NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|149068053|gb|EDM17605|]
View 

rCG39867, isoform CRA_a [Rattus norvegicus]

Protein Classification

vWA domain-containing protein( domain architecture ID 630)

vWA (von Willebrand factor type A) domain-containing protein may be involved in one of a wide variety of important cellular functions, including basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and immune defenses

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 142-297 2.29e-29

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 pfam13768:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 155  Bit Score: 114.42  E-value: 2.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053  142 SRVGLLIDSSQVSSGPQteEFQNDLTSLIDEQLSLKEKLYVLTFGGTTNFLWPDPVEVSASTLQELKLWVKTLQP-EGSS 220
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEP--KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053  221 NLLQALKKVLARKELN----SLVAILRSCPDQPSEFLSDFIQQSTLGrslfIHIVTYKCDDHVPSAILKNLTDALGGHYH 296
Cdd:pfam13768  79 DLLGALKEAVRAPASPgyirHVLLLTDGSPMQGETRVSDLISRAPGK----IRFFAYGLGASISAPMLQLLAEASNGTYE 154


                  .
gi 149068053  297 C 297
Cdd:pfam13768 155 F 155
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 483-623 1.45e-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: 86.89  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053 483 RRVVILLDVSvtNSMF---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTVESWRPEMVAVSHDNLQRAWRWALGLQCQGS 559
Cdd:cd01461    3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149068053 560 RNVLGALRKAIEvdFKDKTKHESQGIYLFTGGVPDQDVHILSAyVAEACGGcdlqlNVCLFYVG 623
Cdd:cd01461   80 TNMNDALEAALE--LLNSSPGSVPQIILLTDGEVTNESQILKN-VREALSG-----RIRLFTFG 135
 
Name Accession Description Interval E-value
VWA_3 pfam13768
von Willebrand factor type A domain;
142-297 2.29e-29

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 114.42  E-value: 2.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053  142 SRVGLLIDSSQVSSGPQteEFQNDLTSLIDEQLSLKEKLYVLTFGGTTNFLWPDPVEVSASTLQELKLWVKTLQP-EGSS 220
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEP--KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053  221 NLLQALKKVLARKELN----SLVAILRSCPDQPSEFLSDFIQQSTLGrslfIHIVTYKCDDHVPSAILKNLTDALGGHYH 296
Cdd:pfam13768  79 DLLGALKEAVRAPASPgyirHVLLLTDGSPMQGETRVSDLISRAPGK----IRFFAYGLGASISAPMLQLLAEASNGTYE 154


                  .
gi 149068053  297 C 297
Cdd:pfam13768 155 F 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 483-623 1.45e-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: 86.89  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053 483 RRVVILLDVSvtNSMF---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTVESWRPEMVAVSHDNLQRAWRWALGLQCQGS 559
Cdd:cd01461    3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149068053 560 RNVLGALRKAIEvdFKDKTKHESQGIYLFTGGVPDQDVHILSAyVAEACGGcdlqlNVCLFYVG 623
Cdd:cd01461   80 TNMNDALEAALE--LLNSSPGSVPQIILLTDGEVTNESQILKN-VREALSG-----RIRLFTFG 135
VWA_3 pfam13768
von Willebrand factor type A domain;
484-639 1.60e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 72.04  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053  484 RVVILLDVSVTNSMFIIHIQHSLRLLLEeQLSNKDYFNIIAFGSTVESWRPEMVAVSHDNLQRAWRWALGLQ-CQGSRNV 562
Cdd:pfam13768   2 DVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQpPLGGSDL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149068053  563 LGALRKAIEVdfKDKTKHESQgIYLFTGGVPDQDVHILSAYVAeacggcDLQLNVCLFYVG-EPQMNTTPPACYASRT 639
Cdd:pfam13768  81 LGALKEAVRA--PASPGYIRH-VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPMLQLLAEAS 149
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 147-299 5.77e-05

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: 44.51  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053 147 LIDSSQVSSGPQTEEFQNDLTSLIDEqLSLKEKLYVLTFGGTTNFLWPDPVEVSASTLQELKLWVKTLQPEGSSNLLQAL 226
Cdd:cd01461    8 VIDTSGSMSGTKIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDAL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149068053 227 KKVlarkelnslVAILRSCPDQPSeflsdfiqqstlgrslFIHIVTykcDDHV--PSAILKNLTDALGGHYHCYS 299
Cdd:cd01461   87 EAA---------LELLNSSPGSVP----------------QIILLT---DGEVtnESQILKNVREALSGRIRLFT 133
 
Name Accession Description Interval E-value
VWA_3 pfam13768
von Willebrand factor type A domain;
142-297 2.29e-29

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 114.42  E-value: 2.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053  142 SRVGLLIDSSQVSSGPQteEFQNDLTSLIDEQLSLKEKLYVLTFGGTTNFLWPDPVEVSASTLQELKLWVKTLQP-EGSS 220
Cdd:pfam13768   1 GDVVIVVDVSSSMSGEP--KLQKDALSVALRQLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQPpLGGS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053  221 NLLQALKKVLARKELN----SLVAILRSCPDQPSEFLSDFIQQSTLGrslfIHIVTYKCDDHVPSAILKNLTDALGGHYH 296
Cdd:pfam13768  79 DLLGALKEAVRAPASPgyirHVLLLTDGSPMQGETRVSDLISRAPGK----IRFFAYGLGASISAPMLQLLAEASNGTYE 154


