ID A0A061H0N9_9BASI Unreviewed; 2344 AA.
AC A0A061H0N9;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN ORFNames=PFL1_06580 {ECO:0000313|EMBL:EPQ25907.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ25907.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ25907.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ25907.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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 ECO:0000256|RuleBase:RU364109};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031, ECO:0000256|RuleBase:RU364109}.
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DR EMBL; KE361649; EPQ25907.1; -; Genomic_DNA.
DR RefSeq; XP_007882314.1; XM_007884123.1.
DR GeneID; 19320653; -.
DR KEGG; pfp:PFL1_06580; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000178_7_1_1; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000053664; 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:0106310; F:protein serine kinase activity; IEA:RHEA.
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; 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; 1.
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; 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, ECO:0000256|RuleBase:RU364109};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364109};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364109};
KW Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU364109};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT DOMAIN 1251..1806
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 1982..2293
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2312..2344
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 2264..2283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2344 AA; 264970 MW; 3477EE37818A0610 CRC64;
MSTISAQQSD TLNRIFTALK SRDDATRQAA GRDLGSHVSL VISELKGDHL STFFNDLHRR
IFELTHSQHA HEKLGGIVAI EGLIDLESED NSARLYRFYQ YLKPNLPCND AQVMIAASKA
LGRVSHFGGQ SLGDQFIEFE VLRALDFLQA GDRNESGRYA AVLIIKEIAR NVPHHFHLYV
PRVLDRIWIA LRDTRVIVRE GAAEAMGACL EIIASREKQM GSHFFETIYE EAERGLKMNT
VEAIHGSLLA VQQLLQYSKT FMRSRFHRAC ELVFRLHKHR DPLIKRTITN LVPVLARYDP
QYFAEEHLGA VMTILTEQLR KEKERSPKES SQTFETIGFV AAAMGSRMKP YIEPILACIK
EGLQMRGKKN APPESPIFLC IGNLATAVGP HLTKYMHDLL DLMFACGLSV SLVTALDRIV
KSIPPLMRVV QDRLLDMLSM TLISQPYRPL GAPLPLRGAR DGAAAAQTSE AKGVETVTVA
LETLGKFDFQ GHILNEFVRN CTLPYLEDDH AAVRKAAAET CADLFVNDPI CYQTSMHAIE
VVNDVLDKLM TVGIADPVAD LRWTVLNKFG TREQFDRHLA QSEYVRSLFI ALNDESFKVR
EVAIVIIGRL AKHNPAYVMP SLRKALIQLL TELEYSTVSR SKEEAAKLLT EVVRASQRLV
KSYALPMLEV LLPKASDASV GVSARVMECL GELAKVGGED LAPNVDQLMR LAIDQLSSTA
PHSSTAKRDA ALKTLGLVAS NTGNVVNPYL TYRNLLGTVV KILKNEQVPA VRRETIRVMG
ILGALDPYRY KLLEKQGDEG SAEASKGSGT DLFELALAIG TSTDDYYQNV AIDALISILK
DPSLSTHHHA VIEAIMYMFK TQGLKCVTFL PQIIPAFLNV IRTCGTGLSE FYYQQLAILI
SIIKQHVRSY LEDIFGLVQE NWNPNSSIQL TIVSLVEAVA KALEGEFKSY LPVLLPNMLQ
TLDGEITSKR QPTLLRILHA FYVFGSNIEE YLHLVLPVIV KMFERPDAST TLRKAAIATV
GNLSRKVSFC DHASRVVHPL VRVLHNNASA DVRGAVMDTL AALVLQLGSS YAIFIPVVNK
VLVQYRIQHA TYDQLIAKLL SGERLPQELV PLDGSLDNKA EEAPLAEATK MTVNQQHLKQ
AWDTSKVSTS EDWKEWLRRM AVEFMRESPS HALRACRSLA DVYQPLGFAM FNAAFVSCWT
ELYEQYQSDL VKAIETAFDA PDVPDHIVHM LLNLAEFMEH DDKALPINIR TLGDRAYKFH
SYAKALHYKE AEFLTDPSPQ VIESLIDINT KLQQSDAAFG ALTYAREHLD MTHHEEWYEK
LHRWEEALFA YDRKAELDPD DYEIAFGRMR CLHALGEWEH LSDLVQQKWH NADPEDRRHI
APLAAAAAWS LGEWETMDEY ISAMRSDSSE RSFYRAILHT HRSQRSAANK QIAKARESLD
GELTALISES YGRAYDLMVR TQMLSELEEA LAYKLDYKDQ PDRQATIRST WMKRLKGCQP
EVEVWQRILS VRSIVLTPAD DTETWIKFAN LCRKSGRMVL AEKTLNSLLG PELNGVDARS
PIGPKAPPPV IYAHLKFMWA SGVKTESLTY LRDFTINLAD DLGIYAVDDQ GNQVVQDWQA
SPRLGEFARL LARCYFKQGE WQTALNEDWV TDDECDVIES YRRATELDRN WYKAWHAWAL
ANFEIITHHE RKGDQITPQM IAASIVPSVQ GFFRSIALAS GNSLQDTLRL LTLWFKYGYQ
EDVAEAVNEG FSSVIVDTWL EVIPQIIARI TAPSQKVRRL IHHLLSDVGL AHPQALVYPL
TVATKSPSVI RIQTAMGIMD NIREHSPVLV EQALLISNEL IRVAILWHEL WHEGLEEASR
LYFTEHNIDA MFATLEPLHD ALEKGPETLR ETSFAQTHGR DLAEARECGR RYRQYGDLSD
LNQAWDLYYH VFKKITKQIP ASNSVQLDLQ YVSPKLLAMR DLELAVPGTY QSGKPIVRIM
NFEQIVLVIA SKQHPRRLKM KGSDGKAYQY LLKGHEDLRQ DERVMQLFGL VNTLLSTDSE
SYKRRLEIRR FPVIPLSPNT GMLGWVEDTD TLHVLIKEYR EQHKILLNIE HRLMLQMAPD
YDHLTLMQKV EVFEYALDNT PGQDLYRVLW LKSRNSESWL ERRLAYTRSL AVSSVAGYIL
GLGDRHPSNL LLDRLTGQII HIDFGDCFEI ACHRPKFPEK VPFRLTRMLV NAMEVGGIKG
TFKVTAENTM RVLRDNRESV LALLEAFVHD PLISWRLVTD DASERQAPDA SENEAAAGHR
TNQVGDVRNQ KALEVVRRIQ NKLNGRDFNP NVSLSVAAQI ERLVQDATSK ENLCVAFVGW
CSFW
//
