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Conserved domains on  [gi|19921336|ref|NP_609711|]
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lethal (2) 34Fd [Drosophila melanogaster]

Protein Classification

WD repeat NOL10/ENP2 family protein( domain architecture ID 11456824)

WD repeat NOL10/ENP2 family protein contains WD40 repeats that fold into a beta-propeller structure and functions as a scaffold, such as Schizosaccharomyces pombe ribosome biogenesis protein enp2 homolog that may be involved in rRNA-processing and ribosome biosynthesis

CATH:  2.130.10.10
Gene Ontology:  GO:0005515
PubMed:  21468892|18925368|10322433|8090199|30069656|29026209
SCOP:  4002744

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
150-303 1.35e-08

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.61  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 150 FIVGVGRD--IFRLNLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGTVEAWDPRTKQRCSTLDVAMklpgvkefP 227
Cdd:COG2319 176 LLASGSDDgtVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS--------G 247

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921336 228 SVTALKF-RNGLHMGVGTASGHVLIYDIRAKQPLLVKNHLNRlPIKRLAFNP-AQNAVYSLDEATLKLWDEQTGKQIA 303
Cdd:COG2319 248 SVRSVAFsPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG-GVNSVAFSPdGKLLASGSDDGTVRLWDLATGKLLR 324
NUC153 pfam08159
NUC153 domain; This small domain is found in a a novel nucleolar family.
 476-503 2.54e-07

NUC153 domain; This small domain is found in a a novel nucleolar family.


:

Pssm-ID: 462385 [Multi-domain]  Cd Length: 29  Bit Score: 46.94  E-value: 2.54e-07
                          10        20
                  ....*....|....*....|....*...
gi 19921336   476 DSRFKAMFENADFEVNKSAEEYRLLAPV 503
Cdd:pfam08159   1 DPRFKALFEDHDFAIDPTSPEFKKTNPM 28
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 56-214 6.19e-05

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 45.40  E-value: 6.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336  56 TSIRMSPDQQYILATGTYKpRVKCFEVSNlsikfERCfdaeVTTFEVISDDYSKMVFLQCDRYVeihaAHGRH------Y 129
Cdd:cd00200  97 SSVAFSPDGRILSSSSRDK-TIKVWDVET-----GKC----LTTLRGHTDWVNSVAFSPDGTFV----ASSSQdgtiklW 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 130 RLRIPRFGRDMKYHK---------PSCDMFIVGVGRDIFRL-NLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGT 199
Cdd:cd00200 163 DLRTGKCVATLTGHTgevnsvafsPDGEKLLSSSSDGTIKLwDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGT 242

                       170
                ....*....|....*
gi 19921336 200 VEAWDPRTKQRCSTL 214
Cdd:cd00200 243 IRVWDLRTGECVQTL 257
BTV_NS2 super family cl04557
Bluetongue virus non-structural protein NS2; This family includes NS2 proteins from other ...
 396-584 1.08e-03

Bluetongue virus non-structural protein NS2; This family includes NS2 proteins from other members of the Orbivirus genus. NS2 is a non-specific single-stranded RNA-binding protein that forms large homomultimers and accumulates in viral inclusion bodies of infected cells. Three RNA binding regions have been identified in Bluetongue virus serotype 17 at residues 2-11, 153-166 and 274-286. NS2 multimers also possess nucleotidyl phosphatase activity. The precise function of NS2 is not known, but it may be involved in the transport and condensation of viral mRNAs.


The actual alignment was detected with superfamily member pfam04514:

Pssm-ID: 282383  Cd Length: 349  Bit Score: 42.03  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   396 HGYFMDARL-YNKAKAVVEPFAFDRFRKDK----------------IRQEIESERKS--RLQIESKLPKvnkelalkimd 456
Cdd:pfam04514 111 NGVMVDAEIkYCKGMGIVQPYMRNDFDRNEmpdlpgvmrsnydireLRQKIKNERESapRLQVHSVAPR----------- 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   457 eqanpsnsakqrnvpsllEDSRFkamFENADFEVNKSAEEYRLLAPVLNRLDKSKAKELKkrvEVAHVAELHADEaqqRE 536
Cdd:pfam04514 180 ------------------EESRW---MDDDEAKVDDEAKEIVPGTSGLEKLREARSNVFK---EVEAVINWNLDE---RD 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 19921336   537 ESDNDEDLFGFEKSDGETKDDSGDEASSDDDDRREYVKE-MKQAYKQVK 584
Cdd:pfam04514 233 EGDRDERGDEEQVKTLSDDDDQGEDASDDEHPKTHITKEyIEKVAKQIK 281
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
150-303 1.35e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.61  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 150 FIVGVGRD--IFRLNLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGTVEAWDPRTKQRCSTLDVAMklpgvkefP 227
Cdd:COG2319 176 LLASGSDDgtVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS--------G 247

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921336 228 SVTALKF-RNGLHMGVGTASGHVLIYDIRAKQPLLVKNHLNRlPIKRLAFNP-AQNAVYSLDEATLKLWDEQTGKQIA 303
Cdd:COG2319 248 SVRSVAFsPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG-GVNSVAFSPdGKLLASGSDDGTVRLWDLATGKLLR 324
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 149-329 1.74e-07

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.49  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 149 MFIVGVGRDIFRLNLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGTVEAWDPRTKQRCSTldvamkLPGVKEFps 228
Cdd:cd00200  66 LASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT------LRGHTDW-- 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 229 VTALKF-RNGLHMGVGTASGHVLIYDIRAKQPLLV-KNHLNrlPIKRLAFNPAQNAVY--SLDeATLKLWDEQTGKQIA- 303
Cdd:cd00200 138 VNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTG--EVNSVAFSPDGEKLLssSSD-GTIKLWDLSTGKCLGt 214

                       170       180
                ....*....|....*....|....*.
gi 19921336 304 YVESTSSFNDFCTIPDTGMFFVAQED 329
Cdd:cd00200 215 LRGHENGVNSVAFSPDGYLLASGSED 240
NUC153 pfam08159
NUC153 domain; This small domain is found in a a novel nucleolar family.
 476-503 2.54e-07

NUC153 domain; This small domain is found in a a novel nucleolar family.


Pssm-ID: 462385 [Multi-domain]  Cd Length: 29  Bit Score: 46.94  E-value: 2.54e-07
                          10        20
                  ....*....|....*....|....*...
gi 19921336   476 DSRFKAMFENADFEVNKSAEEYRLLAPV 503
Cdd:pfam08159   1 DPRFKALFEDHDFAIDPTSPEFKKTNPM 28
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 56-214 6.19e-05

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 45.40  E-value: 6.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336  56 TSIRMSPDQQYILATGTYKpRVKCFEVSNlsikfERCfdaeVTTFEVISDDYSKMVFLQCDRYVeihaAHGRH------Y 129
Cdd:cd00200  97 SSVAFSPDGRILSSSSRDK-TIKVWDVET-----GKC----LTTLRGHTDWVNSVAFSPDGTFV----ASSSQdgtiklW 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 130 RLRIPRFGRDMKYHK---------PSCDMFIVGVGRDIFRL-NLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGT 199
Cdd:cd00200 163 DLRTGKCVATLTGHTgevnsvafsPDGEKLLSSSSDGTIKLwDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGT 242

                       170
                ....*....|....*
gi 19921336 200 VEAWDPRTKQRCSTL 214
Cdd:cd00200 243 IRVWDLRTGECVQTL 257
BTV_NS2 pfam04514
Bluetongue virus non-structural protein NS2; This family includes NS2 proteins from other ...
 396-584 1.08e-03

Bluetongue virus non-structural protein NS2; This family includes NS2 proteins from other members of the Orbivirus genus. NS2 is a non-specific single-stranded RNA-binding protein that forms large homomultimers and accumulates in viral inclusion bodies of infected cells. Three RNA binding regions have been identified in Bluetongue virus serotype 17 at residues 2-11, 153-166 and 274-286. NS2 multimers also possess nucleotidyl phosphatase activity. The precise function of NS2 is not known, but it may be involved in the transport and condensation of viral mRNAs.


Pssm-ID: 282383  Cd Length: 349  Bit Score: 42.03  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   396 HGYFMDARL-YNKAKAVVEPFAFDRFRKDK----------------IRQEIESERKS--RLQIESKLPKvnkelalkimd 456
Cdd:pfam04514 111 NGVMVDAEIkYCKGMGIVQPYMRNDFDRNEmpdlpgvmrsnydireLRQKIKNERESapRLQVHSVAPR----------- 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   457 eqanpsnsakqrnvpsllEDSRFkamFENADFEVNKSAEEYRLLAPVLNRLDKSKAKELKkrvEVAHVAELHADEaqqRE 536
Cdd:pfam04514 180 ------------------EESRW---MDDDEAKVDDEAKEIVPGTSGLEKLREARSNVFK---EVEAVINWNLDE---RD 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 19921336   537 ESDNDEDLFGFEKSDGETKDDSGDEASSDDDDRREYVKE-MKQAYKQVK 584
Cdd:pfam04514 233 EGDRDERGDEEQVKTLSDDDDQGEDASDDEHPKTHITKEyIEKVAKQIK 281
PTZ00121 PTZ00121
MAEBL; Provisional
 401-608 4.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   401 DARLYNKAKAVVEPFAFDRFRKDKIRQEIESERKS----------RLQIESKLPKVNKELALKIMDEQANPSNSAKQRNV 470
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAeeerkaeearKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE 1253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   471 PSLLEDSRfkaMFENADFEVNKSAEEYRLLAPVLNRLDKSKAKELKKRVEVAHVAEL--HADEAQQREESDNDEDlfGFE 548
Cdd:PTZ00121 1254 IRKFEEAR---MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAkkKAEEAKKADEAKKKAE--EAK 1328

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   549 KSDGETKDDSGDEASSDDDDRREYVKEMKQAYKQVKRQREEEEELEDDEQQPDEISDTAK 608
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
150-303 1.35e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.61  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 150 FIVGVGRD--IFRLNLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGTVEAWDPRTKQRCSTLDVAMklpgvkefP 227
Cdd:COG2319 176 LLASGSDDgtVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS--------G 247

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921336 228 SVTALKF-RNGLHMGVGTASGHVLIYDIRAKQPLLVKNHLNRlPIKRLAFNP-AQNAVYSLDEATLKLWDEQTGKQIA 303
Cdd:COG2319 248 SVRSVAFsPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG-GVNSVAFSPdGKLLASGSDDGTVRLWDLATGKLLR 324
WD40 COG2319
WD40 repeat [General function prediction only];
150-303 2.01e-08

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 57.23  E-value: 2.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 150 FIVGVGRD--IFRLNLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGTVEAWDPRTKQRCSTLDvamklpgvKEFP 227
Cdd:COG2319 218 LLASGSADgtVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLT--------GHSG 289

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921336 228 SVTALKF-RNGLHMGVGTASGHVLIYDIRAKQPLLV-KNHLNrlPIKRLAFNPAQNAVYSL-DEATLKLWDEQTGKQIA 303
Cdd:COG2319 290 GVNSVAFsPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTG--AVRSVAFSPDGKTLASGsDDGTVRLWDLATGELLR 366
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 149-329 1.74e-07

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 53.49  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 149 MFIVGVGRDIFRLNLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGTVEAWDPRTKQRCSTldvamkLPGVKEFps 228
Cdd:cd00200  66 LASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTT------LRGHTDW-- 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 229 VTALKF-RNGLHMGVGTASGHVLIYDIRAKQPLLV-KNHLNrlPIKRLAFNPAQNAVY--SLDeATLKLWDEQTGKQIA- 303
Cdd:cd00200 138 VNSVAFsPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTG--EVNSVAFSPDGEKLLssSSD-GTIKLWDLSTGKCLGt 214

                       170       180
                ....*....|....*....|....*.
gi 19921336 304 YVESTSSFNDFCTIPDTGMFFVAQED 329
Cdd:cd00200 215 LRGHENGVNSVAFSPDGYLLASGSED 240
NUC153 pfam08159
NUC153 domain; This small domain is found in a a novel nucleolar family.
 476-503 2.54e-07

NUC153 domain; This small domain is found in a a novel nucleolar family.


Pssm-ID: 462385 [Multi-domain]  Cd Length: 29  Bit Score: 46.94  E-value: 2.54e-07
                          10        20
                  ....*....|....*....|....*...
gi 19921336   476 DSRFKAMFENADFEVNKSAEEYRLLAPV 503
Cdd:pfam08159   1 DPRFKALFEDHDFAIDPTSPEFKKTNPM 28
WD40 COG2319
WD40 repeat [General function prediction only];
162-329 5.26e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 52.61  E-value: 5.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 162 NLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGTVEAWDPRTKQRCSTLDVAMKlpgvkefpSVTALKF-RNGLHM 240
Cdd:COG2319 148 DLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTG--------AVRSVAFsPDGKLL 219

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 241 GVGTASGHVLIYDIRAKQPLLVKNHLNRlPIKRLAFNPAQN--AVYSLDeATLKLWDEQTGKQIAYVES-TSSFNDFCTI 317
Cdd:COG2319 220 ASGSADGTVRLWDLATGKLLRTLTGHSG-SVRSVAFSPDGRllASGSAD-GTVRLWDLATGELLRTLTGhSGGVNSVAFS 297

                       170
                ....*....|..
gi 19921336 318 PDTGMFFVAQED 329
Cdd:COG2319 298 PDGKLLASGSDD 309
WD40 COG2319
WD40 repeat [General function prediction only];
162-303 1.15e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.45  E-value: 1.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 162 NLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGTVEAWDPRTKQRCSTldvamkLPGVKEfpSVTALKF-RNGLHM 240
Cdd:COG2319 106 DLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRT------LTGHSG--AVTSVAFsPDGKLL 177

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921336 241 GVGTASGHVLIYDIRAKQPLLV-KNHLNrlPIKRLAFNPAQN--AVYSLDEaTLKLWDEQTGKQIA 303
Cdd:COG2319 178 ASGSDDGTVRLWDLATGKLLRTlTGHTG--AVRSVAFSPDGKllASGSADG-TVRLWDLATGKLLR 240
WD40 COG2319
WD40 repeat [General function prediction only];
153-303 2.71e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 47.21  E-value: 2.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 153 GVGRDIFRLNLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGTVEAWDPRTKQRCSTLdvamklpgVKEFPSVTAL 232
Cdd:COG2319  55 AGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTL--------TGHTGAVRSV 126

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921336 233 KF-RNGLHMGVGTASGHVLIYDIRAKQPLLVKNHlNRLPIKRLAFNPA-QNAVYSLDEATLKLWDEQTGKQIA 303
Cdd:COG2319 127 AFsPDGKTLASGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDgKLLASGSDDGTVRLWDLATGKLLR 198
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 56-214 6.19e-05

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 45.40  E-value: 6.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336  56 TSIRMSPDQQYILATGTYKpRVKCFEVSNlsikfERCfdaeVTTFEVISDDYSKMVFLQCDRYVeihaAHGRH------Y 129
Cdd:cd00200  97 SSVAFSPDGRILSSSSRDK-TIKVWDVET-----GKC----LTTLRGHTDWVNSVAFSPDGTFV----ASSSQdgtiklW 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 130 RLRIPRFGRDMKYHK---------PSCDMFIVGVGRDIFRL-NLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGT 199
Cdd:cd00200 163 DLRTGKCVATLTGHTgevnsvafsPDGEKLLSSSSDGTIKLwDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGT 242

                       170
                ....*....|....*
gi 19921336 200 VEAWDPRTKQRCSTL 214
Cdd:cd00200 243 IRVWDLRTGECVQTL 257
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 162-329 1.05e-03

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 41.55  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 162 NLERGQFLQPFETDGSCLNACEVNPEHHLLVAGTKEGTVEAWDPRTKQRCSTLDvamklpGVKEfpSVTALKFRNGLHMG 241
Cdd:cd00200  37 DLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT------GHTS--YVSSVAFSPDGRIL 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336 242 VGTAS-GHVLIYDIRAKQPLLV-KNHLNrlPIKRLAFNPAQN-AVYSLDEATLKLWDEQTGKQIA-YVESTSSFNDFCTI 317
Cdd:cd00200 109 SSSSRdKTIKVWDVETGKCLTTlRGHTD--WVNSVAFSPDGTfVASSSQDGTIKLWDLRTGKCVAtLTGHTGEVNSVAFS 186

                       170
                ....*....|..
gi 19921336 318 PDTGMFFVAQED 329
Cdd:cd00200 187 PDGEKLLSSSSD 198
BTV_NS2 pfam04514
Bluetongue virus non-structural protein NS2; This family includes NS2 proteins from other ...
 396-584 1.08e-03

Bluetongue virus non-structural protein NS2; This family includes NS2 proteins from other members of the Orbivirus genus. NS2 is a non-specific single-stranded RNA-binding protein that forms large homomultimers and accumulates in viral inclusion bodies of infected cells. Three RNA binding regions have been identified in Bluetongue virus serotype 17 at residues 2-11, 153-166 and 274-286. NS2 multimers also possess nucleotidyl phosphatase activity. The precise function of NS2 is not known, but it may be involved in the transport and condensation of viral mRNAs.


Pssm-ID: 282383  Cd Length: 349  Bit Score: 42.03  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   396 HGYFMDARL-YNKAKAVVEPFAFDRFRKDK----------------IRQEIESERKS--RLQIESKLPKvnkelalkimd 456
Cdd:pfam04514 111 NGVMVDAEIkYCKGMGIVQPYMRNDFDRNEmpdlpgvmrsnydireLRQKIKNERESapRLQVHSVAPR----------- 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   457 eqanpsnsakqrnvpsllEDSRFkamFENADFEVNKSAEEYRLLAPVLNRLDKSKAKELKkrvEVAHVAELHADEaqqRE 536
Cdd:pfam04514 180 ------------------EESRW---MDDDEAKVDDEAKEIVPGTSGLEKLREARSNVFK---EVEAVINWNLDE---RD 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 19921336   537 ESDNDEDLFGFEKSDGETKDDSGDEASSDDDDRREYVKE-MKQAYKQVK 584
Cdd:pfam04514 233 EGDRDERGDEEQVKTLSDDDDQGEDASDDEHPKTHITKEyIEKVAKQIK 281
PTZ00121 PTZ00121
MAEBL; Provisional
 401-608 4.69e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   401 DARLYNKAKAVVEPFAFDRFRKDKIRQEIESERKS----------RLQIESKLPKVNKELALKIMDEQANPSNSAKQRNV 470
Cdd:PTZ00121 1174 DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAeeerkaeearKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE 1253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   471 PSLLEDSRfkaMFENADFEVNKSAEEYRLLAPVLNRLDKSKAKELKKRVEVAHVAEL--HADEAQQREESDNDEDlfGFE 548
Cdd:PTZ00121 1254 IRKFEEAR---MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAkkKAEEAKKADEAKKKAE--EAK 1328

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921336   549 KSDGETKDDSGDEASSDDDDRREYVKEMKQAYKQVKRQREEEEELEDDEQQPDEISDTAK 608
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
 
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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