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Conserved domains on  [gi|1622914605|ref|XP_014981261|]
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LOW QUALITY PROTEIN: von Willebrand factor A domain-containing protein 3A [Macaca mulatta]

Protein Classification

vWA domain-containing protein( domain architecture ID 10618673)

vWA (von Willebrand factor type A) domain-containing protein similar to Homo sapiens von Willebrand factor A domain-containing protein 3A (VWA3A)

CATH:  3.40.50.410
PubMed:  10830113|12579041|12388743
SCOP:  3000832

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA_3 pfam13768
von Willebrand factor type A domain;
169-324 6.21e-44

von Willebrand factor type A domain;


:

Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 156.40  E-value: 6.21e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  169 ARVSILIDVSAVSSGPQKeeFQKDLMSLIDEQLSHKEKLFVLSFGTNARSLWPDPMEVSASVLQELKLWVKTLQPD-GGS 247
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPK--LQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  248 NLLQALKKIFTLK---GLDSLVVIMRS-CPDQPSEILSDYIQQSTmgrdLIIHFITYSCDDQMPPAVLKNLAEAVRGYYH 323
Cdd:pfam13768   79 DLLGALKEAVRAPaspGYIRHVLLLTDgSPMQGETRVSDLISRAP----GKIRFFAYGLGASISAPMLQLLAEASNGTYE 154


                   .
gi 1622914605  324 C 324
Cdd:pfam13768  155 F 155
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 963-1109 3.02e-19

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.


The actual alignment was detected with superfamily member cd01461:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 171  Bit Score: 86.11  E-value: 3.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  963 LLDTSGSM-GPYLQQVKtELVLLIWEQLRKRcDSFNLLSFAESLQSWQDTLVETTDAACHEAMQWVTHLQAEGSTSILQA 1041
Cdd:cd01461      8 VIDTSGSMsGTKIEQTK-EALLTALKDLPPG-DYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDA 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622914605 1042 LLKAFSFHD-----LEGLYLLTDGKpDTSCSLVLNEVQRlREKRDVKVHT--ISLNCSDRaaveFLRKLASFTGG 1109
Cdd:cd01461     86 LEAALELLNsspgsVPQIILLTDGE-VTNESQILKNVRE-ALSGRIRLFTfgIGSDVNTY----LLERLAREGRG 154
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 510-618 2.20e-15

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.


The actual alignment was detected with superfamily member cd01461:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 171  Bit Score: 75.33  E-value: 2.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  510 KRVVVLLDISAtnSMY---IIHIQHSLRLLLEEqLSNKDYFNLIAFGSTSESWRPEMVPMSHDNLQSAWRWALNLRCWGS 586
Cdd:cd01461      3 KEVVFVIDTSG--SMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622914605  587 RNVLSALRKAVEvdFKDKDKHQSQGIYLFTGG 618
Cdd:cd01461     80 TNMNDALEAALE--LLNSSPGSVPQIILLTDG 109
 
Name Accession Description Interval E-value
VWA_3 pfam13768
von Willebrand factor type A domain;
169-324 6.21e-44

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 156.40  E-value: 6.21e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  169 ARVSILIDVSAVSSGPQKeeFQKDLMSLIDEQLSHKEKLFVLSFGTNARSLWPDPMEVSASVLQELKLWVKTLQPD-GGS 247
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPK--LQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  248 NLLQALKKIFTLK---GLDSLVVIMRS-CPDQPSEILSDYIQQSTmgrdLIIHFITYSCDDQMPPAVLKNLAEAVRGYYH 323
Cdd:pfam13768   79 DLLGALKEAVRAPaspGYIRHVLLLTDgSPMQGETRVSDLISRAP----GKIRFFAYGLGASISAPMLQLLAEASNGTYE 154


                   .
gi 1622914605  324 C 324
Cdd:pfam13768  155 F 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 963-1109 3.02e-19

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: 86.11  E-value: 3.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  963 LLDTSGSM-GPYLQQVKtELVLLIWEQLRKRcDSFNLLSFAESLQSWQDTLVETTDAACHEAMQWVTHLQAEGSTSILQA 1041
Cdd:cd01461      8 VIDTSGSMsGTKIEQTK-EALLTALKDLPPG-DYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDA 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622914605 1042 LLKAFSFHD-----LEGLYLLTDGKpDTSCSLVLNEVQRlREKRDVKVHT--ISLNCSDRaaveFLRKLASFTGG 1109
Cdd:cd01461     86 LEAALELLNsspgsVPQIILLTDGE-VTNESQILKNVRE-ALSGRIRLFTfgIGSDVNTY----LLERLAREGRG 154
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 960-1112 2.05e-17

