQAQSMLDSMSPEAR-----REMEDALAQALDpETQREMAQFA------SLMEQLMPMDD----LRRqypflG 320
Cdd:pfam13779 650 GQQPGQGGQQPGAQMPPQGGAEalgdlAERQQALRRRLE-ELQDELKELGgkepgqALGDAGRAMRDaeeaLGQ-----G 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 321 DDSLTMEQ---AMEMMR-GLQEL-DQLEQSLQEAM------RTGNMDDIDP-----DKLAELLGEEARKIYDELD--RLR 382
Cdd:pfam13779 724 DLAGAVDAqgrALEALRkGAQQLaEAMQQQQGQGQqpgqggQGGRQAGQDPlgrplGGGGDFGDDEAVKVPDEIDaqRAR 803
|
....*
gi 1301426215 383 KLLQE 387
Cdd:pfam13779 804 EILEE 808
|
|
| VWA_CoxE |
pfam05762 |
VWA domain containing CoxE-like protein; This family is annotated by SMART as containing a VWA ... |
454-597 |
6.29e-06 |
|
VWA domain containing CoxE-like protein; This family is annotated by SMART as containing a VWA (von Willebrand factor type A) domain. The exact function of this family is unknown. It is found as part of a CO oxidising (Cox) system operon is several bacteria.
Pssm-ID: 399053 [Multi-domain] Cd Length: 221 Bit Score: 47.77 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 454 DLQATVRNAVLRGGPQV-PVKLSPedfevfRNEHMTRsaTVLLLDQSRSMGLFNNWqaakkvTLALMALMRSQYPRdsLH 532
Cdd:pfam05762 28 DLRRTLRANLRHGGEPVeLVRRKP------RKRRPWR--LVLLLDVSGSMSDYSRV------FLALMHALLRQRPR--TR 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1301426215 533 IVGFS----DYAREIKEEDLA------KCTWNAWVSGTNLHHALMLSRKLLSKEKGGNRQILVVTDGEPTAHLEG 597
Cdd:pfam05762 92 VFAFStrltDLTRQLRERDPDealrrvSARVEDWGGGTRIGAALADFNELVTRPALRRAVVLLVSDGYEGGPREE 166
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
57-224 |
6.32e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 57 QQMPGLRELMEQLKNQRRQQLQQ-HNMDSVVDDLKERLEDIvQTERDGIKRRLDEAREQVDAQADSQDgEDRAQMEGLLD 135
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQlAALERRIAALARRIRAL-EQELAALEAELAELEKEIAELRAELE-AQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 136 LLQKRADNNRGKLDDLPESPAGQIKELLEYDFIDPEAQQKFQDLLDALKSQMAQNMGQQMMDQVKgmsEEDMAATREMMR 215
Cdd:COG4942 112 ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL---EALLAELEEERA 188
|
....*....
gi 1301426215 216 QLNQMIKDK 224
Cdd:COG4942 189 ALEALKAER 197
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG4867 |
COG4867 |
Uncharacterized conserved protein, contains von Willebrand factor type A (vWFA) domain ... |
322-678 |
3.68e-137 |
|
Uncharacterized conserved protein, contains von Willebrand factor type A (vWFA) domain [Function unknown];
Pssm-ID: 443895 [Multi-domain] Cd Length: 371 Bit Score: 406.87 E-value: 3.68e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 322 DSLTMEQAMEMMRGLQELDQLEQSLQEAMRTGNMDDIDPDKLAELLGEEARKIYDELDRLRKLLQESGYV--TGDDKMDL 399
Cdd:COG4867 11 EPLGLGDATGAMQDLAELDALLEQLSQLLPGARLDDIDLDALDRQLGDTAAVDARTLRDLERELREQGYLrrEADGGLEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 400 TARGIRRIGQKALKEVFTHLKKDRIGNHMMDARGANGDLLGETKPYEFGDPFQVDLQATVRNAVLRGGPQVPVKLSPEDF 479
Cdd:COG4867 91 TPKAERRLGKSALRDIFGKLKKGRRGNHDTRRAGAGGELTGETRPWEFGDTLPLDVTRTLRNAVLRHGPGGPVRLDEEDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 480 EVFRNEHMTRSATVLLLDQSRSMGLFNNWQAAKKVTLALMALMRSQYPRDSLHIVGFSDYAREIKEEDLAKCTWnAWVSG 559
Cdd:COG4867 171 EVEETEYRTQAATVLMVDTSHSMILYGRWTPAKKVALALAHLIRTRFPGDTLDIIVFGNDAWEVEIKELPYLQW-VGPYG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 560 TNLHHALMLSRKLLSKEKGGNRQILVVTDGEPTAHLE--GDRSFFAYPPSHRTELETLKEVRRCTQEDIVINTFMLENNY 637
Cdd:COG4867 250 TNTHHGLLLARRLLRRHPNANKQILMITDGEPTAHLEpdGEYYKFSYPPDPETLAKTLAEVDRCRRLGIPITTFMLARDP 329
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1301426215 638 QLVNFVERMTRINSGRAFYSSAANLGEYLLVDYVTNRRKRV 678
Cdd:COG4867 330 YLARFVDEFTRRNGGRAYFPDLDGLGAYVVEDYLRNRRKRV 370
|
|
| vWFA |
cd00198 |
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ... |
493-651 |
2.34e-13 |
|
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.
Pssm-ID: 238119 [Multi-domain] Cd Length: 161 Bit Score: 68.36 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 493 VLLLDQSRSMGLfNNWQAAKKVTLALMALMRSQYPRDSLHIVGFSDYAREIKEEDLAKCTWN----------AWVSGTNL 562
Cdd:cd00198 4 VFLLDVSGSMGG-EKLDKAKEALKALVSSLSASPPGDRVGLVTFGSNARVVLPLTTDTDKADlleaidalkkGLGGGTNI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 563 HHALMLSRKLLSKEKGGNRQ--ILVVTDGEPTAHLEgdrsffayppshrtelETLKEVRRCTQEDIVINTFML---ENNY 637
Cdd:cd00198 83 GAALRLALELLKSAKRPNARrvIILLTDGEPNDGPE----------------LLAEAARELRKLGITVYTIGIgddANED 146
|
170
....*....|....
gi 1301426215 638 QLVNFVERMTRINS 651
Cdd:cd00198 147 ELKEIADKTTGGAV 160
|
|
| VWA |
smart00327 |
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ... |
493-658 |
8.82e-13 |
|
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins mediate adhesion via metal ion-dependent adhesion sites (MIDAS). Intracellular VWA domains and homologues in prokaryotes have recently been identified. The proposed VWA domains in integrin beta subunits have recently been substantiated using sequence-based methods.
Pssm-ID: 214621 [Multi-domain] Cd Length: 175 Bit Score: 67.09 E-value: 8.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 493 VLLLDQSRSMGLfNNWQAAKKVTLALMALMRSQYPRDSLHIVGFSDYAREIK-----------EEDLAKCTWNaWVSGTN 561
Cdd:smart00327 3 VFLLDGSGSMGG-NRFELAKEFVLKLVEQLDIGPDGDRVGLVTFSDDARVLFplndsrskdalLEALASLSYK-LGGGTN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 562 LHHAL-MLSRKLLSKEKGGNRQ----ILVVTDGEPTAHLEgdrsffayppshrtelETLKEVRRCTQEDIVINTFMLENN 636
Cdd:smart00327 81 LGAALqYALENLFSKSAGSRRGapkvVILITDGESNDGPK----------------DLLKAAKELKRSGVKVFVVGVGND 144
|
170 180
....*....|....*....|..
gi 1301426215 637 YqLVNFVERMTRINSGRAFYSS 658
Cdd:smart00327 145 V-DEEELKKLASAPGGVYVFLP 165
|
|
| ChlD |
COG1240 |
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ... |
430-593 |
3.92e-11 |
|
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and metabolism];
Pssm-ID: 440853 [Multi-domain] Cd Length: 262 Bit Score: 64.19 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 430 DARGANGDLLGETKPYEFGDPFQVDLQATVRNAVLRGGPQVPVKLSPEDFEVFRNEHMTRSATVLLLDQSRSMGLFNNWQ 509
Cdd:COG1240 33 PLPLDLLLALPLAGLALLLGLAGLGLLALLLAALLLLLAVLLLLLALALAPLALARPQRGRDVVLVVDASGSMAAENRLE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 510 AAKKVTLALMALMRsqyPRDSLHIVGFSDYAREIKE--EDLAkcTWNAWVS------GTNLHHALMLSRKLLSKE-KGGN 580
Cdd:COG1240 113 AAKGALLDFLDDYR---PRDRVGLVAFGGEAEVLLPltRDRE--ALKRALDelppggGTPLGDALALALELLKRAdPARR 187
|
170
....*....|...
gi 1301426215 581 RQILVVTDGEPTA 593
Cdd:COG1240 188 KVIVLLTDGRDNA 200
|
|
| YfbK |
COG2304 |
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ... |
424-656 |
5.36e-09 |
|
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];
Pssm-ID: 441879 [Multi-domain] Cd Length: 289 Bit Score: 57.80 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 424 IGNHMMDARGANGDLLGETKPYEFGDPFQVDLQATVRNAVLRggpQVPVKLSPEDFEvfrNEHMTRSATVLLLDQSRSMG 503
Cdd:COG2304 32 LVGGEPPPAAAVRLEELVNFFPYDYPLPTGRLAQSPWNPQTR---LLLVGLQPPKAA---AEERPPLNLVFVIDVSGSMS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 504 LfNNWQAAKKVTLALMALMRsqyPRDSLHIVGFSDYAREIKE----EDLAKctWNAWVS------GTNLHHALMLSRKLL 573
Cdd:COG2304 106 G-DKLELAKEAAKLLVDQLR---PGDRVSIVTFAGDARVLLPptpaTDRAK--ILAAIDrlqaggGTALGAGLELAYELA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 574 SKE--KGGNRQILVVTDGEPTAhlegdrsffayppsHRTELETLKE-VRRCTQEDIVINTFMLENNYQlVNFVERMTRIN 650
Cdd:COG2304 180 RKHfiPGRVNRVILLTDGDANV--------------GITDPEELLKlAEEAREEGITLTTLGVGSDYN-EDLLERLADAG 244
|
....*.
gi 1301426215 651 SGRAFY 656
Cdd:COG2304 245 GGNYYY 250
|
|
| ViaA |
COG2425 |
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ... |
450-592 |
7.55e-09 |
|
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];
Pssm-ID: 441973 [Multi-domain] Cd Length: 263 Bit Score: 57.38 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 450 PFQVDLQATVRNAVLRGGPQVPVKLSPEDFEVFRNEHMTRSATVLLLDQSRSMGLFNnWQAAKKVTLALMALMRsqyPRD 529
Cdd:COG2425 79 ALLAALLDALLLAVLLLALLLLAALLLLAAPASAAVPLLEGPVVLCVDTSGSMAGSK-EAAAKAAALALLRALR---PNR 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1301426215 530 SLHIVGFSD--YAREIKEEDLAKCTWNAWVS------GTNLHHALMLSRKLLSKEKGGNRQILVVTDGEPT 592
Cdd:COG2425 155 RFGVILFDTevVEDLPLTADDGLEDAIEFLSglfaggGTDIAPALRAALELLEEPDYRNADIVLITDGEAG 225
|
|
| vWA_interalpha_trypsin_inhibitor |
cd01461 |
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ... |
493-654 |
7.49e-08 |
|
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- two heavy chains and one light chain (bikunin). Bikunin confers the protease-inhibitor function while the heavy chains are involved in rendering stability to the extracellular matrix by binding to hyaluronic acid. The heavy chains carry the VWA domain with a conserved MIDAS motif. Although the exact role of the VWA domains remains unknown, it has been speculated to be involved in mediating protein-protein interactions with the components of the extracellular matrix.
Pssm-ID: 238738 [Multi-domain] Cd Length: 171 Bit Score: 52.60 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 493 VLLLDQSRSMGlfnnWQAAKKVTLALMALMRSQYPRDSLHIVGFSDYAREIK-------EEDLAKCTwnAWVS------G 559
Cdd:cd01461 6 VFVIDTSGSMS----GTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSpssvsatAENVAAAI--EYVNrlqalgG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 560 TNLHHALMLSRKLLSKEKGGNRQILVVTDGEPTahlegdrsffayppshrTELETLKEVRRCTQEDIVINTFMLENNyql 639
Cdd:cd01461 80 TNMNDALEAALELLNSSPGSVPQIILLTDGEVT-----------------NESQILKNVREALSGRIRLFTFGIGSD--- 139
|
170
....*....|....*..