                  .
gi 149068053  297 C 297
Cdd:pfam13768 155 F 155
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 483-623 1.45e-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: 86.89  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053 483 RRVVILLDVSvtNSMF---IIHIQHSLRLLLEEqLSNKDYFNIIAFGSTVESWRPEMVAVSHDNLQRAWRWALGLQCQGS 559
Cdd:cd01461    3 KEVVFVIDTS--GSMSgtkIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 149068053 560 RNVLGALRKAIEvdFKDKTKHESQGIYLFTGGVPDQDVHILSAyVAEACGGcdlqlNVCLFYVG 623
Cdd:cd01461   80 TNMNDALEAALE--LLNSSPGSVPQIILLTDGEVTNESQILKN-VREALSG-----RIRLFTFG 135
VWA_3 pfam13768
von Willebrand factor type A domain;
484-639 1.60e-14

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 72.04  E-value: 1.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053  484 RVVILLDVSVTNSMFIIHIQHSLRLLLEeQLSNKDYFNIIAFGSTVESWRPEMVAVSHDNLQRAWRWALGLQ-CQGSRNV 562
Cdd:pfam13768   2 DVVIVVDVSSSMSGEPKLQKDALSVALR-QLPTGDKFAVLGFGTLPRPLFPGWRVVSPRSLQEAFQFIKTLQpPLGGSDL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149068053  563 LGALRKAIEVdfKDKTKHESQgIYLFTGGVPDQDVHILSAYVAeacggcDLQLNVCLFYVG-EPQMNTTPPACYASRT 639
Cdd:pfam13768  81 LGALKEAVRA--PASPGYIRH-VLLLTDGSPMQGETRVSDLIS------RAPGKIRFFAYGlGASISAPMLQLLAEAS 149
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 483-629 9.37e-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: 69.90  E-value: 9.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053 483 RRVVILLDVSvtNSMF---IIHIQHSLRLLLE--EQLSNKDYFNIIAFGSTVESWRPEMVAVSHDNLQRAWRWaLGLQCQ 557
Cdd:cd00198    1 ADIVFLLDVS--GSMGgekLDKAKEALKALVSslSASPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDA-LKKGLG 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149068053 558 GSRNVLGALRKAIEVDFKDKTKHESQGIYLFTGGVPDQDVHILSAYVAEAcggCDLQLNVCLFYVGEPQMNT 629
Cdd:cd00198   78 GGTNIGAALRLALELLKSAKRPNARRVIILLTDGEPNDGPELLAEAAREL---RKLGITVYTIGIGDDANED 146
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 474-603 3.05e-06

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: 48.93  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053 474 RRFW---GTVCQRRVVILLDVSVTNSMFIIHI-QHSLRLLLEeQLSNKDYFNIIAFGSTVESWRP----EMVAVSHDNlQ 545
Cdd:cd01463    2 NRSWyiqAATSPKDIVILLDVSGSMTGQRLHLaKQTVSSILD-TLSDNDFFNIITFSNEVNPVVPcfndTLVQATTSN-K 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 149068053 546 RAWRWALG-LQCQGSRNVLGALRKAIEVDFKDK-TKHESQG------IYLFTGGVPDQDVHILSAY 603
Cdd:cd01463   80 KVLKEALDmLEAKGIANYTKALEFAFSLLLKNLqSNHSGSRsqcnqaIMLITDGVPENYKEIFDKY 145
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 147-299 5.77e-05

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: 44.51  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053 147 LIDSSQVSSGPQTEEFQNDLTSLIDEqLSLKEKLYVLTFGGTTNFLWPDPVEVSASTLQELKLWVKTLQPEGSSNLLQAL 226
Cdd:cd01461    8 VIDTSGSMSGTKIEQTKEALLTALKD-LPPGDYFNIIGFSDTVEEFSPSSVSATAENVAAAIEYVNRLQALGGTNMNDAL 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 149068053 227 KKVlarkelnslVAILRSCPDQPSeflsdfiqqstlgrslFIHIVTykcDDHV--PSAILKNLTDALGGHYHCYS 299
Cdd:cd01461   87 EAA---------LELLNSSPGSVP----------------QIILLT---DGEVtnESQILKNVREALSGRIRLFT 133
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 485-595 2.62e-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: 2.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053 485 VVILLDVSvtNSMFIIHIQ---HSLRLLLEeQLSNKDYFNIIAFgSTVESWRPEMVAVSHDNlQRAWRWAL-GLQCQGSR 560
Cdd:cd01466    3 LVAVLDVS--GSMAGDKLQlvkHALRFVIS-SLGDADRLSIVTF-STSAKRLSPLRRMTAKG-KRSAKRVVdGLQAGGGT 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 149068053 561 NVLGALRKAIEVDFKDKTKHESQGIYLFTGGVPDQ 595
Cdd:cd01466   78 NVVGGLKKALKVLGDRRQKNPVASIMLLSDGQDNH 112
VWA_2 pfam13519
von Willebrand factor type A domain;
485-588 4.15e-03

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 37.66  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149068053  485 VVILLDVSvtNSM--------FIIHIQHSLRLLLEEQlsNKDYFNIIAFGSTVEswrpemVAVSHDNLQRAWRWAL-GLQ 555
Cdd:pfam13519   1 LVFVLDTS--GSMrngdygptRLEAAKDAVLALLKSL--PGDRVGLVTFGDGPE------VLIPLTKDRAKILRALrRLE 70

                          90       100       110
                  ....*....|....*....|....*....|....
gi 149068053  556 C-QGSRNVLGALRKAIEVdFKDKTKHESQGIYLF 588
Cdd:pfam13519  71 PkGGGTNLAAALQLARAA-LKHRRKNQPRRIVLI 103
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH