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Conserved domains on  [gi|568989357|ref|XP_006519828|]
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uncharacterized protein LOC102631856 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 12-192 6.57e-41

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 cd01474:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 185  Bit Score: 145.35  E-value: 6.57e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  12 CQATPDIYFVLDKSAHMLYGWPHVHKFVLDMVTRLSNPDLRVSIITYSCKGNVILPITGDREEILKGIERMKYSITAGHE 91
Cdd:cd01474    1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  92 LIYQGLWKANKQIIRGNRRGAQHPSMIIFLLHGPLDNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQIIGLAGGQEYA 171
Cdd:cd01474   81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                        170       180
                 ....*....|....*....|..
gi 568989357 172 F-TNKKPEELSDLIIPLSSKAC 192
Cdd:cd01474  161 FpVTSGFQALSGIIESVVKKAC 182
Anth_Ig super family cl05254
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 190-291 1.30e-18

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


The actual alignment was detected with superfamily member pfam05587:

Pssm-ID: 461684  Cd Length: 102  Bit Score: 81.14  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  190 KACPSLKTAITRIICIRESNPVLLEGYGFDFARRKEDVICRFYFGgaKKTIIDSPPINITKTTVTCPGPIVDSVGRAIHI 269
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTIN--ETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDV 78

                          90       100
                  ....*....|....*....|..
gi 568989357  270 QLSLDNGKNFLHNHLYVATRTC 291
Cdd:pfam05587  79 LVSLNNGKSFISSSLTITATTC 100
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 12-192 6.57e-41

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 145.35  E-value: 6.57e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  12 CQATPDIYFVLDKSAHMLYGWPHVHKFVLDMVTRLSNPDLRVSIITYSCKGNVILPITGDREEILKGIERMKYSITAGHE 91
Cdd:cd01474    1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  92 LIYQGLWKANKQIIRGNRRGAQHPSMIIFLLHGPLDNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQIIGLAGGQEYA 171
Cdd:cd01474   81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                        170       180
                 ....*....|....*....|..
gi 568989357 172 F-TNKKPEELSDLIIPLSSKAC 192
Cdd:cd01474  161 FpVTSGFQALSGIIESVVKKAC 182
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 190-291 1.30e-18

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


Pssm-ID: 461684  Cd Length: 102  Bit Score: 81.14  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  190 KACPSLKTAITRIICIRESNPVLLEGYGFDFARRKEDVICRFYFGgaKKTIIDSPPINITKTTVTCPGPIVDSVGRAIHI 269
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTIN--ETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDV 78

                          90       100
                  ....*....|....*....|..
gi 568989357  270 QLSLDNGKNFLHNHLYVATRTC 291
Cdd:pfam05587  79 LVSLNNGKSFISSSLTITATTC 100
VWA pfam00092
von Willebrand factor type A domain;
17-184 4.71e-11

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 61.52  E-value: 4.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357   17 DIYFVLDKSAHMLYG-WPHVHKFVLDMVTRL--SNPDLRVSIITYSCKGNVILPIT--GDREEILKGIERMKYSiTAGHE 91
Cdd:pfam00092   1 DIVFLLDGSGSIGGDnFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNdySSKEELLSAVDNLRYL-GGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357   92 LIYQGLWKANKQII---RGNRRGAqhPSMIIFLLHGpldNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQI--IGLAG 166
Cdd:pfam00092  80 NTGKALKYALENLFssaAGARPGA--PKVVVLLTDG---RSQDGDPEEVARELKSAGVTVFAVGVGNADDEELrkIASEP 154

                         170
                  ....*....|....*...
gi 568989357  167 GQEYAFTNKKPEELSDLI 184
Cdd:pfam00092 155 GEGHVFTVSDFEALEDLQ 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 17-184 1.87e-10

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: 59.78  E-value: 1.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357    17 DIYFVLDKSAHMLYG-WPHVHKFVLDMVTRL--SNPDLRVSIITYSckGNVI----LPITGDREEILKGIERMKYSiTAG 89
Cdd:smart00327   1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLdiGPDGDRVGLVTFS--DDARvlfpLNDSRSKDALLEALASLSYK-LGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357    90 HELIYQGLWKANKQI---IRGNRRGAQHpsMIIFLLHGPlDNQGYGYSLDETNDTRRMG--GYVCGVGTGQS-ERNQIIG 163
Cdd:smart00327  78 GTNLGAALQYALENLfskSAGSRRGAPK--VVILITDGE-SNDGPKDLLKAAKELKRSGvkVFVVGVGNDVDeEELKKLA 154

                          170       180
                   ....*....|....*....|.
gi 568989357   164 LAGGQEYAFTNKKPEELSDLI 184
Cdd:smart00327 155 SAPGGVYVFLPELLDLLIDLL 175
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 20-121 6.91e-03

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 38.54  E-value: 6.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  20 FVLDKSAHMLYG-WPHVHKFVLDMVTRLsNPDLRVSIITYSCKGNVILPIT--GDREEILKGIERMK--YSiTAghelIY 94
Cdd:COG2304   96 FVIDVSGSMSGDkLELAKEAAKLLVDQL-RPGDRVSIVTFAGDARVLLPPTpaTDRAKILAAIDRLQagGG-TA----LG 169

                         90       100
                 ....*....|....*....|....*..
gi 568989357  95 QGLWKANKQIIRGNRRGAqhPSMIIFL 121
Cdd:COG2304  170 AGLELAYELARKHFIPGR--VNRVILL 194
 
Name Accession Description Interval E-value
vWA_ATR cd01474
ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, ...
 12-192 6.57e-41

ATR (Anthrax Toxin Receptor): Anthrax toxin is a key virulence factor for Bacillus anthracis, the causative agent of anthrax. ATR is the cellular receptor for the anthrax protective antigen and facilitates entry of the toxin into cells. The VWA domain in ATR contains the toxin binding site and mediates interaction with protective antigen. The binding is mediated by divalent cations that binds to the MIDAS motif. These proteins are a family of vertebrate ECM receptors expressed by endothelial cells.


Pssm-ID: 238751 [Multi-domain]  Cd Length: 185  Bit Score: 145.35  E-value: 6.57e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  12 CQATPDIYFVLDKSAHMLYGWPHVHKFVLDMVTRLSNPDLRVSIITYSCKGNVILPITGDREEILKGIERMKYSITAGHE 91
Cdd:cd01474    1 CAGHFDLYFVLDKSGSVAANWIEIYDFVEQLVDRFNSPGLRFSFITFSTRATKILPLTDDSSAIIKGLEVLKKVTPSGQT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  92 LIYQGLWKANKQIIRGNRRGAQHPSMIIFLLHGPLDNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQIIGLAGGQEYA 171
Cdd:cd01474   81 YIHEGLENANEQIFNRNGGGRETVSVIIALTDGQLLLNGHKYPEHEAKLSRKLGAIVYCVGVTDFLKSQLINIADSKEYV 160

                        170       180
                 ....*....|....*....|..
gi 568989357 172 F-TNKKPEELSDLIIPLSSKAC 192
Cdd:cd01474  161 FpVTSGFQALSGIIESVVKKAC 182
Anth_Ig pfam05587
Anthrax receptor extracellular domain; This region is found in the putatively extracellular ...
 190-291 1.30e-18

Anthrax receptor extracellular domain; This region is found in the putatively extracellular N-terminal half of the anthrax receptor. It is probably part of the Ig superfamily and most closely related to pfam01833 (personal obs: C Yeats).


Pssm-ID: 461684  Cd Length: 102  Bit Score: 81.14  E-value: 1.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  190 KACPSLKTAITRIICIRESNPVLLEGYGFDFARRKEDVICRFYFGgaKKTIIDSPPINITKTTVTCPGPIVDSVGRAIHI 269
Cdd:pfam05587   1 KSCIEILSVEPSSVCVGESFQVVLRGRGFNNAKNIDEVLCRFTIN--ETTVYNEKPSSVQDNSILCPAPVLNEAGQTLDV 78

                          90       100
                  ....*....|....*....|..
gi 568989357  270 QLSLDNGKNFLHNHLYVATRTC 291
Cdd:pfam05587  79 LVSLNNGKSFISSSLTITATTC 100
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-166 4.42e-12

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: 64.23  E-value: 4.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  17 DIYFVLDKSAHM-LYGWPHVHKFVLDMVTRLSNPDL--RVSIITYSCKGNVILPIT--GDREEILKGIERMKYsITAGHE 91
Cdd:cd01450    2 DIVFLLDGSESVgPENFEKVKDFIEKLVEKLDIGPDktRVGLVQYSDDVRVEFSLNdyKSKDDLLKAVKNLKY-LGGGGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568989357  92 LIYQGLWKANKQIIRGNRRGAQHPSMIIFLLHGPldNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQIIGLAG 166
Cdd:cd01450   81 NTGKALQYALEQLFSESNARENVPKVIIVLTDGR--SDDGGDPKEAAAKLKDEGIKVFVVGVGPADEEELREIAS 153
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 17-172 1.83e-11

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: 62.58  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  17 DIYFVLDKSAHML-YGWPHVHKFVLDMVTRLSN--PDLRVSIITYSCKGNVILPIT--GDREEILKGIERMKYSiTAGHE 91
Cdd:cd00198    2 DIVFLLDVSGSMGgEKLDKAKEALKALVSSLSAspPGDRVGLVTFGSNARVVLPLTtdTDKADLLEAIDALKKG-LGGGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  92 LIYQGLWKANKQIIRGNRRGAqhPSMIIFLLHGpLDNQGYGYSLDETNDTRRMG--GYVCGVGTGQSERN-QIIGLAGGQ 168
Cdd:cd00198   81 NIGAALRLALELLKSAKRPNA--RRVIILLTDG-EPNDGPELLAEAARELRKLGitVYTIGIGDDANEDElKEIADKTTG 157


