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Conserved domains on  [gi|821595246|ref|NP_001295760|]
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WD repeat-containing protein 36 [Danio rerio]

Protein Classification

WD40 repeat and Utp21 domain-containing protein( domain architecture ID 13236737)

WD40 repeat and Utp21 domain-containing protein similar to human WD repeat-containing protein 36 and Schizosaccharomyces pombe U3 small nucleolar RNA-associated protein 21 (Utp21) homolog, which is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Utp21 pfam04192
Utp21 specific WD40 associated putative domain; Utp21 is a subunit of U3 snoRNP, which is ...
 692-892 4.62e-62

Utp21 specific WD40 associated putative domain; Utp21 is a subunit of U3 snoRNP, which is essential for synthesis of 18S rRNA.


:

Pssm-ID: 461219  Cd Length: 209  Bit Score: 208.93  E-value: 4.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  692 QLDEHLVTLSLLPDSRWKNLLHLDIIKKKNKPKEPPKVPKAAPFFIPTIPGLVPQFSLP-------NTPSEAQSKVVNLG 764
Cdd:pfam04192   2 QLSEDLVTLSLLPRSRWQTLLHLDLIKQRNKPKEAPKKPEKAPFFLPTLGGLVGDFASVeaqeeeeEEEEEERSRLLKLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  765 VLAQKSNFYIELENAIESNSYEEPVKLLRELGPSAIETELRALspDMGGDVGVMKSFLKMISCILKSKKDFDLAQAYLAL 844
Cdd:pfam04192  82 SLGFESEFTKLLREGSETGDYTPFLEYLKSLSPSAIDLEIRSL--NSGGPLEELVSFIRALTSRLKSNRDFELVQAYMAV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 821595246  845 FLKLHLRLISDEPE--LMEEAERVSAQLEETWMCIQTLLNQSICLLSYIK 892
Cdd:pfam04192 160 FLKLHGDVIHSNEEeeLREALEEWKSVQEEEWERLDELVGYCSGVVGFLR 209
WD40 COG2319
WD40 repeat [General function prediction only];
167-641 1.29e-38

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.91  E-value: 1.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 167 GSSQGSLQLWNIKSNKLLFTFSGWSAAVTVLQQTPAVDVVGVGLASGQIIIHNIKFDETLMKFQQDWGPITALSFRTDGH 246
Cdd:COG2319   12 ASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 247 PImASGSPIGHIGLWDLEEKKLVSQMRdAHTTAIAGLTFLQNEPLLITNGADNAIRVWifDVAggDGRLLRQRMGHSAPP 326
Cdd:COG2319   92 LL-ASASADGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSADGTVRLW--DLA--TGKLLRTLTGHSGAV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 327 TKIRhYDQSGLNILSAGQDGTLqsfstvherfnkslghgtlnkakakkkgvkydtaKLpsittfasetarqsdwdgiiac 406
Cdd:COG2319  166 TSVA-FSPDGKLLASGSDDGTV----------------------------------RL---------------------- 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 407 hrgflmttsWNYQKGSMGahkleperfnrnRSLNVHA---TAVDISSCGNFAVIALSSGHIDVYNMQSGLHRGHYgedKA 483
Cdd:COG2319  189 ---------WDLATGKLL------------RTLTGHTgavRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTL---TG 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 484 HEGPVRGVAVDALNQLTFSVGADHLLKIWKFKSKEHLHTHRLPAAPASSL-LHRDSGMLAIALDVFAIHILDVETRRIVR 562
Cdd:COG2319  245 HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVaFSPDGKLLASGSDDGTVRLWDLATGKLLR 324

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 563 KFSGHRGQINDMTFSPDGRWLITASMDCTIRTWDLPSGSLVDCFLVEAAAV-SVSLSPTGNFLASSHVDGlGVYLWSNNT 641
Cdd:COG2319  325 TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVtSVAFSPDGRTLASGSADG-TVRLWDLAT 403
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 95-132 6.95e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


:

Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.06  E-value: 6.95e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 821595246    95 SREVVHTYTGHQADVH--LLLPFGNHLISVDKDNVVIIWD 132
Cdd:smart00320   1 SGELLKTLKGHTGPVTsvAFSPDGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
Utp21 pfam04192
Utp21 specific WD40 associated putative domain; Utp21 is a subunit of U3 snoRNP, which is ...
 692-892 4.62e-62

Utp21 specific WD40 associated putative domain; Utp21 is a subunit of U3 snoRNP, which is essential for synthesis of 18S rRNA.