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: 83.45  E-value: 2.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSMGPY--LQQVKTELVLLIwEQLRKRcDSFNLLSFAESLqswqDTLVE-TTDAAchEAMQWVTHLQAEGST 1036
Cdd:COG1240     95 VVLVVDASGSMAAEnrLEAAKGALLDFL-DDYRPR-DRVGLVAFGGEA----EVLLPlTRDRE--ALKRALDELPPGGGT 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1037 SILQALLKAFSFHDLEG------LYLLTDGKPDTSCSLVLNEVQRLREkRDVKVHTISLNcSDRAAVEFLRKLASFTGGR 1110
Cdd:COG1240    167 PLGDALALALELLKRADparrkvIVLLTDGRDNAGRIDPLEAAELAAA-AGIRIYTIGVG-TEAVDEGLLREIAEATGGR 244


                   ..
gi 1622914605 1111 YH 1112
Cdd:COG1240    245 YF 246
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 510-618 2.20e-15

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: 75.33  E-value: 2.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  510 KRVVVLLDISAtnSMY---IIHIQHSLRLLLEEqLSNKDYFNLIAFGSTSESWRPEMVPMSHDNLQSAWRWALNLRCWGS 586
Cdd:cd01461      3 KEVVFVIDTSG--SMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622914605  587 RNVLSALRKAVEvdFKDKDKHQSQGIYLFTGG 618
Cdd:cd01461     80 TNMNDALEAALE--LLNSSPGSVPQIILLTDG 109
VWA_3 pfam13768
von Willebrand factor type A domain;
960-1113 2.17e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.66  E-value: 2.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSM-GPYLQQVKTELVLLiwEQLRKRcDSFNLLSFAESLQSWQDTLVETTDAACHEAMQWVTHLQA-EGSTS 1037
Cdd:pfam13768    3 VVIVVDVSSSMsGEPKLQKDALSVAL--RQLPTG-DKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGSD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1038 ILQALLKAFSFHDLEG----LYLLTDGKPDTSCSLVLNEVQRLRekRDVKVHTISLNCSDRAAVefLRKLASFTGGRYHC 1113
Cdd:pfam13768   80 LLGALKEAVRAPASPGyirhVLLLTDGSPMQGETRVSDLISRAP--GKIRFFAYGLGASISAPM--LQLLAEASNGTYEF 155
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 960-1112 1.03e-11

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: 64.78  E-value: 1.03e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605   960 VCILLDTSGSMGP-YLQQVKTELVLLIwEQLRKRCDS--FNLLSFAESLQSWQDTLVETTDAACHEAMQwVTHLQAEGST 1036
Cdd:smart00327    2 VVFLLDGSGSMGGnRFELAKEFVLKLV-EQLDIGPDGdrVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  1037 SILQALLKAFS--FHDLEG--------LYLLTDGKPDTSCSLVLNEVQRLREKRdVKVHTISLncSDRAAVEFLRKLASF 1106
Cdd:smart00327   80 NLGAALQYALEnlFSKSAGsrrgapkvVILITDGESNDGPKDLLKAAKELKRSG-VKVFVVGV--GNDVDEEELKKLASA 156


                    ....*.
gi 1622914605  1107 TGGRYH 1112
Cdd:smart00327  157 PGGVYV 162
VWA_3 pfam13768
von Willebrand factor type A domain;
510-684 1.00e-09

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 58.56  E-value: 1.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  510 KRVVVLLDISATNSMYIIHIQHSLRLLLEeQLSNKDYFNLIAFGSTSESWRPEMVPMSHDNLQSAWRW--ALNLRCWGSr 587
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFikTLQPPLGGS- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  588 NVLSALRKAVEVDFKDK-DKHqsqgIYLFTGGIPDQDMPTISAYMAeacsgcDLQLNVCLFYVG-EPKMDTTPPacyasr 665
Cdd:pfam13768   79 DLLGALKEAVRAPASPGyIRH----VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPML------ 142

                          170
                   ....*....|....*....
gi 1622914605  666 tdtaaayKEVTRAAGGRFH 684
Cdd:pfam13768  143 -------QLLAEASNGTYE 154
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 174-269 2.35e-06

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: 49.14  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  174 LIDVSAVSSGPqKEEFQKDLMSLIDEQLSHKEKLFVLSFGTNARSLWPDPMEVSASVLQELKLWVKTLQPDGGSNLLQAL 253
Cdd:cd01461      8 VIDTSGSMSGT-KIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDAL 86

                           90       100
                   ....*....|....*....|
gi 1622914605  254 KKIFTLK----GLDSLVVIM 269
Cdd:cd01461     87 EAALELLnsspGSVPQIILL 106
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 960-1109 3.49e-06

calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out AC found a row in 1A13.INFO that was not parsed out EC found a row in 1A13.INFO that was not parsed out GA found a row in 1A13.INFO that was not parsed out SO found a row in 1A13.INFO that was not parsed out RH found a row in 1A13.INFO that was not parsed out EN found a row in 1A13.INFO that was not parsed out GS found a row in 1A13.INFO that was not parsed out AL found a row in 1A13.INFO that was not parsed out The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13) found a row in 1A13.INFO that was not parsed out found a row in 1A13.INFO that was not parsed out Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca found a row in 1A13.INFO that was not parsed out 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified found a row in 1A13.INFO that was not parsed out complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent found a row in 1A13.INFO that was not parsed out mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, found a row in 1A13.INFO that was not parsed out Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in found a row in 1A13.INFO that was not parsed out several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions. found a row in 1A13.INFO that was not parsed out [Transport and binding proteins, Anions]


Pssm-ID: 129946 [Multi-domain]  Cd Length: 863  Bit Score: 51.42  E-value: 3.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSMGP-----YLQQVkTELVLLiweQLRKRCDSFNLLSFaESLQSWQDTLVETTDAACHEAMQWVTHLQAEG 1034
Cdd:TIGR00868  307 VCLVLDKSGSMTVedrlkRMNQA-AKLFLL---QTVEKGSWVGMVTF-DSAAYIKNELIQITSSAERDALTANLPTAASG 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1035 STSILQALLKAF-----SFHDLEG--LYLLTDGKpDTSCSLVLNEVQRlrekRDVKVHTISLNcsdRAAVEFLRKLASFT 1107
Cdd:TIGR00868  382 GTSICSGLKAAFqvikkSYQSTDGseIVLLTDGE-DNTISSCFEEVKQ----SGAIIHTIALG---PSAAKELEELSDMT 453


                   ..
gi 1622914605 1108 GG 1109
Cdd:TIGR00868  454 GG 455
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 167-347 7.00e-05

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: 46.08  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  167 KGARVSILIDVSAVSSGPQKEEFQKD-LMSLIDeQLSHKEKLFVLSFGTNARSLWPdpmeVSASVlQELKLWVKTLQPDG 245
Cdd:COG1240     91 RGRDVVLVVDASGSMAAENRLEAAKGaLLDFLD-DYRPRDRVGLVAFGGEAEVLLP----LTRDR-EALKRALDELPPGG 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  246 GSNLLQALKKiftlkgldSLVVIMRSCPDQPSEI--LSD---------YIQQSTMGRDLIIHFITYSC-DDQMPPAVLKN 313
Cdd:COG1240    165 GTPLGDALAL--------ALELLKRADPARRKVIvlLTDgrdnagridPLEAAELAAAAGIRIYTIGVgTEAVDEGLLRE 236

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1622914605  314 LAEAVRGYYhcyspkmelYTSRDMDELLAEIQKA 347
Cdd:COG1240    237 IAEATGGRY---------FRADDLSELAAIYREI 261
 
Name Accession Description Interval E-value
VWA_3 pfam13768
von Willebrand factor type A domain;
169-324 6.21e-44

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 156.40  E-value: 6.21e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  169 ARVSILIDVSAVSSGPQKeeFQKDLMSLIDEQLSHKEKLFVLSFGTNARSLWPDPMEVSASVLQELKLWVKTLQPD-GGS 247
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPK--LQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPPlGGS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  248 NLLQALKKIFTLK---GLDSLVVIMRS-CPDQPSEILSDYIQQSTmgrdLIIHFITYSCDDQMPPAVLKNLAEAVRGYYH 323
Cdd:pfam13768   79 DLLGALKEAVRAPaspGYIRHVLLLTDgSPMQGETRVSDLISRAP----GKIRFFAYGLGASISAPMLQLLAEASNGTYE 154


                   .
gi 1622914605  324 C 324
Cdd:pfam13768  155 F 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 963-1109 3.02e-19