                 ....
gi 568989357 169 EYAF 172
Cdd:cd00198  158 GAVF 161
VWA pfam00092
von Willebrand factor type A domain;
17-184 4.71e-11

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 61.52  E-value: 4.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357   17 DIYFVLDKSAHMLYG-WPHVHKFVLDMVTRL--SNPDLRVSIITYSCKGNVILPIT--GDREEILKGIERMKYSiTAGHE 91
Cdd:pfam00092   1 DIVFLLDGSGSIGGDnFEKVKEFLKKLVESLdiGPDGTRVGLVQYSSDVRTEFPLNdySSKEELLSAVDNLRYL-GGGTT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357   92 LIYQGLWKANKQII---RGNRRGAqhPSMIIFLLHGpldNQGYGYSLDETNDTRRMGGYVCGVGTGQSERNQI--IGLAG 166
Cdd:pfam00092  80 NTGKALKYALENLFssaAGARPGA--PKVVVLLTDG---RSQDGDPEEVARELKSAGVTVFAVGVGNADDEELrkIASEP 154

                         170
                  ....*....|....*...
gi 568989357  167 GQEYAFTNKKPEELSDLI 184
Cdd:pfam00092 155 GEGHVFTVSDFEALEDLQ 172
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 17-184 1.87e-10

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: 59.78  E-value: 1.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357    17 DIYFVLDKSAHMLYG-WPHVHKFVLDMVTRL--SNPDLRVSIITYSckGNVI----LPITGDREEILKGIERMKYSiTAG 89
Cdd:smart00327   1 DVVFLLDGSGSMGGNrFELAKEFVLKLVEQLdiGPDGDRVGLVTFS--DDARvlfpLNDSRSKDALLEALASLSYK-LGG 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357    90 HELIYQGLWKANKQI---IRGNRRGAQHpsMIIFLLHGPlDNQGYGYSLDETNDTRRMG--GYVCGVGTGQS-ERNQIIG 163
Cdd:smart00327  78 GTNLGAALQYALENLfskSAGSRRGAPK--VVILITDGE-SNDGPKDLLKAAKELKRSGvkVFVVGVGNDVDeEELKKLA 154

                          170       180
                   ....*....|....*....|.
gi 568989357   164 LAGGQEYAFTNKKPEELSDLI 184
Cdd:smart00327 155 SAPGGVYVFLPELLDLLIDLL 175
VWA_2 pfam13519
von Willebrand factor type A domain;
18-121 1.17e-07

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 49.98  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357   18 IYFVLDKSAHMLYGWPHVHKF--VLDMVTRL--SNPDLRVSIITYSCKGNVILPITGDREEILKGIERMKysITAGHELI 93
Cdd:pfam13519   1 LVFVLDTSGSMRNGDYGPTRLeaAKDAVLALlkSLPGDRVGLVTFGDGPEVLIPLTKDRAKILRALRRLE--PKGGGTNL 78

                          90       100
                  ....*....|....*....|....*...
gi 568989357   94 YQGLWKANKQIirgNRRGAQHPSMIIFL 121
Cdd:pfam13519  79 AAALQLARAAL---KHRRKNQPRRIVLI 103
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 20-173 2.30e-04

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: 41.87  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  20 FVLDKSAHM----LygwPHVHKFVLDMVTRLsNPDLRVSIITYSCKGNVILPIT--GDREEILKGIERMKYS-ITAGHEl 92
Cdd:cd01465    5 FVIDRSGSMdgpkL---PLVKSALKLLVDQL-RPDDRLAIVTYDGAAETVLPATpvRDKAAILAAIDRLTAGgSTAGGA- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  93 iyqGLWKANKQIIRGNRRGAQHPsmiIFLL------HGPLDNQgygySLDETNDTRRMGG-YVCGVGTGQsERN----QI 161
Cdd:cd01465   80 ---GIQLGYQEAQKHFVPGGVNR---ILLAtdgdfnVGETDPD----ELARLVAQKRESGiTLSTLGFGD-NYNedlmEA 148

                        170
                 ....*....|..
gi 568989357 162 IGLAGGQEYAFT 173
Cdd:cd01465  149 IADAGNGNTAYI 160
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 20-121 6.91e-03

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 38.54  E-value: 6.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568989357  20 FVLDKSAHMLYG-WPHVHKFVLDMVTRLsNPDLRVSIITYSCKGNVILPIT--GDREEILKGIERMK--YSiTAghelIY 94
Cdd:COG2304   96 FVIDVSGSMSGDkLELAKEAAKLLVDQL-RPGDRVSIVTFAGDARVLLPPTpaTDRAKILAAIDRLQagGG-TA----LG 169

                         90       100
                 ....*....|....*....|....*..
gi 568989357  95 QGLWKANKQIIRGNRRGAqhPSMIIFL 121
Cdd:COG2304  170 AGLELAYELARKHFIPGR--VNRVILL 194
 
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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