ID W2HLG1_PHYPR Unreviewed; 2580 AA.
AC W2HLG1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=AGC/PKC protein kinase {ECO:0000313|EMBL:ETK95964.1};
GN ORFNames=L915_01170 {ECO:0000313|EMBL:ETK95964.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETK95964.1};
RN [1] {ECO:0000313|EMBL:ETK95964.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ02B3 {ECO:0000313|EMBL:ETK95964.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ02B3.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KI684138; ETK95964.1; -; Genomic_DNA.
DR EnsemblProtists; ETK95964; ETK95964; L915_01170.
DR VEuPathDB; FungiDB:PPTG_20834; -.
DR Proteomes; UP000053236; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR13371:SF0; CENTROSOMAL PROTEIN OF 104 KDA; 1.
DR PANTHER; PTHR13371; GLYCINE-, GLUTAMATE-, THIENYLCYCLOHEXYLPIPERIDINE-BINDING PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF21040; CEP104-like_TOG; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00397; WW; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM01349; TOG; 2.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ETK95964.1};
KW Transferase {ECO:0000313|EMBL:ETK95964.1}.
FT DOMAIN 7..34
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 634..928
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 1020..1052
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1098..1130
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 510..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1800..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2489..2557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..423
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 556..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2580 AA; 287420 MW; F739A459F8FDEA58 CRC64;
MTQTGKWQVH SDDYGNIYFY NSITGESVWE LPDEEPEVSG ETVDNAHKPI DIEKPREQYS
VYSVAVGVAD VMVKIIENIE KNAEQVKKTK VKRKFMSPAA EKRFLKNAAN DEKKKKHLHD
RTVTAYMNIL IPKIGTGGSE ESKKPREVGS LFTAEESRRW QQERELEREV KRRAVRRVRR
QHHAKVESLQ KHQHMLIQFR SDLMKYLLGK IKCSTELQKQ RILLLTTPQM LAEMKERKRE
MQMKLEPEIA EKTMAEERLS ELKYDKNVRN VFDTIDEAGT GKLHLLQILF GVFSKEKPQK
YAAKVRGLAE LLGSPELQRF LVDFVSQADK KDAIGPHLIT VSEFREFVSI LEEVLDHYAG
VKAAVEDAEN DIAAIIAAAS SGGVSLAQAR MGALSAKKIK HELAVLKEHE AQLEAARQRE
KKKSFGAERE SFVAPKEEWE KNHHHRLIRL EESSPVYCCL CRRRKWELWR REQEEIESEY
RSHWPTMLTL RVKAEELRFV QERDGENGIP IEIIEPARQD KQEQNSSIVD TKYEISSDND
KPRRRAHKKK ATRSPRKHAN EPPTSEVPER VKVFENEEQE RKSMYIEERH MVIMLERNRR
ILERPLLRIE DAAHDAFIRL VEHCVNPSGF LLRLEFERCL SFTPPHKMVL AARDNSVKSK
RLSKRLVLQT IPCRTEKMAG YIFSQVANMQ KTLRSPFVAE VESVDKHMFQ LFSELGLLVE
CRPVVFVVTE YFDCGSWLIH YQRHFINENV KYSAVEQHLR NVFREVASGL AAMHSLGLLH
LNVNLGNVYI AGSADNSIHV KIGGLSAWKH DFEAANFQDS NMHDCFNYNY APPEVVKEAQ
ITAKADSWML GCALCEALFM WQRQQLILSA PNQPAQSTQS LIFHTKSIGE LLQKLPIATS
SSLRSLLRML LQPNPAQRPQ MKGINRILSM TKDHAQKLTL KELFQAAQQD DFEAVRDYLQ
VVLHDESESN AQSSIQSIVE PKTNNSLLHY ACDNGNVDAC KYLLMCEGFA TAFLNEPNAF
GHTPLFYAAS SGNLSLVKWL VSNGADIDTD YSDRGDIEPR DEDLGIFTPL QIASFRGHED
VANFLVECNA ELSGTRRNSK TPLHFASAQN HPAIVKLLIE AGADVHACDG DGRTPVDVAH
SAVLPLLLPD EYDVQNEDND LETGSGDNDD DDEFEGDDKT KGGMESVKSA FGAEIARAFR
SKAWKTRVAA INDASMCFQN VFKGKKLVKM FDGACFMMEI ALQDAVSQVA SSCCTSLLKI
AFNAVMSDKD FHTKAFHEER PVLQRIATAL LLRGAGSNEK DSSEAVSSLL FLICKSTDIT
RYLTLQISQM MMSSTTPPLS PSQNSTGPSV SNTNVSRRHQ LVAIKVLTAI TNQYRLDEKT
SGLSFADALK ISMVGLENSS VHVRTASIDL LVQCLVIRCE ESGMKGTTDG IYEHTKNWCE
SLFKQQNQQL KPSIQAKINT GLKNALQKSK RLSNRADESS DTDGRNGIDN SNTAAFDIRT
AMLSPRTKAS QREDDLPYAE PIQGQNKDLA GDMLACFGEK ATRCLFSNAW APRVEALSYL
QYLVETRQLS FASQNASRRT LVSAMQTTLM QALQDRVNSV FEAGVSLLME VSIACEGAVA
SPTDVNVVHD LIRPLIPRLL VKLGDSKNRL HVATEDALLL LSRQASCIGP VFLLEELIAC
DRNSSPQTLS ATYLTNKMAL VSKLMLEFGI IESSDDEGLL PIRNMLQLAL QVCEHKDQNV
RQMSLQIVAD TMQVARSAAM PFLDALARSS RQKLISKLVE RGVMESDMLM DEVDDFYIPT
ETARPGTSGT IRPPTASGSS TKHRPVLTNP SLSATSSSQS SSAAQSQSVQ LPYGTALTTE
QRKMFSNIIQ GFGEELVRCL LDKAWAQREA AIREVERQVL CCASGRVVND SALPKTLEAL
GMLAQMLEIG LNDTVARVFQ CALRLFQVIA AEFLPLVSSE NQYVDEILEN VVGLVLQKLG
DTKQRLRQDC FTLLHSMASL THVGHARMCK MLAEKYQQLT SSSSAVASSP LVIGELLRLF
TMLVREAPAG ENHEQPEVSR ILGIVISALE NKHVDVRNAA ITTYVTIYEA TNGGTNDSYG
EVDLNGFLAE LKPSIRETIT RSVVQITKTL PSSMSRENDD SSRSEIESGR KLQRVLGADA
HKLQQICTAE ITELLTSPTD SRVQRCLGVD KLVDYLVDSS PDMAFKGAWE TCCLLVKQLT
LDAAPTVCLA AFDLLQLLVD PPTQNASYAI PWGEWGVHLV LGSTIRSVVQ QSASENVRVR
LKVRDILRLV AGKSAVGKNA VCNAILSAPE QSDMSGSAGE SIVARKIAFT KLRWQLTLRL
ELLYEFLVVI DSSGEGALSS WRKPTGRGAK SSSEPLGLEN VVPFLGSCMT HPSPMIKTAS
IKIVRFLRST SEEQFSSFIQ ASCSAALQRR LQALMAQAAR NDDEGNNADH FDADRTTCVR
GSRASHVRRV AALRPPRSVP VEETQMMVDV FPPPNSAPGI SRRIAGADDD DSMNDGSRKS
KQQPIWLEKS GSKGLSRKAG SMSFDDGEPE GPVLVGGGVA GLMKARRKTP LRGNNDDVKA
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