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: 86.11  E-value: 3.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  963 LLDTSGSM-GPYLQQVKtELVLLIWEQLRKRcDSFNLLSFAESLQSWQDTLVETTDAACHEAMQWVTHLQAEGSTSILQA 1041
Cdd:cd01461      8 VIDTSGSMsGTKIEQTK-EALLTALKDLPPG-DYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDA 85

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622914605 1042 LLKAFSFHD-----LEGLYLLTDGKpDTSCSLVLNEVQRlREKRDVKVHT--ISLNCSDRaaveFLRKLASFTGG 1109
Cdd:cd01461     86 LEAALELLNsspgsVPQIILLTDGE-VTNESQILKNVRE-ALSGRIRLFTfgIGSDVNTY----LLERLAREGRG 154
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 960-1109 8.06e-19

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: 84.92  E-value: 8.06e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSMGPYLQQVKTELVLLIWEQLRKRC--DSFNLLSFAESLQSWQDTLVETTDAACHEAMQWVTHlQAEGSTS 1037
Cdd:cd00198      3 IVFLLDVSGSMGGEKLDKAKEALKALVSSLSASPpgDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALKK-GLGGGTN 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622914605 1038 ILQALLKAFSFHDLEG-------LYLLTDGKPDTSCSLVLNEVQRLReKRDVKVHTISLncSDRAAVEFLRKLASFTGG 1109
Cdd:cd00198     82 IGAALRLALELLKSAKrpnarrvIILLTDGEPNDGPELLAEAARELR-KLGITVYTIGI--GDDANEDELKEIADKTTG 157
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 960-1112 2.05e-17

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: 83.45  E-value: 2.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSMGPY--LQQVKTELVLLIwEQLRKRcDSFNLLSFAESLqswqDTLVE-TTDAAchEAMQWVTHLQAEGST 1036
Cdd:COG1240     95 VVLVVDASGSMAAEnrLEAAKGALLDFL-DDYRPR-DRVGLVAFGGEA----EVLLPlTRDRE--ALKRALDELPPGGGT 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1037 SILQALLKAFSFHDLEG------LYLLTDGKPDTSCSLVLNEVQRLREkRDVKVHTISLNcSDRAAVEFLRKLASFTGGR 1110
Cdd:COG1240    167 PLGDALALALELLKRADparrkvIVLLTDGRDNAGRIDPLEAAELAAA-AGIRIYTIGVG-TEAVDEGLLREIAEATGGR 244


                   ..
gi 1622914605 1111 YH 1112
Cdd:COG1240    245 YF 246
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 510-618 2.20e-15

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: 75.33  E-value: 2.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  510 KRVVVLLDISAtnSMY---IIHIQHSLRLLLEEqLSNKDYFNLIAFGSTSESWRPEMVPMSHDNLQSAWRWALNLRCWGS 586
Cdd:cd01461      3 KEVVFVIDTSG--SMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622914605  587 RNVLSALRKAVEvdFKDKDKHQSQGIYLFTGG 618
Cdd:cd01461     80 TNMNDALEAALE--LLNSSPGSVPQIILLTDG 109
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 960-1112 2.85e-15

Secreted protein containing bacterial Ig-like domain and vWFA domain [General function prediction only];


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 77.83  E-value: 2.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSM-GPYLQQVKTELVLLIwEQLRKRcDSFNLLSFAESLQswqdTLVETTDAA-CHEAMQWVTHLQAEGSTS 1037
Cdd:COG2304     94 LVFVIDVSGSMsGDKLELAKEAAKLLV-DQLRPG-DRVSIVTFAGDAR----VLLPPTPATdRAKILAAIDRLQAGGGTA 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1038 ILQALLKAFSF---HDLEG----LYLLTDGKPD---TSCSLVLNEVQRLREKrDVKVHTI----SLNcsdraaVEFLRKL 1103
Cdd:COG2304    168 LGAGLELAYELarkHFIPGrvnrVILLTDGDANvgiTDPEELLKLAEEAREE-GITLTTLgvgsDYN------EDLLERL 240


                   ....*....
gi 1622914605 1104 ASFTGGRYH 1112
Cdd:COG2304    241 ADAGGGNYY 249
VWA_3 pfam13768
von Willebrand factor type A domain;
960-1113 2.17e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 71.66  E-value: 2.17e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSM-GPYLQQVKTELVLLiwEQLRKRcDSFNLLSFAESLQSWQDTLVETTDAACHEAMQWVTHLQA-EGSTS 1037
Cdd:pfam13768    3 VVIVVDVSSSMsGEPKLQKDALSVAL--RQLPTG-DKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGSD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1038 ILQALLKAFSFHDLEG----LYLLTDGKPDTSCSLVLNEVQRLRekRDVKVHTISLNCSDRAAVefLRKLASFTGGRYHC 1113
Cdd:pfam13768   80 LLGALKEAVRAPASPGyirhVLLLTDGSPMQGETRVSDLISRAP--GKIRFFAYGLGASISAPM--LQLLAEASNGTYEF 155
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 941-1104 4.70e-14

Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain [Function unknown];


Pssm-ID: 441973 [Multi-domain]  Cd Length: 263  Bit Score: 73.56  E-value: 4.70e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  941 LQWLLSGSRRLFGTVLESKVCILLDTSGSM-GPYLQQVKTELVLLIwEQLRKRcDSFNLLSFaeSLQSWQDTLVeTTDAA 1019
Cdd:COG2425    102 ALLLLAAPASAAVPLLEGPVVLCVDTSGSMaGSKEAAAKAAALALL-RALRPN-RRFGVILF--DTEVVEDLPL-TADDG 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1020 CHEAMQWVTHLQAEGSTSILQALLKAfsFHDLEG-------LYLLTDGKPDTSCSLVLNEVQrlREKRDVKVHTISLncS 1092
Cdd:COG2425    177 LEDAIEFLSGLFAGGGTDIAPALRAA--LELLEEpdyrnadIVLITDGEAGVSPEELLREVR--AKESGVRLFTVAI--G 250

                          170
                   ....*....|..
gi 1622914605 1093 DRAAVEFLRKLA 1104
Cdd:COG2425    251 DAGNPGLLEALA 262
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 512-652 6.26e-14

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: 70.67  E-value: 6.26e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  512 VVVLLDISAtnSM---YIIHIQHSLRLLLE--EQLSNKDYFNLIAFGSTSESWRPEMVPMSHDNLQSAWRWaLNLRCWGS 586
Cdd:cd00198      3 IVFLLDVSG--SMggeKLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDA-LKKGLGGG 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622914605  587 RNVLSALRKAVEVDFKDKDKHQSQGIYLFTGGIPDQDMPTISAYMAEAcsgCDLQLNVCLFYVGEP 652
Cdd:cd00198     80 TNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAAREL---RKLGITVYTIGIGDD 142
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 960-1112 1.03e-11

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: 64.78  E-value: 1.03e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605   960 VCILLDTSGSMGP-YLQQVKTELVLLIwEQLRKRCDS--FNLLSFAESLQSWQDTLVETTDAACHEAMQwVTHLQAEGST 1036
Cdd:smart00327    2 VVFLLDGSGSMGGnRFELAKEFVLKLV-EQLDIGPDGdrVGLVTFSDDARVLFPLNDSRSKDALLEALA-SLSYKLGGGT 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  1037 SILQALLKAFS--FHDLEG--------LYLLTDGKPDTSCSLVLNEVQRLREKRdVKVHTISLncSDRAAVEFLRKLASF 1106
Cdd:smart00327   80 NLGAALQYALEnlFSKSAGsrrgapkvVILITDGESNDGPKDLLKAAKELKRSG-VKVFVVGV--GNDVDEEELKKLASA 156


                    ....*.
gi 1622914605  1107 TGGRYH 1112
Cdd:smart00327  157 PGGVYV 162
VWA_3 pfam13768
von Willebrand factor type A domain;
510-684 1.00e-09

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 58.56  E-value: 1.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  510 KRVVVLLDISATNSMYIIHIQHSLRLLLEeQLSNKDYFNLIAFGSTSESWRPEMVPMSHDNLQSAWRW--ALNLRCWGSr 587
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFikTLQPPLGGS- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  588 NVLSALRKAVEVDFKDK-DKHqsqgIYLFTGGIPDQDMPTISAYMAeacsgcDLQLNVCLFYVG-EPKMDTTPPacyasr 665
Cdd:pfam13768   79 DLLGALKEAVRAPASPGyIRH----VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPML------ 142

                          170
                   ....*....|....*....
gi 1622914605  666 tdtaaayKEVTRAAGGRFH 684
Cdd:pfam13768  143 -------QLLAEASNGTYE 154
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 961-1087 2.85e-07

VWA subgroup: 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. Not much is known about the function of the VWA domain in these proteins. The members do have a conserved MIDAS motif. The biochemical function however is not known.