Pssm-ID: 461219  Cd Length: 209  Bit Score: 208.93  E-value: 4.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  692 QLDEHLVTLSLLPDSRWKNLLHLDIIKKKNKPKEPPKVPKAAPFFIPTIPGLVPQFSLP-------NTPSEAQSKVVNLG 764
Cdd:pfam04192   2 QLSEDLVTLSLLPRSRWQTLLHLDLIKQRNKPKEAPKKPEKAPFFLPTLGGLVGDFASVeaqeeeeEEEEEERSRLLKLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  765 VLAQKSNFYIELENAIESNSYEEPVKLLRELGPSAIETELRALspDMGGDVGVMKSFLKMISCILKSKKDFDLAQAYLAL 844
Cdd:pfam04192  82 SLGFESEFTKLLREGSETGDYTPFLEYLKSLSPSAIDLEIRSL--NSGGPLEELVSFIRALTSRLKSNRDFELVQAYMAV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 821595246  845 FLKLHLRLISDEPE--LMEEAERVSAQLEETWMCIQTLLNQSICLLSYIK 892
Cdd:pfam04192 160 FLKLHGDVIHSNEEeeLREALEEWKSVQEEEWERLDELVGYCSGVVGFLR 209
WD40 COG2319
WD40 repeat [General function prediction only];
167-641 1.29e-38

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.91  E-value: 1.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 167 GSSQGSLQLWNIKSNKLLFTFSGWSAAVTVLQQTPAVDVVGVGLASGQIIIHNIKFDETLMKFQQDWGPITALSFRTDGH 246
Cdd:COG2319   12 ASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 247 PImASGSPIGHIGLWDLEEKKLVSQMRdAHTTAIAGLTFLQNEPLLITNGADNAIRVWifDVAggDGRLLRQRMGHSAPP 326
Cdd:COG2319   92 LL-ASASADGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSADGTVRLW--DLA--TGKLLRTLTGHSGAV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 327 TKIRhYDQSGLNILSAGQDGTLqsfstvherfnkslghgtlnkakakkkgvkydtaKLpsittfasetarqsdwdgiiac 406
Cdd:COG2319  166 TSVA-FSPDGKLLASGSDDGTV----------------------------------RL---------------------- 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 407 hrgflmttsWNYQKGSMGahkleperfnrnRSLNVHA---TAVDISSCGNFAVIALSSGHIDVYNMQSGLHRGHYgedKA 483
Cdd:COG2319  189 ---------WDLATGKLL------------RTLTGHTgavRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTL---TG 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 484 HEGPVRGVAVDALNQLTFSVGADHLLKIWKFKSKEHLHTHRLPAAPASSL-LHRDSGMLAIALDVFAIHILDVETRRIVR 562
Cdd:COG2319  245 HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVaFSPDGKLLASGSDDGTVRLWDLATGKLLR 324

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 563 KFSGHRGQINDMTFSPDGRWLITASMDCTIRTWDLPSGSLVDCFLVEAAAV-SVSLSPTGNFLASSHVDGlGVYLWSNNT 641
Cdd:COG2319  325 TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVtSVAFSPDGRTLASGSADG-TVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 276-596 4.15e-26

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: 109.35  E-value: 4.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 276 HTTAIAGLTFLQNEPLLITNGADNAIRVWifDVAGGDgrLLRQRMGHSAPPTKIRHYDQSGLnILSAGQDGTLQSfstvh 355
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSGDGTIKVW--DLETGE--LLRTLKGHTGPVRDVAASADGTY-LASGSSDKTIRL----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 356 erfnkslghgtlnkakakkkgvkYDTAKLPSITTFASETarqsdwDGIIAC----HRGFLMTTSWNyqkgsmGAHKL-EP 430
Cdd:cd00200   78 -----------------------WDLETGECVRTLTGHT------SYVSSVafspDGRILSSSSRD------KTIKVwDV 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 431 ERFNRNRSLNVH---ATAVDISSCGNFAVIALSSGHIDVYNMQSGLHRGHYgedKAHEGPVRGVAVDALNQLTFSVGADH 507
Cdd:cd00200  123 ETGKCLTTLRGHtdwVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATL---TGHTGEVNSVAFSPDGEKLLSSSSDG 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 508 LLKIWKFKSKEHLHTHRLPAAPASSLLHRDSGMLAIALDV-FAIHILDVETRRIVRKFSGHRGQINDMTFSPDGRWLITA 586
Cdd:cd00200  200 TIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASG 279

                        330
                 ....*....|
gi 821595246 587 SMDCTIRTWD 596
Cdd:cd00200  280 SADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 557-596 1.39e-09

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 54.24  E-value: 1.39e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 821595246   557 TRRIVRKFSGHRGQINDMTFSPDGRWLITASMDCTIRTWD 596
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
558-596 3.17e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.12  E-value: 3.17e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 821595246  558 RRIVRKFSGHRGQINDMTFSPDGRWLITASMDCTIRTWD 596
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 95-132 6.95e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.06  E-value: 6.95e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 821595246    95 SREVVHTYTGHQADVH--LLLPFGNHLISVDKDNVVIIWD 132
Cdd:smart00320   1 SGELLKTLKGHTGPVTsvAFSPDGKYLASGSDDGTIKLWD 40
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 522-631 8.04e-04

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 42.33  E-value: 8.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  522 THRLPAAPASSL--LHRDSGMLAIA-LDVFAIHILDVETRRIVrkfsghrGQIN------DMTFSPDGRWLITASMDCTI 592
Cdd:TIGR03866  76 LHTLPSGPDPEQfaLHPNGKILYIAnEDDALVTVIDIETRKVL-------AQIDvgvepeGMAVSPDGKIVVNTSETTNM 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 821595246  593 RTW-DLPSGSLVDCFLVEAAAVSVSLSPTGNFL-ASSHVDG 631
Cdd:TIGR03866 149 AHWiDTATYEIVDNTLVDARPRFAEFTADGKELwVSSEIGG 189
 
Name Accession Description Interval E-value
Utp21 pfam04192
Utp21 specific WD40 associated putative domain; Utp21 is a subunit of U3 snoRNP, which is ...
 692-892 4.62e-62

Utp21 specific WD40 associated putative domain; Utp21 is a subunit of U3 snoRNP, which is essential for synthesis of 18S rRNA.


Pssm-ID: 461219  Cd Length: 209  Bit Score: 208.93  E-value: 4.62e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  692 QLDEHLVTLSLLPDSRWKNLLHLDIIKKKNKPKEPPKVPKAAPFFIPTIPGLVPQFSLP-------NTPSEAQSKVVNLG 764
Cdd:pfam04192   2 QLSEDLVTLSLLPRSRWQTLLHLDLIKQRNKPKEAPKKPEKAPFFLPTLGGLVGDFASVeaqeeeeEEEEEERSRLLKLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  765 VLAQKSNFYIELENAIESNSYEEPVKLLRELGPSAIETELRALspDMGGDVGVMKSFLKMISCILKSKKDFDLAQAYLAL 844
Cdd:pfam04192  82 SLGFESEFTKLLREGSETGDYTPFLEYLKSLSPSAIDLEIRSL--NSGGPLEELVSFIRALTSRLKSNRDFELVQAYMAV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 821595246  845 FLKLHLRLISDEPE--LMEEAERVSAQLEETWMCIQTLLNQSICLLSYIK 892
Cdd:pfam04192 160 FLKLHGDVIHSNEEeeLREALEEWKSVQEEEWERLDELVGYCSGVVGFLR 209
WD40 COG2319
WD40 repeat [General function prediction only];
167-641 1.29e-38

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 148.91  E-value: 1.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 167 GSSQGSLQLWNIKSNKLLFTFSGWSAAVTVLQQTPAVDVVGVGLASGQIIIHNIKFDETLMKFQQDWGPITALSFRTDGH 246
Cdd:COG2319   12 ASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 247 PImASGSPIGHIGLWDLEEKKLVSQMRdAHTTAIAGLTFLQNEPLLITNGADNAIRVWifDVAggDGRLLRQRMGHSAPP 326
Cdd:COG2319   92 LL-ASASADGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSADGTVRLW--DLA--TGKLLRTLTGHSGAV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 327 TKIRhYDQSGLNILSAGQDGTLqsfstvherfnkslghgtlnkakakkkgvkydtaKLpsittfasetarqsdwdgiiac 406
Cdd:COG2319  166 TSVA-FSPDGKLLASGSDDGTV----------------------------------RL---------------------- 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 407 hrgflmttsWNYQKGSMGahkleperfnrnRSLNVHA---TAVDISSCGNFAVIALSSGHIDVYNMQSGLHRGHYgedKA 483
Cdd:COG2319  189 ---------WDLATGKLL------------RTLTGHTgavRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTL---TG 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 484 HEGPVRGVAVDALNQLTFSVGADHLLKIWKFKSKEHLHTHRLPAAPASSL-LHRDSGMLAIALDVFAIHILDVETRRIVR 562
Cdd:COG2319  245 HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVaFSPDGKLLASGSDDGTVRLWDLATGKLLR 324

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 563 KFSGHRGQINDMTFSPDGRWLITASMDCTIRTWDLPSGSLVDCFLVEAAAV-SVSLSPTGNFLASSHVDGlGVYLWSNNT 641
Cdd:COG2319  325 TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVtSVAFSPDGRTLASGSADG-TVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
164-599 9.52e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 140.43  E-value: 9.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 164 ILFGSSQGSLQLWNIKSNKLLFTFSGWSAAVTVLQQTPAVDVVGVGLASGQIIIHNIKFDETLMKFQQDWGPITALSFRT 243
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 244 DGHPImASGSPIGHIGLWDLEEKKLVSQMRdAHTTAIAGLTFLQNEPLLITNGADNAIRVWifDVAggDGRLLRQRMGHS 323
Cdd:COG2319  131 DGKTL-ASGSADGTVRLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKLLASGSDDGTVRLW--DLA--TGKLLRTLTGHT 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 324 APPTKIRhYDQSGLNILSAGQDGTlqsfstvherfnkslghgtlnkakakkkgVK-YDTAKLPSITTFASETARqsdwdg 402
Cdd:COG2319  205 GAVRSVA-FSPDGKLLASGSADGT-----------------------------VRlWDLATGKLLRTLTGHSGS------ 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 403 iiachrgflmttswnyqkgsmgahkleperfnrnrslnvhATAVDISSCGNFAVIALSSGHIDVYNMQSGLHRGHYGedk 482
Cdd:COG2319  249 ----------------------------------------VRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLT--- 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 483 AHEGPVRGVAVDALNQLTFSVGADHLLKIWKFKSKEHLHTHRLPAAPASSL-LHRDSGMLAIALDVFAIHILDVETRRIV 561
Cdd:COG2319  286 GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVaFSPDGKTLASGSDDGTVRLWDLATGELL 365

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 821595246 562 RKFSGHRGQINDMTFSPDGRWLITASMDCTIRTWDLPS 599
Cdd:COG2319  366 RTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 276-596 4.15e-26

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: 109.35  E-value: 4.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 276 HTTAIAGLTFLQNEPLLITNGADNAIRVWifDVAGGDgrLLRQRMGHSAPPTKIRHYDQSGLnILSAGQDGTLQSfstvh 355
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSGDGTIKVW--DLETGE--LLRTLKGHTGPVRDVAASADGTY-LASGSSDKTIRL----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 356 erfnkslghgtlnkakakkkgvkYDTAKLPSITTFASETarqsdwDGIIAC----HRGFLMTTSWNyqkgsmGAHKL-EP 430
Cdd:cd00200   78 -----------------------WDLETGECVRTLTGHT------SYVSSVafspDGRILSSSSRD------KTIKVwDV 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 431 ERFNRNRSLNVH---ATAVDISSCGNFAVIALSSGHIDVYNMQSGLHRGHYgedKAHEGPVRGVAVDALNQLTFSVGADH 507
Cdd:cd00200  123 ETGKCLTTLRGHtdwVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATL---TGHTGEVNSVAFSPDGEKLLSSSSDG 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 508 LLKIWKFKSKEHLHTHRLPAAPASSLLHRDSGMLAIALDV-FAIHILDVETRRIVRKFSGHRGQINDMTFSPDGRWLITA 586
Cdd:cd00200  200 TIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEdGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASG 279

                        330
                 ....*....|
gi 821595246 587 SMDCTIRTWD 596
Cdd:cd00200  280 SADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 482-642 1.20e-25

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: 107.81  E-value: 1.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 482 KAHEGPVRGVAVDALNQLTFSVGADHLLKIWKFKSKEHLHT---HRLPAapASSLLHRDSGMLAIALDVFAIHILDVETR 558
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlkgHTGPV--RDVAASADGTYLASGSSDKTIRLWDLETG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 559 RIVRKFSGHRGQINDMTFSPDGRWLITASMDCTIRTWDLPSGSLVDCFL-VEAAAVSVSLSPTGNFLASSHVDGLgVYLW 637
Cdd:cd00200   84 ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgHTDWVNSVAFSPDGTFVASSSQDGT-IKLW 162


                 ....*
gi 821595246 638 SNNTL 642
Cdd:cd00200  163 DLRTG 167
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 99-364 9.82e-25

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: 105.11  E-value: 9.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  99 VHTYTGHQADVHLL--LPFGNHLISVDKDNVVIIWDVESEDtyLQISYDKASFEVSALMhPSTYLNKILFGSSQGSLQLW 176
Cdd:cd00200    2 RRTLKGHTGGVTCVafSPDGKLLATGSGDGTIKVWDLETGE--LLRTLKGHTGPVRDVA-ASADGTYLASGSSDKTIRLW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 177 NIKSNKLLFTFSGWSAAVTVLQQTPAVDVVGVGLASGQIIIHNIKFDETLMKFQQDWGPITALSFRTDGHpIMASGSPIG 256
Cdd:cd00200   79 DLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGT-FVASSSQDG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 257 HIGLWDLEEKKLVsQMRDAHTTAIAGLTFLQNEPLLITNGADNAIRVWifDVAggDGRLLRQRMGHSAPPTKIRhYDQSG 336
Cdd:cd00200  158 TIKLWDLRTGKCV-ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW--DLS--TGKCLGTLRGHENGVNSVA-FSPDG 231

                        250       260
                 ....*....|....*....|....*....
gi 821595246 337 LNILSAGQDGTLQSFSTVHERFNKSL-GH 364
Cdd:cd00200  232 YLLASGSEDGTIRVWDLRTGECVQTLsGH 260
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 416-638 5.60e-24

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: 103.18  E-value: 5.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 416 WNYQKGsmgahklEPERFNRNRSLNVhaTAVDISSCGNFAVIALSSGHIDVYNMQSGLHRGHYgedKAHEGPVRGVAVDA 495
Cdd:cd00200   36 WDLETG-------ELLRTLKGHTGPV--RDVAASADGTYLASGSSDKTIRLWDLETGECVRTL---TGHTSYVSSVAFSP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 496 LNQLTFSVGADHLLKIWKFKSKEHLHTHRLPAAPASSL-LHRDSGMLAIALDVFAIHILDVETRRIVRKFSGHRGQINDM 574
Cdd:cd00200  104 DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVaFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSV 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821595246 575 TFSPDGRWLITASMDCTIRTWDLPSGSLVDCFLV-EAAAVSVSLSPTGNFLASSHVDGlGVYLWS 638
Cdd:cd00200  184 AFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGhENGVNSVAFSPDGYLLASGSEDG-TIRVWD 247
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 97-348 8.51e-22

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: 96.64  E-value: 8.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  97 EVVHTYTGHQADVH--LLLPFGNHLISVDKDNVVIIWDVESEDtyLQISYDKASFEVSALM-HPStylNKILFGSS-QGS 172
Cdd:cd00200   42 ELLRTLKGHTGPVRdvAASADGTYLASGSSDKTIRLWDLETGE--CVRTLTGHTSYVSSVAfSPD---GRILSSSSrDKT 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 173 LQLWNIKSNKLLFTFSGWSAAVTVLQQTPAVDVVGVGLASGQIIIHNIKFDETLMKFQQDWGPITALSFRTDGHPIMASG 252
Cdd:cd00200  117 IKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSS 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 253 SPiGHIGLWDLEEKKLVSQMRdAHTTAIAGLTFLQNEPLLITNGADNAIRVWifDVAggDGRLLRQRMGHSAPPTKIRhY 332
Cdd:cd00200  197 SD-GTIKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGYLLASGSEDGTIRVW--DLR--TGECVQTLSGHTNSVTSLA-W 269

                        250
                 ....*....|....*.
gi 821595246 333 DQSGLNILSAGQDGTL 348
Cdd:cd00200  270 SPDGKRLASGSADGTI 285
WD40 COG2319
WD40 repeat [General function prediction only];
93-304 7.31e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 93.05  E-value: 7.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  93 ARSREVVHTYTGHQADVHLL--LPFGNHLISVDKDNVVIIWDVESEDtyLQISYDKASFEVSAL-MHPSTYLnkILFGSS 169
Cdd:COG2319  191 LATGKLLRTLTGHTGAVRSVafSPDGKLLASGSADGTVRLWDLATGK--LLRTLTGHSGSVRSVaFSPDGRL--LASGSA 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 170 QGSLQLWNIKSNKLLFTFSGWSAAVTVLQQTPAVDVVGVGLASGQIIIHNIKFDETLMKFQQDWGPITALSFRTDGHPIm 249
Cdd:COG2319  267 DGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTL- 345

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 821595246 250 ASGSPIGHIGLWDLEEKKLVSQMRdAHTTAIAGLTFLQNEPLLITNGADNAIRVW 304
Cdd:COG2319  346 ASGSDDGTVRLWDLATGELLRTLT-GHTGAVTSVAFSPDGRTLASGSADGTVRLW 399
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 44-304 1.64e-19

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: 89.70  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  44 TAVGQCFHTYNVKKLGIVavsnalpeDISSVTADCMLVYAAYGKLISAF-ARSREVVHTYTGHQADVH--LLLPFGNHLI 120
Cdd:cd00200   38 LETGELLRTLKGHTGPVR--------DVAASADGTYLASGSSDKTIRLWdLETGECVRTLTGHTSYVSsvAFSPDGRILS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 121 SVDKDNVVIIWDVESEDtyLQISYDKASFEVSAL-MHPStylNKILFGSSQ-GSLQLWNIKSNKLLFTFSGWSAAVTVLQ 198
Cdd:cd00200  110 SSSRDKTIKVWDVETGK--CLTTLRGHTDWVNSVaFSPD---GTFVASSSQdGTIKLWDLRTGKCVATLTGHTGEVNSVA 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 199 QTPAVDVVGVGLASGQIIIHNIKFDETLMKFQQDWGPITALSFRTDGHpIMASGSPIGHIGLWDLEEKKLVSQMRdAHTT 278
Cdd:cd00200  185 FSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGY-LLASGSEDGTIRVWDLRTGECVQTLS-GHTN 262

                        250       260
                 ....*....|....*....|....*.
gi 821595246 279 AIAGLTFLQNEPLLITNGADNAIRVW 304
Cdd:cd00200  263 SVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
492-638 2.75e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 72.64  E-value: 2.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 492 AVDALNQLTFSVGADHLLKIWKFKSKEHLHTHR-LPAAPASSLLHRDSGMLAIALDVFAIHILDVETRRIVRKFSGHRGQ 570
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLgLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821595246 571 INDMTFSPDGRWLITASMDCTIRTWDLPSGSLVDCFLVEAAAV-SVSLSPTGNFLASSHVDGlGVYLWS 638
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVrSVAFSPDGKTLASGSADG-TVRLWD 148
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 561-649 4.64e-12

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: 67.75  E-value: 4.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 561 VRKFSGHRGQINDMTFSPDGRWLITASMDCTIRTWDLPSGSLVDCFLVEAAAV-SVSLSPTGNFLASSHVDGLgVYLWSN 639
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVrDVAASADGTYLASGSSDKT-IRLWDL 80

                         90
                 ....*....|
gi 821595246 640 NTLCSLVSLR 649
Cdd:cd00200   81 ETGECVRTLT 90
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 557-596 1.39e-09

