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Conserved domains on  [gi|1002271039|ref|XP_015639843|]
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protein SUPPRESSOR OF PHYA-105 1 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00181 super family cl31831
protein SPA1-RELATED; Provisional
 348-1144 0e+00

protein SPA1-RELATED; Provisional


The actual alignment was detected with superfamily member PLN00181:

Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 627.88  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  348 QCEGTSLRELIKPARQTMSKFEKMHFFKQILDLVDKSHAQGFSLQHLRPSYFTISASNQVKYIGSygtqdlsapskldia 427
Cdd:PLN00181    60 ECEDVSLRQWLDNPDRSVDAFECFHVFRQIVEIVNAAHSQGIVVHNVRPSCFVMSSFNHVSFIES--------------- 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  428 tddifntkryldpkVESQDSNGDNASITKYQKVGEQgsiavrrpvhtfwanhrggNQSEGVDpgalwqgnssctvRERFK 507
Cdd:PLN00181   125 --------------ASCSDSGSDEDATTKSREIGSS-------------------RREEILS-------------ERRIE 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  508 AAEPFYGGSMPYAQrpsssgnqqsvfeLRMLEESWYRSPEEISQLKGILPSNIYSLGVLLFELFCCCETWEVHCAAMSDL 587
Cdd:PLN00181   159 KLEEVKKQPFPMKQ-------------ILAMEMSWYTSPEEDNGSSSNCASDVYRLGVLLFELFCPVSSREEKSRTMSSL 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  588 RHRILPPNFLSESPKEAGFCLWLLHPDPCSRPKARDILGCDLINEGRDlSLLDNKTPVAVNEEDTESGLLLGFLSQLKEE 667
Cdd:PLN00181   226 RHRVLPPQILLNWPKEASFCLWLLHPEPSCRPSMSELLQSEFINEPRE-NLEEREAAMELRDRIEEQELLLEFLFLIQQR 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  668 KEMHAAKLSADLASLETDIAEVEKRHSM--RMGFSLEDMdvLAGSNDL-SGASACALG---GASLSGLPPSLCRSSIYEE 741
Cdd:PLN00181   305 KQEAADKLQDTISLLSSDIDQVVKRQLVlqQKGSDVRSF--LASRKRIrQGAETLAAEeenDDNSSKLDDTLESTLLESS 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  742 RVMRNLEQLENAYYSMRSTIDTSEANIIKRVDN--DALRVRQNFHELHSDANAIDEQADPL------GW---FFDGLCKY 810
Cdd:PLN00181   383 RLMRNLKKLESVYFATRYRQIKAAAAAEKPLARyySALSENGRSSEKSSMSNPAKPPDFYIndsrqgGWidpFLEGLCKY 462

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  811 ARYSRFEVRGILKNADILNSPNVICSLSFDRDEEYFAAAGVSKKIKIFEFDALLNDRVDIHYPLIEMPSKSKLSCVCWNS 890
Cdd:PLN00181   463 LSFSKLRVKADLKQGDLLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFECESIIKDGRDIHYPVVELASRSKLSGICWNS 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  891 YIKNYLASTDYDGTVQLWDASSGQGFTQFTEHRKRAWSVSFSEVDPTKLASGSDDCCVKVWSINQKNCTDTIRNVANVCC 970
Cdd:PLN00181   543 YIKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICC 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  971 VQFSPYSSRMLAFGSADYKIYCYDLRNTRIPWCTISGHGKAVSYVRFLDPETLISASTDNTLKIWDLNQTnSSGLSTDAC 1050
Cdd:PLN00181   623 VQFPSESGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMS-ISGINETPL 701

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039 1051 SmTLSGHTNEKNFVGLSVHDGYITCGSENNEVFSYYKTFPMPITSHKFGSIDPITGQETnDDNQQFVSSVCWRGRSNMVV 1130
Cdd:PLN00181   702 H-SFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKAFPMPVLSYKFKTIDPVSGLEV-DDASQFISSVCWRGQSSTLV 779

                          810
                   ....*....|....
gi 1002271039 1131 AANSTGSIKVLELV 1144
Cdd:PLN00181   780 AANSTGNIKILEMV 793
 
Name Accession Description Interval E-value
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 348-1144 0e+00

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 627.88  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  348 QCEGTSLRELIKPARQTMSKFEKMHFFKQILDLVDKSHAQGFSLQHLRPSYFTISASNQVKYIGSygtqdlsapskldia 427
Cdd:PLN00181    60 ECEDVSLRQWLDNPDRSVDAFECFHVFRQIVEIVNAAHSQGIVVHNVRPSCFVMSSFNHVSFIES--------------- 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  428 tddifntkryldpkVESQDSNGDNASITKYQKVGEQgsiavrrpvhtfwanhrggNQSEGVDpgalwqgnssctvRERFK 507
Cdd:PLN00181   125 --------------ASCSDSGSDEDATTKSREIGSS-------------------RREEILS-------------ERRIE 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  508 AAEPFYGGSMPYAQrpsssgnqqsvfeLRMLEESWYRSPEEISQLKGILPSNIYSLGVLLFELFCCCETWEVHCAAMSDL 587
Cdd:PLN00181   159 KLEEVKKQPFPMKQ-------------ILAMEMSWYTSPEEDNGSSSNCASDVYRLGVLLFELFCPVSSREEKSRTMSSL 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  588 RHRILPPNFLSESPKEAGFCLWLLHPDPCSRPKARDILGCDLINEGRDlSLLDNKTPVAVNEEDTESGLLLGFLSQLKEE 667
Cdd:PLN00181   226 RHRVLPPQILLNWPKEASFCLWLLHPEPSCRPSMSELLQSEFINEPRE-NLEEREAAMELRDRIEEQELLLEFLFLIQQR 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  668 KEMHAAKLSADLASLETDIAEVEKRHSM--RMGFSLEDMdvLAGSNDL-SGASACALG---GASLSGLPPSLCRSSIYEE 741
Cdd:PLN00181   305 KQEAADKLQDTISLLSSDIDQVVKRQLVlqQKGSDVRSF--LASRKRIrQGAETLAAEeenDDNSSKLDDTLESTLLESS 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  742 RVMRNLEQLENAYYSMRSTIDTSEANIIKRVDN--DALRVRQNFHELHSDANAIDEQADPL------GW---FFDGLCKY 810
Cdd:PLN00181   383 RLMRNLKKLESVYFATRYRQIKAAAAAEKPLARyySALSENGRSSEKSSMSNPAKPPDFYIndsrqgGWidpFLEGLCKY 462

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  811 ARYSRFEVRGILKNADILNSPNVICSLSFDRDEEYFAAAGVSKKIKIFEFDALLNDRVDIHYPLIEMPSKSKLSCVCWNS 890
Cdd:PLN00181   463 LSFSKLRVKADLKQGDLLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFECESIIKDGRDIHYPVVELASRSKLSGICWNS 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  891 YIKNYLASTDYDGTVQLWDASSGQGFTQFTEHRKRAWSVSFSEVDPTKLASGSDDCCVKVWSINQKNCTDTIRNVANVCC 970
Cdd:PLN00181   543 YIKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICC 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  971 VQFSPYSSRMLAFGSADYKIYCYDLRNTRIPWCTISGHGKAVSYVRFLDPETLISASTDNTLKIWDLNQTnSSGLSTDAC 1050
Cdd:PLN00181   623 VQFPSESGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMS-ISGINETPL 701

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039 1051 SmTLSGHTNEKNFVGLSVHDGYITCGSENNEVFSYYKTFPMPITSHKFGSIDPITGQETnDDNQQFVSSVCWRGRSNMVV 1130
Cdd:PLN00181   702 H-SFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKAFPMPVLSYKFKTIDPVSGLEV-DDASQFISSVCWRGQSSTLV 779

                          810
                   ....*....|....
gi 1002271039 1131 AANSTGSIKVLELV 1144
Cdd:PLN00181   780 AANSTGNIKILEMV 793
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 831-1140 1.81e-36

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: 139.78  E-value: 1.81e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  831 PNVICSLSFDRDEEYFAAAGVSKKIKIFEFDALLNDRVD-IHYPLIempskSKLSCVCWNsyikNYLASTDYDGTVQLWD 909
Cdd:cd00200      9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkGHTGPV-----RDVAASADG----TYLASGSSDKTIRLWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  910 ASSGQGFTQFTEHRKRAWSVSFSeVDPTKLASGSDDCCVKVWSINQKNCTDTIRNVAN-VCCVQFSPySSRMLAFGSADY 988
Cdd:cd00200     80 LETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDwVNSVAFSP-DGTFVASSSQDG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  989 KIYCYDLRNTRipwC--TISGHGKAVSYVRFL-DPETLISASTDNTLKIWDlnqtnssgLSTDACSMTLSGHTNEKNFVG 1065
Cdd:cd00200    158 TIKLWDLRTGK---CvaTLTGHTGEVNSVAFSpDGEKLLSSSSDGTIKLWD--------LSTGKCLGTLRGHENGVNSVA 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002271039 1066 LSVHDGYITCGSENN--EVFSYYKTFPMP-ITSHkfgsidpitgqetnddnQQFVSSVCWRGRSNMVVAANSTGSIKV 1140
Cdd:cd00200    227 FSPDGYLLASGSEDGtiRVWDLRTGECVQtLSGH-----------------TNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 COG2319
WD40 repeat [General function prediction only];
895-1140 4.07e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 133.11  E-value: 4.07e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  895 YLASTDYDGTVQLWDASSGQGFTQFTEHRKRAWSVSFSEvDPTKLASGSDDCCVKVWSINQKNCTDTIR-NVANVCCVQF 973
Cdd:COG2319    176 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGKLLRTLTgHSGSVRSVAF 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  974 SPySSRMLAFGSADYKIYCYDLRNTRIPWcTISGHGKAVSYVRFL-DPETLISASTDNTLKIWDlnqtnssgLSTDACSM 1052
Cdd:COG2319    255 SP-DGRLLASGSADGTVRLWDLATGELLR-TLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLWD--------LATGKLLR 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039 1053 TLSGHTNEKNFVGLSVHDGYITCGSENNEVFSYyktfpmpitshkfgsiDPITGQETN--DDNQQFVSSVCWRGRSNMVV 1130
Cdd:COG2319    325 TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLW----------------DLATGELLRtlTGHTGAVTSVAFSPDGRTLA 388

                          250
                   ....*....|
gi 1002271039 1131 AANSTGSIKV 1140
Cdd:COG2319    389 SGSADGTVRL 398
Pkinase pfam00069
Protein kinase domain;
541-625 1.43e-07

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 53.40  E-value: 1.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  541 SWYRSPEEISQlKGILP-SNIYSLGVLLFELFCCCETW------EVHCAAMSDLRHRILPPNFLSESPKEagFCLWLLHP 613
Cdd:pfam00069  124 PWYMAPEVLGG-NPYGPkVDVWSLGCILYELLTGKPPFpgingnEIYELIIDQPYAFPELPSNLSEEAKD--LLKKLLKK 200

                           90
                   ....*....|..
gi 1002271039  614 DPCSRPKARDIL 625
Cdd:pfam00069  201 DPSKRLTATQAL 212
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 542-625 3.42e-06

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 49.84  E-value: 3.42e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039   542 WYRSPEEISQLKGILPSNIYSLGVLLFELFCCC-------ETWEVHCAAMSDLRHRILPPNFLSESPKEagFCLWLLHPD 614
Cdd:smart00220  161 EYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKppfpgddQLLELFKKIGKPKPPFPPPEWDISPEAKD--LIRKLLVKD 238

                            90
                    ....*....|.
gi 1002271039   615 PCSRPKARDIL 625
Cdd:smart00220  239 PEKRLTAEEAL 249
 
Name Accession Description Interval E-value
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 348-1144 0e+00

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 627.88  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  348 QCEGTSLRELIKPARQTMSKFEKMHFFKQILDLVDKSHAQGFSLQHLRPSYFTISASNQVKYIGSygtqdlsapskldia 427
Cdd:PLN00181    60 ECEDVSLRQWLDNPDRSVDAFECFHVFRQIVEIVNAAHSQGIVVHNVRPSCFVMSSFNHVSFIES--------------- 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  428 tddifntkryldpkVESQDSNGDNASITKYQKVGEQgsiavrrpvhtfwanhrggNQSEGVDpgalwqgnssctvRERFK 507
Cdd:PLN00181   125 --------------ASCSDSGSDEDATTKSREIGSS-------------------RREEILS-------------ERRIE 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  508 AAEPFYGGSMPYAQrpsssgnqqsvfeLRMLEESWYRSPEEISQLKGILPSNIYSLGVLLFELFCCCETWEVHCAAMSDL 587
Cdd:PLN00181   159 KLEEVKKQPFPMKQ-------------ILAMEMSWYTSPEEDNGSSSNCASDVYRLGVLLFELFCPVSSREEKSRTMSSL 225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  588 RHRILPPNFLSESPKEAGFCLWLLHPDPCSRPKARDILGCDLINEGRDlSLLDNKTPVAVNEEDTESGLLLGFLSQLKEE 667
Cdd:PLN00181   226 RHRVLPPQILLNWPKEASFCLWLLHPEPSCRPSMSELLQSEFINEPRE-NLEEREAAMELRDRIEEQELLLEFLFLIQQR 304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  668 KEMHAAKLSADLASLETDIAEVEKRHSM--RMGFSLEDMdvLAGSNDL-SGASACALG---GASLSGLPPSLCRSSIYEE 741
Cdd:PLN00181   305 KQEAADKLQDTISLLSSDIDQVVKRQLVlqQKGSDVRSF--LASRKRIrQGAETLAAEeenDDNSSKLDDTLESTLLESS 382

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  742 RVMRNLEQLENAYYSMRSTIDTSEANIIKRVDN--DALRVRQNFHELHSDANAIDEQADPL------GW---FFDGLCKY 810
Cdd:PLN00181   383 RLMRNLKKLESVYFATRYRQIKAAAAAEKPLARyySALSENGRSSEKSSMSNPAKPPDFYIndsrqgGWidpFLEGLCKY 462

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  811 ARYSRFEVRGILKNADILNSPNVICSLSFDRDEEYFAAAGVSKKIKIFEFDALLNDRVDIHYPLIEMPSKSKLSCVCWNS 890
Cdd:PLN00181   463 LSFSKLRVKADLKQGDLLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFECESIIKDGRDIHYPVVELASRSKLSGICWNS 542

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  891 YIKNYLASTDYDGTVQLWDASSGQGFTQFTEHRKRAWSVSFSEVDPTKLASGSDDCCVKVWSINQKNCTDTIRNVANVCC 970
Cdd:PLN00181   543 YIKSQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICC 622

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  971 VQFSPYSSRMLAFGSADYKIYCYDLRNTRIPWCTISGHGKAVSYVRFLDPETLISASTDNTLKIWDLNQTnSSGLSTDAC 1050
Cdd:PLN00181   623 VQFPSESGRSLAFGSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFVDSSTLVSSSTDNTLKLWDLSMS-ISGINETPL 701

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039 1051 SmTLSGHTNEKNFVGLSVHDGYITCGSENNEVFSYYKTFPMPITSHKFGSIDPITGQETnDDNQQFVSSVCWRGRSNMVV 1130
Cdd:PLN00181   702 H-SFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKAFPMPVLSYKFKTIDPVSGLEV-DDASQFISSVCWRGQSSTLV 779

                          810
                   ....*....|....
gi 1002271039 1131 AANSTGSIKVLELV 1144
Cdd:PLN00181   780 AANSTGNIKILEMV 793
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 831-1140 1.81e-36

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: 139.78  E-value: 1.81e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  831 PNVICSLSFDRDEEYFAAAGVSKKIKIFEFDALLNDRVD-IHYPLIempskSKLSCVCWNsyikNYLASTDYDGTVQLWD 909
Cdd:cd00200      9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLkGHTGPV-----RDVAASADG----TYLASGSSDKTIRLWD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  910 ASSGQGFTQFTEHRKRAWSVSFSeVDPTKLASGSDDCCVKVWSINQKNCTDTIRNVAN-VCCVQFSPySSRMLAFGSADY 988
Cdd:cd00200     80 LETGECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDwVNSVAFSP-DGTFVASSSQDG 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  989 KIYCYDLRNTRipwC--TISGHGKAVSYVRFL-DPETLISASTDNTLKIWDlnqtnssgLSTDACSMTLSGHTNEKNFVG 1065
Cdd:cd00200    158 TIKLWDLRTGK---CvaTLTGHTGEVNSVAFSpDGEKLLSSSSDGTIKLWD--------LSTGKCLGTLRGHENGVNSVA 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002271039 1066 LSVHDGYITCGSENN--EVFSYYKTFPMP-ITSHkfgsidpitgqetnddnQQFVSSVCWRGRSNMVVAANSTGSIKV 1140
Cdd:cd00200    227 FSPDGYLLASGSEDGtiRVWDLRTGECVQtLSGH-----------------TNSVTSLAWSPDGKRLASGSADGTIRI 287
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 834-1036 3.36e-34

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: 133.23  E-value: 3.36e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  834 ICSLSFDRDEEYFAAAGVSKKIKIFEFDALlndrvdihYPLIEMPSKSK-LSCVCWNSYiKNYLASTDYDGTVQLWDASS 912
Cdd:cd00200     96 VSSVAFSPDGRILSSSSRDKTIKVWDVETG--------KCLTTLRGHTDwVNSVAFSPD-GTFVASSSQDGTIKLWDLRT 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  913 GQGFTQFTEHRKRAWSVSFSEvDPTKLASGSDDCCVKVWSINQKNCTDTIR-NVANVCCVQFSPySSRMLAFGSADYKIY 991
Cdd:cd00200    167 GKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGKCLGTLRgHENGVNSVAFSP-DGYLLASGSEDGTIR 244

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1002271039  992 CYDLRNTRiPWCTISGHGKAVSYVRFL-DPETLISASTDNTLKIWD 1036
Cdd:cd00200    245 VWDLRTGE-CVQTLSGHTNSVTSLAWSpDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
895-1140 4.07e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 133.11  E-value: 4.07e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  895 YLASTDYDGTVQLWDASSGQGFTQFTEHRKRAWSVSFSEvDPTKLASGSDDCCVKVWSINQKNCTDTIR-NVANVCCVQF 973
Cdd:COG2319    176 LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGTVRLWDLATGKLLRTLTgHSGSVRSVAF 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  974 SPySSRMLAFGSADYKIYCYDLRNTRIPWcTISGHGKAVSYVRFL-DPETLISASTDNTLKIWDlnqtnssgLSTDACSM 1052
Cdd:COG2319    255 SP-DGRLLASGSADGTVRLWDLATGELLR-TLTGHSGGVNSVAFSpDGKLLASGSDDGTVRLWD--------LATGKLLR 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039 1053 TLSGHTNEKNFVGLSVHDGYITCGSENNEVFSYyktfpmpitshkfgsiDPITGQETN--DDNQQFVSSVCWRGRSNMVV 1130
Cdd:COG2319    325 TLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLW----------------DLATGELLRtlTGHTGAVTSVAFSPDGRTLA 388

                          250
                   ....*....|
gi 1002271039 1131 AANSTGSIKV 1140
Cdd:COG2319    389 SGSADGTVRL 398
WD40 COG2319
WD40 repeat [General function prediction only];
895-1143 3.94e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 127.33  E-value: 3.94e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  895 YLASTDYDGTVQLWDASSGQGFTQFTEHRKRAWSVSFSEvDPTKLASGSDDCCVKVWSINQKNCTDTIRNVAN-VCCVQF 973
Cdd:COG2319     92 LLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGTVRLWDLATGKLLRTLTGHSGaVTSVAF 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  974 SPySSRMLAFGSADYKIYCYDLRNTRIPWcTISGHGKAVSYVRFL-DPETLISASTDNTLKIWDLNqtnssglsTDACSM 1052
Cdd:COG2319    171 SP-DGKLLASGSDDGTVRLWDLATGKLLR-TLTGHTGAVRSVAFSpDGKLLASGSADGTVRLWDLA--------TGKLLR 240

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039 1053 TLSGHTNEKNFVGLSvHDG-YITCGSENNEVFSYyktfpmpitshkfgsiDPITGQE--TNDDNQQFVSSVCWRGRSNMV 1129
Cdd:COG2319    241 TLTGHSGSVRSVAFS-PDGrLLASGSADGTVRLW----------------DLATGELlrTLTGHSGGVNSVAFSPDGKLL 303

                          250
                   ....*....|....
gi 1002271039 1130 VAANSTGSIKVLEL 1143
Cdd:COG2319    304 ASGSDDGTVRLWDL 317
WD40 COG2319
WD40 repeat [General function prediction only];
836-1082 3.98e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 127.33  E-value: 3.98e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  836 SLSFDRDEEYFAAAGVSKKIKIFEFDAL-LNDRVDIHypliempsKSKLSCVCW--NSyikNYLASTDYDGTVQLWDASS 912
Cdd:COG2319    167 SVAFSPDGKLLASGSDDGTVRLWDLATGkLLRTLTGH--------TGAVRSVAFspDG---KLLASGSADGTVRLWDLAT 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  913 GQGFTQFTEHRKRAWSVSFSEvDPTKLASGSDDCCVKVWSINQKNCTDTIR-NVANVCCVQFSPySSRMLAFGSADYKIY 991
Cdd:COG2319    236 GKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSP-DGKLLASGSDDGTVR 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  992 CYDLRNTRIPWcTISGHGKAVSYVRFL-DPETLISASTDNTLKIWDLNqtnssglsTDACSMTLSGHTNEKNFVGLSVHD 1070
Cdd:COG2319    314 LWDLATGKLLR-TLTGHTGAVRSVAFSpDGKTLASGSDDGTVRLWDLA--------TGELLRTLTGHTGAVTSVAFSPDG 384

                          250
                   ....*....|..
gi 1002271039 1071 GYITCGSENNEV 1082
Cdd:COG2319    385 RTLASGSADGTV 396
WD40 COG2319
WD40 repeat [General function prediction only];
895-1140 4.41e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 126.95  E-value: 4.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  895 YLASTDYDGTVQLWDASSGQGFTQFTEHRKRAWSVSFSeVDPTKLASGSDDCCVKVWSINQKNCTDTIRNVAN-VCCVQF 973
Cdd:COG2319    134 TLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGaVRSVAF 212

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  974 SPySSRMLAFGSADYKIYCYDLRNTRIPWcTISGHGKAVSYVRFL-DPETLISASTDNTLKIWDLNqtnssglsTDACSM 1052
Cdd:COG2319    213 SP-DGKLLASGSADGTVRLWDLATGKLLR-TLTGHSGSVRSVAFSpDGRLLASGSADGTVRLWDLA--------TGELLR 282

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039 1053 TLSGHTNEKNFVGLSvHDG-YITCGSENNEVFSYyktfpmpitshkfgsiDPITGQE--TNDDNQQFVSSVCWRGRSNMV 1129
Cdd:COG2319    283 TLTGHSGGVNSVAFS-PDGkLLASGSDDGTVRLW----------------DLATGKLlrTLTGHTGAVRSVAFSPDGKTL 345

                          250
                   ....*....|.
gi 1002271039 1130 VAANSTGSIKV 1140
Cdd:COG2319    346 ASGSDDGTVRL 356
WD40 COG2319
WD40 repeat [General function prediction only];
831-1038 5.77e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 120.79  E-value: 5.77e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  831 PNVICSLSFDRDEEYFAAAGVSKKIKIFEfdalLNDRVDIHypLIEMPSKSkLSCVCWNSYIKnYLASTDYDGTVQLWDA 910
Cdd:COG2319    204 TGAVRSVAFSPDGKLLASGSADGTVRLWD----LATGKLLR--TLTGHSGS-VRSVAFSPDGR-LLASGSADGTVRLWDL 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  911 SSGQGFTQFTEHRKRAWSVSFSEvDPTKLASGSDDCCVKVWSINQKNCTDTIR-NVANVCCVQFSPySSRMLAFGSADYK 989
Cdd:COG2319    276 ATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSP-DGKTLASGSDDGT 353

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1002271039  990 IYCYDLrNTRIPWCTISGHGKAVSYVRFL-DPETLISASTDNTLKIWDLN 1038
Cdd:COG2319    354 VRLWDL-ATGELLRTLTGHTGAVTSVAFSpDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
896-1140 3.91e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 100.37  E-value: 3.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  896 LASTDYDGTVQLWDASSGQGFTQFTEHRKRAWSVSFSeVDPTKLASGSDDCCVKVWSINQKNCTDTIRNVAN-VCCVQFS 974
Cdd:COG2319     51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFS-PDGRLLASASADGTVRLWDLATGLLLRTLTGHTGaVRSVAFS 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  975 PySSRMLAFGSADYKIYCYDLRNTRIPWcTISGHGKAVSYVRFL-DPETLISASTDNTLKIWDlnqtnssgLSTDACSMT 1053
Cdd:COG2319    130 P-DGKTLASGSADGTVRLWDLATGKLLR-TLTGHSGAVTSVAFSpDGKLLASGSDDGTVRLWD--------LATGKLLRT 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039 1054 LSGHTNEKNFVGLSvHDG-YITCGSENNEVFSYyktfpmpitshkfgsiDPITGQE--TNDDNQQFVSSVCWRGRSNMVV 1130
Cdd:COG2319    200 LTGHTGAVRSVAFS-PDGkLLASGSADGTVRLW----------------DLATGKLlrTLTGHSGSVRSVAFSPDGRLLA 262

                          250
                   ....*....|
gi 1002271039 1131 AANSTGSIKV 1140
Cdd:COG2319    263 SGSADGTVRL 272
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 543-625 4.64e-14

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 73.87  E-value: 4.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  543 YRSPEeisQLKGIL---PSNIYSLGVLLFELFCCCETWEVHCAAMSDLRHRILPPNFLSESPKEAGFCLWLLHPDPCSRP 619
Cdd:cd13996    188 YASPE---QLDGENyneKADIYSLGIILFEMLHPFKTAMERSTILTDLRNGILPESFKAKHPKEADLIQSLLSKNPEERP 264


                   ....*.
gi 1002271039  620 KARDIL 625
Cdd:cd13996    265 SAEQLL 270
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1003-1143 2.64e-10