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 51.50  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  961 CILLDTSGSM-GPYLQQVKTELVLLIwEQLRKRcDSFNLLSFAESLQswqdTLVETT----DAACHEAMQwvtHLQAEGS 1035
Cdd:cd01465      4 VFVIDRSGSMdGPKLPLVKSALKLLV-DQLRPD-DRLAIVTYDGAAE----TVLPATpvrdKAAILAAID---RLTAGGS 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622914605 1036 TSI---LQALLKAFSFHDLEG----LYLLTDGKP---DTSCSLVLNEVQRLREKrDVKVHTI 1087
Cdd:cd01465     75 TAGgagIQLGYQEAQKHFVPGgvnrILLATDGDFnvgETDPDELARLVAQKRES-GITLSTL 135
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 959-1090 2.12e-06

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: 48.88  E-value: 2.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  959 KVCILLDTSGSMGPYLQQVKTELVLLIWEQLRKRCDSFNLLSFAEslqSWQDTLVETTDaACHEAMQWVTHLQAEGSTSI 1038
Cdd:cd01462      2 PVILLVDQSGSMYGAPEEVAKAVALALLRIALAENRDTYLILFDS---EFQTKIVDKTD-DLEEPVEFLSGVQLGGGTDI 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622914605 1039 LQALLKAFSF---HDLEG--LYLLTDGKPDTSCSLVLNEVQrLREKRDVKVHTISLN 1090
Cdd:cd01462     78 NKALRYALELierRDPRKadIVLITDGYEGGVSDELLREVE-LKRSRVARFVALALG 133
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 174-269 2.35e-06

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: 49.14  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  174 LIDVSAVSSGPqKEEFQKDLMSLIDEQLSHKEKLFVLSFGTNARSLWPDPMEVSASVLQELKLWVKTLQPDGGSNLLQAL 253
Cdd:cd01461      8 VIDTSGSMSGT-KIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDAL 86

                           90       100
                   ....*....|....*....|
gi 1622914605  254 KKIFTLK----GLDSLVVIM 269
Cdd:cd01461     87 EAALELLnsspGSVPQIILL 106
VWA pfam00092
von Willebrand factor type A domain;
960-1105 2.58e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 48.81  E-value: 2.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSMGPY-LQQVKTELVLLIwEQLRKRCDS--FNLLSFAE------SLQSWQDTlvettdaacHEAMQWVTHL 1030
Cdd:pfam00092    2 IVFLLDGSGSIGGDnFEKVKEFLKKLV-ESLDIGPDGtrVGLVQYSSdvrtefPLNDYSSK---------EELLSAVDNL 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1031 --QAEGSTSILQALLKA--FSFHDLEG--------LYLLTDGKPDtsCSLVLNEVQRLREkRDVKVHTISLNcsdRAAVE 1098
Cdd:pfam00092   72 ryLGGGTTNTGKALKYAleNLFSSAAGarpgapkvVVLLTDGRSQ--DGDPEEVARELKS-AGVTVFAVGVG---NADDE 145


                   ....*..
gi 1622914605 1099 FLRKLAS 1105
Cdd:pfam00092  146 ELRKIAS 152
hCaCC TIGR00868
calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out ...
 960-1109 3.49e-06

calcium-activated chloride channel protein 1; found a row in 1A13.INFO that was not parsed out AC found a row in 1A13.INFO that was not parsed out EC found a row in 1A13.INFO that was not parsed out GA found a row in 1A13.INFO that was not parsed out SO found a row in 1A13.INFO that was not parsed out RH found a row in 1A13.INFO that was not parsed out EN found a row in 1A13.INFO that was not parsed out GS found a row in 1A13.INFO that was not parsed out AL found a row in 1A13.INFO that was not parsed out The Epithelial Chloride Channel (E-ClC) Family (TC 1.A.13) found a row in 1A13.INFO that was not parsed out found a row in 1A13.INFO that was not parsed out Mammals have multiple isoforms of epithelial chloride channel proteins. The first member of this family to be characterized was a respiratory epithelium, Ca found a row in 1A13.INFO that was not parsed out 2+-regulated, chloride channel protein isolated from bovine tracheal apical membranes. It was biochemically characterized as a 140 kDa complex. The purified found a row in 1A13.INFO that was not parsed out complex when reconstituted in a planar lipid bilayer behaved as an anion-selective channel. It was regulated by Ca 2+ via a calmodulin kinase II-dependent found a row in 1A13.INFO that was not parsed out mechanism. When the cRNA was injected into Xenopus oocytes, an outward rectifying, DIDS-sensitive, anion conductance was measured. A related gene, found a row in 1A13.INFO that was not parsed out Lu-ECAM, was cloned from the bovine aortic endothelial cell line, BAEC. It is expressed in the lung and spleen but not in the trachea. Homologues are found in found a row in 1A13.INFO that was not parsed out several mammals, and at least three paralogues(hCaCC-1-3) are present in humans, each with different tissue distributions. found a row in 1A13.INFO that was not parsed out [Transport and binding proteins, Anions]


Pssm-ID: 129946 [Multi-domain]  Cd Length: 863  Bit Score: 51.42  E-value: 3.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSMGP-----YLQQVkTELVLLiweQLRKRCDSFNLLSFaESLQSWQDTLVETTDAACHEAMQWVTHLQAEG 1034
Cdd:TIGR00868  307 VCLVLDKSGSMTVedrlkRMNQA-AKLFLL---QTVEKGSWVGMVTF-DSAAYIKNELIQITSSAERDALTANLPTAASG 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1035 STSILQALLKAF-----SFHDLEG--LYLLTDGKpDTSCSLVLNEVQRlrekRDVKVHTISLNcsdRAAVEFLRKLASFT 1107
Cdd:TIGR00868  382 GTSICSGLKAAFqvikkSYQSTDGseIVLLTDGE-DNTISSCFEEVKQ----SGAIIHTIALG---PSAAKELEELSDMT 453


                   ..
gi 1622914605 1108 GG 1109
Cdd:TIGR00868  454 GG 455
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 167-347 7.00e-05

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: 46.08  E-value: 7.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  167 KGARVSILIDVSAVSSGPQKEEFQKD-LMSLIDeQLSHKEKLFVLSFGTNARSLWPdpmeVSASVlQELKLWVKTLQPDG 245
Cdd:COG1240     91 RGRDVVLVVDASGSMAAENRLEAAKGaLLDFLD-DYRPRDRVGLVAFGGEAEVLLP----LTRDR-EALKRALDELPPGG 164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  246 GSNLLQALKKiftlkgldSLVVIMRSCPDQPSEI--LSD---------YIQQSTMGRDLIIHFITYSC-DDQMPPAVLKN 313
Cdd:COG1240    165 GTPLGDALAL--------ALELLKRADPARRKVIvlLTDgrdnagridPLEAAELAAAAGIRIYTIGVgTEAVDEGLLRE 236

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1622914605  314 LAEAVRGYYhcyspkmelYTSRDMDELLAEIQKA 347
Cdd:COG1240    237 IAEATGGRY---------FRADDLSELAAIYREI 261
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
960-1105 9.54e-05

Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 44.53  E-value: 9.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSM-GPYLQQVKTELVLLIwEQLRKRCDS-----FNLLSFAESLQswqdTLVETTDAachEAMQWvTHLQAE 1033
Cdd:COG4245      8 VYLLLDTSGSMsGEPIEALNEGLQALI-DELRQDPYAletveVSVITFDGEAK----VLLPLTDL---EDFQP-PDLSAS 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1034 GSTSILQAL---------LKAFSFHDLEG-----LYLLTDGKP-DTSCSLVLNEVQRLREKRDVKVHTISLncsDRAA-V 1097
Cdd:COG4245     79 GGTPLGAALellldlierRVQKYTAEGKGdwrpvVFLITDGEPtDSDWEAALQRLKDGEAAKKANIFAIGV---GPDAdT 155


                   ....*...
gi 1622914605 1098 EFLRKLAS 1105
Cdd:COG4245    156 EVLKQLTD 163
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 501-621 1.30e-04

VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five proteins: alpha 1, beta 1, gamma, alpha 2 and delta. The alpha 2 and delta subunits result from proteolytic processing of a single gene product and carries at its N-terminus the VWA and cache domains, The alpha 2 delta gene family has orthologues in D. melanogaster and C. elegans but none have been detected in aither A. thaliana or yeast. The exact biochemical function of the VWA domain is not known but the alpha 2 delta complex has been shown to regulate various functional properties of the channel complex.


Pssm-ID: 238740 [Multi-domain]  Cd Length: 190  Bit Score: 44.31  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  501 RRIW---GTVCEKRVVVLLDISATNSMYIIHI-QHSLRLLLEeQLSNKDYFNLIAFGSTSESWRP----EMVPMSHDNLQ 572
Cdd:cd01463      2 NRSWyiqAATSPKDIVILLDVSGSMTGQRLHLaKQTVSSILD-TLSDNDFFNIITFSNEVNPVVPcfndTLVQATTSNKK 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622914605  573 SAWRWALNLRCWGSRNVLSALRKAVEVDFKDKDKHQS-------QGIYLFTGGIPD 621
Cdd:cd01463     81 VLKEALDMLEAKGIANYTKALEFAFSLLLKNLQSNHSgsrsqcnQAIMLITDGVPE 136
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 512-622 3.59e-04

VWA C3HC4-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. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 42.38  E-value: 3.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  512 VVVLLDISATNSMYIIH-IQHSLRLLLEeQLSNKDYFNLIAFGSTSESWRPeMVPMSHDNLQSAWRWALNLRCWGSRNVL 590
Cdd:cd01466      3 LVAVLDVSGSMAGDKLQlVKHALRFVIS-SLGDADRLSIVTFSTSAKRLSP-LRRMTAKGKRSAKRVVDGLQAGGGTNVV 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1622914605  591 SALRKAVEVDFKDKDKHQSQGIYLFTGGIPDQ 622
Cdd:cd01466     81 GGLKKALKVLGDRRQKNPVASIMLLSDGQDNH 112
vWA_subfamily cd01464
VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 960-1105 7.63e-04

VWA subfamily: 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 no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.


Pssm-ID: 238741 [Multi-domain]  Cd Length: 176  Bit Score: 41.56  E-value: 7.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  960 VCILLDTSGSM-GPYLQQVKTELVLLIWEQlrkRCDSFNLLS-------FAESLQSWQDtLVETTDaacheamQWVTHLQ 1031
Cdd:cd01464      6 IYLLLDTSGSMaGEPIEALNQGLQMLQSEL---RQDPYALESveisvitFDSAARVIVP-LTPLES-------FQPPRLT 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1032 AEGSTSILQALLKAfsFHDLEG----------------LYLLTDGKP-DTSCSlvlnEVQRLREKRDVKVHTISLNCSDR 1094
Cdd:cd01464     75 ASGGTSMGAALELA--LDCIDRrvqryradqkgdwrpwVFLLTDGEPtDDLTA----AIERIKEARDSKGRIVACAVGPK 148

                          170
                   ....*....|.
gi 1622914605 1095 AAVEFLRKLAS 1105
Cdd:cd01464    149 ADLDTLKQITE 159
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 174-323 8.74e-04

VWA C3HC4-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. Membes of this subgroup belong to Zinc-finger family as they are found fused to RING finger domains. The MIDAS motif is not conserved in all the members of this family. The function of vWA domains however is not known.


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 41.22  E-value: 8.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  174 LIDVSAVSSGpQKEEFQKDLMSLIDEQLSHKEKLFVLSFGTNARSLWPdPMEVSASVLQELKLWVKTLQPDGGSNLLQAL 253
Cdd:cd01466      6 VLDVSGSMAG-DKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-LRRMTAKGKRSAKRVVDGLQAGGGTNVVGGL 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  254 KkiftlKGLDslvVIMRSCPDQPSE---ILSDYiQQSTMGRDL-------IIHFITYSCDDQmpPAVLKNLAEAVRGYYH 323
Cdd:cd01466     84 K-----KALK---VLGDRRQKNPVAsimLLSDG-QDNHGAVVLradnapiPIHTFGLGASHD--PALLAFIAEITGGTFS 152
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 962-1113 5.58e-03

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: 238727 [Multi-domain]  Cd Length: 161  Bit Score: 38.81  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605  962 ILLDTSGSMGPY-LQQVKTELVLLIwEQLR--KRCDSFNLLSFAESLQSWQDTLVETTDAACHEAMQWVTHLQAEGsTSI 1038
Cdd:cd01450      5 FLLDGSESVGPEnFEKVKDFIEKLV-EKLDigPDKTRVGLVQYSDDVRVEFSLNDYKSKDDLLKAVKNLKYLGGGG-TNT 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622914605 1039 LQALLKAFSFHDLEG---------LYLLTDGKPDTScSLVLNEVQRLREKrDVKVHTISLNcsdRAAVEFLRKLASfTGG 1109
Cdd:cd01450     83 GKALQYALEQLFSESnarenvpkvIIVLTDGRSDDG-GDPKEAAAKLKDE-GIKVFVVGVG---PADEEELREIAS-CPS 156


                   ....
gi 1622914605 1110 RYHC 1113
Cdd:cd01450    157 ERHV 160
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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