ID A0A1E3NJQ3_9ASCO Unreviewed; 2384 AA.
AC A0A1E3NJQ3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=PICMEDRAFT_33858 {ECO:0000313|EMBL:ODQ46372.1};
OS Pichia membranifaciens NRRL Y-2026.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=763406 {ECO:0000313|EMBL:ODQ46372.1, ECO:0000313|Proteomes:UP000094455};
RN [1] {ECO:0000313|EMBL:ODQ46372.1, ECO:0000313|Proteomes:UP000094455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-2026 {ECO:0000313|EMBL:ODQ46372.1,
RC ECO:0000313|Proteomes:UP000094455};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
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DR EMBL; KV454003; ODQ46372.1; -; Genomic_DNA.
DR RefSeq; XP_019017485.1; XM_019162849.1.
DR STRING; 763406.A0A1E3NJQ3; -.
DR GeneID; 30179536; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000094455; Unassembled WGS sequence.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProt.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt.
DR GO; GO:0019219; P:regulation of nucleobase-containing compound metabolic process; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR_cat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000094455};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 996..1034
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1251..1831
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2005..2322
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2352..2384
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 2384 AA; 271815 MW; BE13D72714834BD5 CRC64;
MQNFTLDQIF QELKSNDEIR RLKAAKNLRV HFISISRDST STEQMTVYNN YINKKIFDLT
NSSKTNEQLG GIDAINSLIE LLSPDENSNM ITRYANYLRR LLSSNDINVM RAATATIGKL
AIPGVSTTAD FVEFEVKRSL EWLITEKIEG KRHAAILIIS SLAENSPALL YQYVKQIFNN
IWIGLRDSKS SIREDSAVCL RHCLDIVYER DNDLRNYWFS KLYSEAFSIL NSPPEFIHGS
LLCFRELVNQ GTSVLGSKID EIYETIMRVK DYKSVDVRRE VTTIIPQMAR YDKIKFVDRY
MHRVLLYYIS QLKVGKDKVM ILLSIGDIAT EAKNNMVNYL NGIVLESVRD GLSQSSIKVQ
RELSPACCYC LAKLVLALGP PMTKFINAYQ ILRLLLKSPI NDNVLSVLKI FSKHLPSLEP
IINDRLINNV SCCLSGYEFR HPGSPDFERL FDPDLAYNYR YDMLLKEDIP ASKYFEDPDV
TIILQGLKTL RCFAFKNYDL TEFVQYAITH YISHQNPEIR LQASVTCAEL YRRSSICYER
SAHSLKSVDF VLEKLLTTCI TDPVAEIRLE VIKSLDDKFD PHLSQAENVK LLFMTLNDED
FEIRKQSYRV VGRLTFFNPA FIVPPLRKIL IQLITNLEYG SHTTRIKEES NVLLGILISS
TDDLTKSYTK QIMNALLPQA ADISPVVSAS AITTIGCLAD VSCEDIMPFV PQIMPILIDS
FQEQNSGIKR DASLKTLGQI AGSAGYVIQP LLDYPQLLGL LVNILRSESS TIVRRDTIRL
LGILGALDPY KHREVERKGH DAETVARQNA PPIDMELLMK GKSPTNDDYF PTVVIRTLIK
ILKDNSLAAQ HLAVTQTIMN IFSGLGMKCV PFLDQVIPAF EIVMHNCPIS MLNTYFQQIC
DLIDIVKLNI RSYLPQIFKL IQEFFPNVKL QSKVICVIER VSKALEDEFK LYMLDLINIF
LNVLEKDLSP GNMSTLRVLK AFVIFGSNSE PYIYMIIPSL IKLFEYASVN VRKAAIECVG
RLSRTIPLND YASEIIQPLL RLLSTYGGTG LRTVAMTTIC SLLLQMGSDF KVFIPVVSSV
LIKSKLQFPL YDQFVDRLNK GRQLPSGVVL YPDLETTTSD NIQAEQPQKK LSVNPQTLRL
VWDCSSKRTR EDWQEWMRKL SIALLKESPS QALRACSTLA SVYPQLAKDL FNCAFASCWN
ELHIQYQGEL AQALCIALSS VNSSPEIHQA LLNLTEFLEH DEKSLPIRIQ TLGQYAQRSH
AYAKALHYKE LEFIQEPSIP TIESLISINN QLQQSDAAIG ILKYAQEHHG LQLKETWYEK
LQRWDDALHA YNEREKEEPN STEITMGKMR CLHALGEWET LSMLAREKWD TSSADIKRSI
APLAAAAAWG LRQWERMDTY IAVMKKDSPD KAFFNAILSL HNNNFDEASL QINKARDLLA
TEVTALVSES YNRAYGVVVR VQMLAELEEI IKYKCLPQGS DKRIHIIDTW NKRLLGCQKN
VDIWQRMLKA RALVVKPKQD MEIWIKFANL CRKSGRLRLA EKSLNSLLDE GSAGKPGNKA
SPHVVYAQLK YMWSRGQKAE ALNHLVDFTS KLSRDLGLNE NEAITQPLPT NIPGITDDIE
KFTKLLARCY LKQGEWKIAM DDTWIEKEAP SILGSFLLAT HFDPKWYKAW HNWALANFEV
ISPQSKHRQN YIVNGNSNAS GNGISENNGG DNKMDVQHHN INMNMILRYV VPAVKGFFHS
IALSFSNPLQ DTLRLLTLWL DFGGVEEVAT AMQEGLQMVK VDTWLDVIPQ LISHIHQPDP
VVSHSLLGLL SDLGRAHPQA LVYPLTVAIK SESVSRQKAA LTIIDKMRAH SSILVDQADM
VSNELIRVSV LWHEMWYEAL EDASRAYFNE HDVEKMFSIL DPLNELIQKG PQTIREISFT
NAFGKDLSDA HGWLHQFKRT KDVTYITQAW DLYYTIFRRI SKQLPLLQNL DLQHVSPKLL
NAHDLELAIP GTYEAGKEVI RIMKFDPIFI VITSKQRPRK LHIHGSDGKT YTFVLKAHED
IRQDSLVMQL FGLVNTLLAN DPECFKRHVD IQKYAAIPLS PSSGLLGWVP NSDTFHVLIK
EYRDPRKIYL DVEHRVMLQM SPDYDNLTLL EKVEVFTYAL DITRGQDLYK VLWFKSKSSE
SWLDRRTTYT RSLAVMSMVG YILGLGDRHP SNLMMDRITG KVVHIDFGDC FEAAIMRDKY
PEKVPFRLTR MLSYAMEVSG IEGSFRITSE NVMKVLRDNK DSLMAILEAF AYDPLINWGF
DFPIQRVIEQ AGLPIKLQEG NYVELLRNGQ ITEEEAAVMA MRYKAGVRDA RAACVLKRIN
DKLTGNDFKR FKGLDVPTQV DKLIQQATSV ENLCQHYIGW CAFW
//