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: 62.74  E-value: 2.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039 1003 CTISGHGKAVSYVRFL-DPETLISASTDNTLKIWDLNqtnssglsTDACSMTLSGHTNEKNFVGLSVHDGYITCGSENNE 1081
Cdd:cd00200      3 RTLKGHTGGVTCVAFSpDGKLLATGSGDGTIKVWDLE--------TGELLRTLKGHTGPVRDVAASADGTYLASGSSDKT 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002271039 1082 VFSYyktfpmpitshkfgsiDPITGQETND--DNQQFVSSVCWRGRSNMVVAANSTGSIKVLEL 1143
Cdd:cd00200     75 IRLW----------------DLETGECVRTltGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV 122
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 543-625 6.09e-08

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 55.19  E-value: 6.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  543 YRSPEEISQLKGILPSNIYSLGVLLFELFCCCETWEVHCAAMSDLRHRILPPNFLSESPKEAGFCLWLLHPDPCSRPKAR 622
Cdd:cd14047    182 YMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSKFWTDLRNGILPDIFDKRYKIEKTIIKKMLSKKPEDRPNAS 261


                   ...
gi 1002271039  623 DIL 625
Cdd:cd14047    262 EIL 264
Pkinase pfam00069
Protein kinase domain;
541-625 1.43e-07

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 53.40  E-value: 1.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  541 SWYRSPEEISQlKGILP-SNIYSLGVLLFELFCCCETW------EVHCAAMSDLRHRILPPNFLSESPKEagFCLWLLHP 613
Cdd:pfam00069  124 PWYMAPEVLGG-NPYGPkVDVWSLGCILYELLTGKPPFpgingnEIYELIIDQPYAFPELPSNLSEEAKD--LLKKLLKK 200

                           90
                   ....*....|..
gi 1002271039  614 DPCSRPKARDIL 625
Cdd:pfam00069  201 DPSKRLTATQAL 212
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
 518-625 3.15e-07

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 53.14  E-value: 3.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  518 PYAQRPSSSGNQQSvfelrMLEESWYRSPEEISQLKGIL--PSNIYSLGVLLFELfcccetWEVHCAAMSdlRHRIL--- 592
Cdd:cd14046    168 STSAALGSSGDLTG-----NVGTALYVAPEVQSGTKSTYneKVDMYSLGIIFFEM------CYPFSTGME--RVQILtal 234

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1002271039  593 -------PPNFL-SESPKEAGFCLWLLHPDPCSRPKARDIL 625
Cdd:cd14046    235 rsvsiefPPDFDdNKHSKQAKLIRWLLNHDPAKRPSAQELL 275
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 543-624 6.75e-07

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 52.18  E-value: 6.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  543 YRSPEEISQLKGILPSNIYSLGVLLFELFCCCETWEVHCAAMSDLRHRILPPNFLSESPKEAGFCLWLLHPDPCSRPKAR 622
Cdd:cd14048    196 YMSPEQIHGNQYSEKVDIFALGLILFELIYSFSTQMERIRTLTDVRKLKFPALFTNKYPEERDMVQQMLSPSPSERPEAH 275


                   ..
gi 1002271039  623 DI 624
Cdd:cd14048    276 EV 277
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 542-625 3.42e-06

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 49.84  E-value: 3.42e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039   542 WYRSPEEISQLKGILPSNIYSLGVLLFELFCCC-------ETWEVHCAAMSDLRHRILPPNFLSESPKEagFCLWLLHPD 614
Cdd:smart00220  161 EYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKppfpgddQLLELFKKIGKPKPPFPPPEWDISPEAKD--LIRKLLVKD 238

                            90
                    ....*....|.
gi 1002271039   615 PCSRPKARDIL 625
Cdd:smart00220  239 PEKRLTAEEAL 249
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
 543-625 1.53e-05

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 47.69  E-value: 1.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  543 YRSPEeisQLKGIL--PSNIYSLGVLLFELFCCCE------TWEvhcaamsDLRHRILPPNFLSESPKEAGFCL-WLLHP 613
Cdd:cd14050    165 YMAPE---LLQGSFtkAADIFSLGITILELACNLElpsggdGWH-------QLRQGYLPEEFTAGLSPELRSIIkLMMDP 234

                           90
                   ....*....|..
gi 1002271039  614 DPCSRPKARDIL 625
Cdd:cd14050    235 DPERRPTAEDLL 246
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 543-625 1.80e-05

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 47.89  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  543 YRSPEEISQLKGILPSNIYSLGVLLFELFCCCETWEVHCAAMSDLRHRILPPNFLSESPKEAGFCLWLLHPDPCSRPKAR 622
Cdd:cd14049    199 YAAPEQLEGSHYDFKSDMYSIGVILLELFQPFGTEMERAEVLTQLRNGQIPKSLCKRWPVQAKYIKLLTSTEPSERPSAS 278


                   ...
gi 1002271039  623 DIL 625
Cdd:cd14049    279 QLL 281
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
 537-626 2.44e-04

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 44.30  E-value: 2.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  537 MLEESWYRSPEEIsqlkgilPSNIYSLGVLLFELfcCCETWEVHCAAMSDLRHRIL-------PPNFLSESPKeagFCLW 609
Cdd:cd08530    168 AAPEVWKGRPYDY-------KSDIWSLGCLLYEM--ATFRPPFEARTMQELRYKVCrgkfppiPPVYSQDLQQ---IIRS 235

                           90
                   ....*....|....*..
gi 1002271039  610 LLHPDPCSRPKARDILG 626
Cdd:cd08530    236 LLQVNPKKRPSCDKLLQ 252
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 998-1036 3.42e-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: 39.22  E-value: 3.42e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1002271039   998 TRIPWCTISGHGKAVSYVRFL-DPETLISASTDNTLKIWD 1036
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSpDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1004-1036 7.10e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.10  E-value: 7.10e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1002271039 1004 TISGHGKAVSYVRFL-DPETLISASTDNTLKIWD 1036
Cdd:pfam00400    6 TLEGHTGSVTSLAFSpDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 912-952 7.80e-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: 7.80e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1002271039   912 SGQGFTQFTEHRKRAWSVSFSEvDPTKLASGSDDCCVKVWS 952
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSP-DGKYLASGSDDGTIKLWD 40
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 542-625 1.33e-03

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 41.84  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  542 WYRSPEEISQLKGILPS-NIYSLGVLLFELFCCCETWEVHC-----AAMsdlrHRIL-PPNFLSespkeagFCLWLLHPD 614
Cdd:cd05118    165 WYRAPEVLLGAKPYGSSiDIWSLGCILAELLTGRPLFPGDSevdqlAKI----VRLLgTPEALD-------LLSKMLKYD 233

                           90
                   ....*....|.
gi 1002271039  615 PCSRPKARDIL 625
Cdd:cd05118    234 PAKRITASQAL 244
WD40 pfam00400
WD domain, G-beta repeat;
919-952 1.47e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 1.47e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1002271039  919 FTEHRKRAWSVSFSEvDPTKLASGSDDCCVKVWS 952
Cdd:pfam00400    7 LEGHTGSVTSLAFSP-DGKLLASGSDDGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 929-1036 5.26e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 40.65  E-value: 5.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  929 VSFSEVDPTKLASGSDDCCVKVWSIN----QKNCTDTIRNV----ANVCCVQFSPYSSRMLAFGSADYKIYCYDLrNTRI 1000
Cdd:PTZ00421    81 VAFNPFDPQKLFTASEDGTIMGWGIPeeglTQNISDPIVHLqghtKKVGIVSFHPSAMNVLASAGADMVVNVWDV-ERGK 159

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1002271039 1001 PWCTISGHGKAVSYVRF-LDPETLISASTDNTLKIWD 1036
Cdd:PTZ00421   160 AVEVIKCHSDQITSLEWnLDGSLLCTTSKDKKLNIID 196
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
 543-619 5.46e-03

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 39.96  E-value: 5.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  543 YRSPEEISQLKGI---LPSNIYSLGVLLFEL-FCCCETWEVHCAAMSDLRHRIlpPNFLSESPKEAGFCLWLLHPDPCSR 618
Cdd:cd14037    185 YRAPEMIDLYRGKpitEKSDIWALGCLLYKLcFYTTPFEESGQLAILNGNFTF--PDNSRYSKRLHKLIRYMLEEDPEKR 262


                   .
gi 1002271039  619 P 619
Cdd:cd14037    263 P 263
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
 543-626 6.13e-03

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 39.98  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002271039  543 YRSPEEISQLK--GiLPSNIYSLGVLLFELFCCCETWEVhcAAMSDLR-----------HRILPPNFLSESPKEAGFCLW 609
Cdd:cd13994    168 YMAPEVFTSGSydG-RAVDVWSCGIVLFALFTGRFPWRS--AKKSDSAykayeksgdftNGPYEPIENLLPSECRRLIYR 244

                           90
                   ....*....|....*..
gi 1002271039  610 LLHPDPCSRPKARDILG 626
Cdd:cd13994    245 MLHPDPEKRITIDEALN 261
 
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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