gi 1301426215 640 VN--FVERMTRINSGRA 654
Cdd:cd01461 140 VNtyLLERLAREGRGIA 156
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
21-387 |
1.85e-06 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 51.14 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 21 DADQLMDLLSED--ILNHGDVMQALRDMlrqglqdRDGQQmpglrELMEQLKNQRRQqlqqhnmdsvvddlkERLEDIVQ 98
Cdd:pfam13779 464 ALDEVADLLWELalRIEDGDLSDAERRL-------RAAQE-----RLSEALERGASD---------------EEIAKLMQ 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 99 TERDGIKRRLDE-AREQVDAQADSQDGEDRAQMEGLLDLLQKRADnnrgklddlpespagQIKELLEYDFIDpEAQQkfq 177
Cdd:pfam13779 517 ELREALDDYMQAlAEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLD---------------RIEELARSGRRA-EAQQ--- 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 178 dLLDALkSQMAQNMGQQMMDQVKGMSEEDMaatREMMRQLNQMIKDKlagQEPDFDGF--MQQFGKMFGDNPPQSFDELM 255
Cdd:pfam13779 578 -MLSQL-QQMLENLQAGQPQQQQQQGQSEM---QQAMDELGDLLREQ---QQLLDETFrqLQQQGGQQQGQPGQQGQQGQ 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 256 EQMQQQLAQAQSMLDSMSPEAR-----REMEDALAQALDpETQREMAQFA------SLMEQLMPMDD----LRRqypflG 320
Cdd:pfam13779 650 GQQPGQGGQQPGAQMPPQGGAEalgdlAERQQALRRRLE-ELQDELKELGgkepgqALGDAGRAMRDaeeaLGQ-----G 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 321 DDSLTMEQ---AMEMMR-GLQEL-DQLEQSLQEAM------RTGNMDDIDP-----DKLAELLGEEARKIYDELD--RLR 382
Cdd:pfam13779 724 DLAGAVDAqgrALEALRkGAQQLaEAMQQQQGQGQqpgqggQGGRQAGQDPlgrplGGGGDFGDDEAVKVPDEIDaqRAR 803
|
....*
gi 1301426215 383 KLLQE 387
Cdd:pfam13779 804 EILEE 808
|
|
| VWA_CoxE |
pfam05762 |
VWA domain containing CoxE-like protein; This family is annotated by SMART as containing a VWA ... |
454-597 |
6.29e-06 |
|
VWA domain containing CoxE-like protein; This family is annotated by SMART as containing a VWA (von Willebrand factor type A) domain. The exact function of this family is unknown. It is found as part of a CO oxidising (Cox) system operon is several bacteria.
Pssm-ID: 399053 [Multi-domain] Cd Length: 221 Bit Score: 47.77 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 454 DLQATVRNAVLRGGPQV-PVKLSPedfevfRNEHMTRsaTVLLLDQSRSMGLFNNWqaakkvTLALMALMRSQYPRdsLH 532
Cdd:pfam05762 28 DLRRTLRANLRHGGEPVeLVRRKP------RKRRPWR--LVLLLDVSGSMSDYSRV------FLALMHALLRQRPR--TR 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1301426215 533 IVGFS----DYAREIKEEDLA------KCTWNAWVSGTNLHHALMLSRKLLSKEKGGNRQILVVTDGEPTAHLEG 597
Cdd:pfam05762 92 VFAFStrltDLTRQLRERDPDealrrvSARVEDWGGGTRIGAALADFNELVTRPALRRAVVLLVSDGYEGGPREE 166
|
|
| VWA_2 |
pfam13519 |
von Willebrand factor type A domain; |
492-586 |
1.76e-05 |
|
von Willebrand factor type A domain;
Pssm-ID: 463909 [Multi-domain] Cd Length: 103 Bit Score: 44.21 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 492 TVLLLDQSRSMG----LFNNWQAAKKVTLALMALMrsqyPRDSLHIVGFSDYAREIKE-----EDLAKC--TWNAWVSGT 560
Cdd:pfam13519 1 LVFVLDTSGSMRngdyGPTRLEAAKDAVLALLKSL----PGDRVGLVTFGDGPEVLIPltkdrAKILRAlrRLEPKGGGT 76
|
90 100
....*....|....*....|....*.