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 54.24  E-value: 1.39e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 821595246   557 TRRIVRKFSGHRGQINDMTFSPDGRWLITASMDCTIRTWD 596
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
558-596 3.17e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 53.12  E-value: 3.17e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 821595246  558 RRIVRKFSGHRGQINDMTFSPDGRWLITASMDCTIRTWD 596
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
421-624 2.44e-05

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 46.61  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 421 GSMGAHKLEPERFNRNRSLNVHATAVDISSCGNFAVIALSSGHIDVYNMQSGLHRGHYGEDKAHEGPVRGVAVDALNQLT 500
Cdd:COG3391    4 ASSLLVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 501 FSVGADHLLKIWKFKSKEHLHTHRLPAAPASSLLHRDSGMLAIA-LDVFAIHILDVETRRIVRKFSGHRGqINDMTFSPD 579
Cdd:COG3391   84 VANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVAdSGNGRVSVIDTATGKVVATIPVGAG-PHGIAVDPD 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 821595246 580 GRWLITASMDCT-----IRTWDLPSGSLVDCFLVEAAAVSVSLSPTGNFL 624
Cdd:COG3391  163 GKRLYVANSGSNtvsviVSVIDTATGKVVATIPVGGGPVGVAVSPDGRRL 212
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 515-625 4.16e-04

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 43.48  E-value: 4.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246 515 KSKEHLHTHR-LPAAPASSllhRDSG--MLAIALDVFAIHILDVETRRIVRKFSGHRGQINDMTFSPDGRWLITASMDCT 591
Cdd:cd20718    5 KSLEVLVPEReLPPVAYGI---WDLEnlMVVVERDAGSVLVIDGSTHEVLGRIDDGGAQVHVVVFSPDGRFAYVISRDGW 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 821595246 592 IRTWDLPSGSLVDCFLVEAAAVSVSLSPTGNFLA 625
Cdd:cd20718   82 LTKIDLYTLRPVASIRIGVNSRGIALSDDGKYVI 115
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 95-132 6.95e-04

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.06  E-value: 6.95e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 821595246    95 SREVVHTYTGHQADVH--LLLPFGNHLISVDKDNVVIIWD 132
Cdd:smart00320   1 SGELLKTLKGHTGPVTsvAFSPDGKYLASGSDDGTIKLWD 40
PQQ_ABC_repeats TIGR03866
PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family ...
 522-631 8.04e-04

PQQ-dependent catabolism-associated beta-propeller protein; Members of this protein family consist of seven repeats each of the YVTN family beta-propeller repeat (see TIGR02276). Members occur invariably as part of a transport operon that is associated with PQQ-dependent catabolism of alcohols such as phenylethanol.


Pssm-ID: 274824 [Multi-domain]  Cd Length: 310  Bit Score: 42.33  E-value: 8.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  522 THRLPAAPASSL--LHRDSGMLAIA-LDVFAIHILDVETRRIVrkfsghrGQIN------DMTFSPDGRWLITASMDCTI 592
Cdd:TIGR03866  76 LHTLPSGPDPEQfaLHPNGKILYIAnEDDALVTVIDIETRKVL-------AQIDvgvepeGMAVSPDGKIVVNTSETTNM 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 821595246  593 RTW-DLPSGSLVDCFLVEAAAVSVSLSPTGNFL-ASSHVDG 631
Cdd:TIGR03866 149 AHWiDTATYEIVDNTLVDARPRFAEFTADGKELwVSSEIGG 189
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 201-285 8.75e-03

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 36.49  E-value: 8.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821595246  201 PAVDVVGVGLASGQIIIHNIKFdetlmkfQQDWG--------PITALSFRTDGHpIMASGSPIGHIGLWDLEEKKLVSQm 272
Cdd:pfam12894   5 PTMDLIALATEDGELLLHRLNW-------QRVWTlspdkedlEVTSLAWRPDGK-LLAVGYSDGTVRLLDAENGKIVHH- 75

                          90
                  ....*....|...
gi 821595246  273 RDAHTTAIAGLTF 285
Cdd:pfam12894  76 FSAGSDLITCLGW 88
 
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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