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Database: UniProt
Entry: W9PEQ8_FUSOX
LinkDB: W9PEQ8_FUSOX
Original site: W9PEQ8_FUSOX 
ID   W9PEQ8_FUSOX            Unreviewed;      2374 AA.
AC   W9PEQ8;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Serine/threonine-protein kinase TOR {ECO:0000256|RuleBase:RU364109};
DE            EC=2.7.11.1 {ECO:0000256|RuleBase:RU364109};
GN   ORFNames=FOVG_09941 {ECO:0000313|EMBL:EXA41461.1};
OS   Fusarium oxysporum f. sp. pisi HDV247.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=1080344 {ECO:0000313|EMBL:EXA41461.1};
RN   [1] {ECO:0000313|EMBL:EXA41461.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HDV247 {ECO:0000313|EMBL:EXA41461.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum HDV247.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EXA41461.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HDV247 {ECO:0000313|EMBL:EXA41461.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., 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   "Annotation of the Genome Sequence of Fusarium oxysporum HDV247.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; JH650973; EXA41461.1; -; Genomic_DNA.
DR   Proteomes; UP000030751; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; 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   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
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   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; PF08771; FRB_dom; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01346; DUF3385; 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; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU364109};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU364109};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364109};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU364109};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364109}.
FT   DOMAIN          1242..1842
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2017..2340
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   REGION          2327..2374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2327..2358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2374 AA;  268391 MW;  BD7B3B453EA61A18 CRC64;
     MAQAQQVALD RLDNISRALK SRTSDDLRKR SAVQLRELVA VCHRDLSPEQ FQVFYNAVNN
     RITQLITHGN DSSERLGGIY ALDALIDFDG VDVGVKYTRF TQNLKTILRG KDINPMQPAA
     IALGKLCRPG GAMISEVVDS EVNTALEWLQ NDRIEERRYS AVLVLRELAR SAPTLMYQYI
     PTIFDWIWVG LRDPRQLIRA TSAETVSACF RILRERDQEM KQIWMDKIYN EARSGLKVNT
     VESIHGSLLV LKELLEQGAM YMQEHYQEAC EIVFKHKDHR DPTIRKTVVL LIPDLASYSP
     ADFAHTWLHK FMVYLSGMLK KDKERNDAFL AIGNIANSVK SAIAPYLDGV LIYVREGLSL
     QSRKRGSVDP VFDCISRLAV AVGQTLSKYM EALLDPIFAC DLTPKLTQAL VDMAFYIPPV
     KPTIQERLLD MLSVVLCGEP FKPLGAPQPN TLSSVPIIPK DAKDPHAYEH RRAEVKLALN
     TLGSFDFSGH VLNEFVRDVA IKYVEDEDPE IREAAALTCC QLYVRDPIVN QTSYHALQVV
     GDVIEKLLTV GVSDPEPNIR RTVLAALDER FDRHLAKAEN IRILFFALND EVFSIREVAI
     SIIGRLARYN PAYVIPSLRK TLIQMLTELE FSDVARNKEE SAKLLSLLVQ NAQSLIKPYV
     EPMISVLLPK AKDSNPSVAA TILKAIGELA TVGGEDMMPY KDRLMPIILD ALQDQSSNAK
     RGAALHALGQ LASNSGYVIQ PYIEYPQLLE ILQSIIRTEG QQVPLRQETI KLMGILGALD
     PYKHQAEERT PDSRRGEANQ LTDISLMMTG LTPSNKEYFP TVVINALLQI LKDSSLVQHH
     AAVIEAIMNI FRTLGLECVS FLDRIIPAFL QVIRSATSTR LESYFNQLAT LVSIVRQHIR
     NYLPSIVEIL QEYWHTSPSL QTTILSLVEA ISRSLEGEFK IYLAGLLPLM LGVLDKDTSA
     KRTPSERVMH AFLVFGASAE EYMHLIIPVI VRTFEKQGQP TFIRKQAIDT IGKISRQVNL
     NDFAAKIIHP LTRVLDMGEP VLRTAALDTL CALIQQLGKD YLHFMGTVNK TINQHQIQHS
     NYELLVSKLQ KGEVLPQDLS SGAGFADGAD ETPFADQGTK KLEMNAIHLK AAWDTKGKST
     KEDWQEWLRR FSTTLLTESP NHALRACASL ASVYLPLARE LFNSAFVSCW SELYEQFQDE
     LIQNIESAIK SENVPPDLLG LLLNLAEFME HDDKALPIDI RVLGREAARC HAYAKALHYK
     ELEFLQDQSS GAVEALIVIN NQLQQSDAAI GILRKAQLYK EGIQLRETWF EKLERWEEAL
     AFYEKREEEV PEDQAIPVDI VMGKMRCLHA LGEWEALASL TGSTWANSTP EVQRMIAPLA
     TAAAWGLNKW DSMDNYLSSL KRYSPDRSFF GAILALHRNQ FREAIACVQQ AREGLDTELS
     ALVSESYNRA YQVVVRVQML AELEELIVYK QCDEKKQAIM RRTWETRLKG CQRNVEVWQR
     MLRLRAIVIA PTENMHMWIK FANLCRKSGR MGLAEKSLKQ LIGTDAPLIS AIPYWNEQRQ
     PAPNSRAAPA AQVIYAVLKY QWELGQQLPV NKKGNIPEKT LYCLRKFTND AAHRLEVARA
     HLAAQAGNDV NITGDYGFQN PMDPSLISPH TSRALYDQTV LLAKCYLRQG EWLIALNKDD
     WQYTQVQDIL LSYSQATKYN PRWYKAWHAW ALANFEIVQT LTAGNEGHLS RTDHNMVIDH
     VVPAVKGFFK SIALSQGSSL QDTLRLLTLW FTHGGSSDVN VAVTEGFANV SVDTWLEVIP
     QLIARINQPN KRVQQSVHNL LADVGRAHPQ ALVYPLTVAM KSWQNTRRSR SAAQIMDSMR
     QHSANLVAQA DIVSHELIRV AVLWHELWHE GLEEASRLYF GDSNIEGMFA TLAPLHELLE
     RGPETLREIS FAQAFGRDLK EAQDWCRQYE TSQDVNDLNQ AWDLYYQVFR RISRQLPQVT
     TLELTYCSPK LLNAKNLDLA VPGTYKSGQP IVRIMSFDTT FSVINSKQRP RKLNVNGSDG
     KSYAFLLKGH EDIRQDERVM QLFGLCNTLL AHDSECFKRH LNIQRYPAIP LSQNSGLLGW
     VPNSDTLHVL IREYRESRKI LLNIEHRIML QMAPDYDNLT LMQKVEVFGY ALDNTTGQDL
     YRVLWLKSKS SEAWLERRTN YTRSLGVMSM VGYILGLGDR HPSNLMLDRV TGKIIHIDFG
     DCFEVAMKRE KYPERVPFRL TRMLTYAMEV SNIEGSFRIT CENVMRVLRD NKESVMAVLE
     AVSHPPLQID TSHTDIHSSS MILSLHGVSQ TPHPQQAPTS TLIATQPCPS QAESARVANP
     SSTATSRQVN SSTPLNHQFR PAHAPEQTVQ RARP
//
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