gi 1301426215 561 NLHHALMLSRKLLSKEKGGNRQILVV 586
Cdd:pfam13519 77 NLAAALQLARAALKHRRKNQPRRIVL 102
|
|
| TerY |
COG4245 |
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown]; |
487-593 |
2.15e-05 |
|
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
Pssm-ID: 443387 [Multi-domain] Cd Length: 196 Bit Score: 45.69 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 487 MTRSATVLLLDQSRSMgLFNNWQAAKK-VTLALMALMRSQYPRDSLHI--VGFSDYAREIKE-EDLAKCTWNAWVS--GT 560
Cdd:COG4245 3 MRRLPVYLLLDTSGSM-SGEPIEALNEgLQALIDELRQDPYALETVEVsvITFDGEAKVLLPlTDLEDFQPPDLSAsgGT 81
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1301426215 561 NLHHALML--------SRKLLSKEKGGNRQILV-VTDGEPTA 593
Cdd:COG4245 82 PLGAALELlldlierrVQKYTAEGKGDWRPVVFlITDGEPTD 123
|
|
| vWA_norD_type |
cd01454 |
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate ... |
491-598 |
7.08e-04 |
|
norD type: Denitrifying bacteria contain both membrane bound and periplasmic nitrate reductases. Denitrification plays a major role in completing the nitrogen cycle by converting nitrate or nitrite to nitrogen gas. The pathway for microbial denitrification has been established as NO3- ------> NO2- ------> NO -------> N2O ---------> N2. This reaction generally occurs under oxygen limiting conditions. Genetic and biochemical studies have shown that the first srep of the biochemical pathway is catalyzed by periplasmic nitrate reductases. This family is widely present in proteobacteria and firmicutes. This version of the domain is also present in some archaeal members. The function of the vWA domain in this sub-group is not known. Members of this subgroup have a conserved MIDAS motif.
Pssm-ID: 238731 [Multi-domain] Cd Length: 174 Bit Score: 41.16 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 491 ATVLLLDQSRSMGLFNNWQAAKKVTLAL-MALMRsqyPRDSLHIVGFSDYAREIKEEDLAKC-TWNAWVSGTNLHHALML 568
Cdd:cd01454 2 AVTLLLDLSGSMRSDRRIDVAKKAAVLLaEALEA---CGVPHAILGFTTDAGGRERVRWIKIkDFDESLHERARKRLAAL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1301426215 569 SR--------------KLLSKEKGGNRQILVVTDGEPTA--HLEGD 598
Cdd:cd01454 79 SPggntrdgaairhaaERLLARPEKRKILLVISDGEPNDldYYEGN 124
|
|
| VWA |
pfam00092 |
von Willebrand factor type A domain; |
493-592 |
9.44e-04 |
|
von Willebrand factor type A domain;
Pssm-ID: 459670 [Multi-domain] Cd Length: 174 Bit Score: 40.72 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 493 VLLLDQSRSMGLfNNWQAAKKVTLALMALMRSQYPRDSLHIVGFSDYAREI--------KEE------DLAKCTWNAWVS 558
Cdd:pfam00092 3 VFLLDGSGSIGG-DNFEKVKEFLKKLVESLDIGPDGTRVGLVQYSSDVRTEfplndyssKEEllsavdNLRYLGGGTTNT 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 1301426215 559 GTNLHHALmlsRKLLSKEKG---GNRQILVV-TDGEPT 592
Cdd:pfam00092 82 GKALKYAL---ENLFSSAAGarpGAPKVVVLlTDGRSQ 116
|
|
| VWA_YIEM_type |
cd01462 |
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ... |
493-590 |
1.35e-03 |
|
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have a conserved MIDAS motif, however, their biochemical function is not well characterised.
Pssm-ID: 238739 [Multi-domain] Cd Length: 152 Bit Score: 39.64 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 493 VLLLDQSRSMGLFNNwQAAKKVTLALMALMRSQYPRdsLHIVGFSDyAREIKEED-----------LAKCTWNAwvsGTN 561
Cdd:cd01462 4 ILLVDQSGSMYGAPE-EVAKAVALALLRIALAENRD--TYLILFDS-EFQTKIVDktddleepvefLSGVQLGG---GTD 76
|
90 100
....*....|....*....|....*....
gi 1301426215 562 LHHALMLSRKLLSKEKGGNRQILVVTDGE 590
Cdd:cd01462 77 INKALRYALELIERRDPRKADIVLITDGY 105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
57-224 |
6.32e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 57 QQMPGLRELMEQLKNQRRQQLQQ-HNMDSVVDDLKERLEDIvQTERDGIKRRLDEAREQVDAQADSQDgEDRAQMEGLLD 135
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQlAALERRIAALARRIRAL-EQELAALEAELAELEKEIAELRAELE-AQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1301426215 136 LLQKRADNNRGKLDDLPESPAGQIKELLEYDFIDPEAQQKFQDLLDALKSQMAQNMGQQMMDQVKgmsEEDMAATREMMR 215
Cdd:COG4942 112 ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL---EALLAELEEERA 188
|
....*....
gi 1301426215 216 QLNQMIKDK 224
Cdd:COG4942 189 ALEALKAER 197
|
|
| |
