ID X0C8J9_FUSOX Unreviewed; 2294 AA.
AC X0C8J9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=FKBP12-rapamycin complex-associated protein {ECO:0000313|EMBL:EXK79037.1};
GN ORFNames=FOQG_16328 {ECO:0000313|EMBL:EXK79037.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK79037.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK79037.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK79037.1,
RC ECO:0000313|Proteomes:UP000030663};
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 PHW815.";
RL Submitted (NOV-2011) 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 -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
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DR EMBL; JH658486; EXK79037.1; -; Genomic_DNA.
DR HOGENOM; CLU_000178_7_1_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
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; 5.
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; IPR000357; HEAT.
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 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; PF02985; HEAT; 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; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REPEAT 704..736
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1242..1842
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2017..2294
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 2294 AA; 260174 MW; 2AEEB7008AA94334 CRC64;
MAQAQHVALE RLEQISRGLR SRTSDDLRKR SAIQLRELVA VCHRDLSPEQ FQAFYNSVNN
KITQLITHGS DSSERLGGIY ALDALIDFEG VDVGVKYTRF TQNLKTILRG KDINPMQPAA
IALGKLCRPG GSMISEVVDS EVNTALEWLQ NDRVEERRYS AVLVLRELAR SAPTLMYQYI
PTIFDWIWIG LRDTRQLIRA TSAETVSACF RILRERDQEM KQLWMSKIYN ESKAGLKVNT
VESIHGSLLV LKELLEQGAM YMQEHYQEAC EIVFKHKDHR DPTIRKTVVL LIPDLASYSP
ADFAHTWLHK FMVYLSGVLK KDKERNDAFL AIGNIANSVK SAIAPYLDGV LIYVREGLSV
QSRKRGSADP VFDCISRLAV AVGQTLSKYM EALLDPIFAC DLTPKLTQAL VDMGFYIHPV
KPTIQERLLD MLSMVLCGEP FKPLGAPQPN TLNSVPIIPK DAKDPHAYEH RKAEVKLALN
TLGSFDFSGH VLNEFVRDVA IKYVEDEDPE IREAAALTCC QLYIRDPIVN QTSYHALQVV
GDVIEKLLTV GVSDPEPNIR RTVLAALDER FDRHLAKAEN IRILFFALND EVFSIREVAI
SIIGRLARYN PAYVIPSLRK TLIRMLTELE FSDVARNKEE SAKLLSLLVQ NAQSLIKPYI
EPMISVLLPK AKDNNPSVAA TILKAIGELA TVGGEDMMPY KNKLMPIILD ALQDQSSNVK
REAALHALGQ LASNSGYVIQ PYIEYPQLLE ILQSIIRTEG QCVPLRQETI KLMGILGALD
PYKHQAEERT PDSRRGEANQ LTDISLMMTG LTPSNKEYFP TVVINALLQI LKDSSLVQHH
SAVIEAIMNI FRTLGLECVS FLDRIIPAFL QVIRSATSTR LESYFNQLAT LVSIVRQHIR
NYLPSIVEIL QGYWHTSPSL QTTILSLVEA ISRSLEGEFK IYLAGLLPLM LGVLDKDTSA
KRTPSERVMH AFLVFGASAE EYMHLIIPVI VRTFEKQGQP TFIRKQAIDT IGKISRQVNL
NDFAAKIIHP LTRVLDMGEP PLRTAALDTL CALIQQLGKD YLHFMGTVNK VINQHQIQHS
NYELLVSKLQ KGEVLPQDLS SGAGFADGAD KPPFADQATK KLEMNAIHLK AAWDTKGKST
KEDWQEWLRR FSTTLLTESP NHALRACASL ATVYLPLARE LFNSAFVSCW SELYEQFQDE
FIQNIESAMK SESVPPDLLG LLLNLAEFME HDDKSLPIDI RVLGREAACC HAYAKALHYK
ELEFLQDQSS GAVEALIVTN NQLQQSDAAI GILRKAQLYR EGIQLRETWF EKLERWEEAL
AFYNKREEEV PEDQAIPIDI VMGKMRCLHA LGEWEALASL AGSTWANSTP EVQRTIAPLA
TAAAWGLNKW DSMDNYLSSL KRYSPDRSFF GAILALHRNQ FREAIACVQQ AREGLDTELS
ALISESYNRA YQVVVRVQML AELEELIVYK QCDEKKQAIM RRTWETRLKG CQRNVEVWQR
MLRLRAIVIA PTENMHMWIK FANLCRKSGR MGLAEKSLKQ LIGTDAPLVS TIPYWSEQRQ
PGPGPRNAPA AQVIYAVLKY QWELGQQLSA NKKANIPEKT LYCLRKFTND AAHRLEVAKA
HLNAQAGSKV NITGDYGFQN QMGPTLMSQQ TQRALYDQTV LLAKCYLRQG EWLIALNKDD
WQYTQVQDIL TSYSQATKYN PRWYKAWHAW ALANFEIVQT LTAGNEGHLS RTDHNMVIDH
VIPAVKGFFK SIALSQGSSL QDTLRLLTLW FTHGGSADVN TAVTEGFDNI SIDTWLEVIP
QLIARINQPN KRVQQSVHNL LADVGRAHPQ ALVYPLTVAM KSWQNTHRSR SAAQIMDSMR
QHSANLVAQA DTVSHELIRV AVLWHELWHE GLEEASRLYF GDHNIEGMFA TLEPLHELLE
RGPETLREIS FAQAFGRDLK EAQDWCRQYE TSQDVNDLNQ AWDLYYQVFR RISRQLPQVT
TLELTYCSPK LLNTKNLDLA VPGTYKSEQP IVRIMSFNTT FSVINSKQRP RKLNINGSDG
KSYAFLLKGH EDIRQDERVM QLFGLCNTIL AHDPECFKRH LNIQRYPAIP LSQNSGLLGW
FPNSDTLHDL IREYRESRKI LLNIEHRIML QMAPDYDNLT LMQKVEVFGY ALDNTTGQDL
YRVLWLKSKS SEAWLERRTS YTRSLGVMSM VGYILGLGDR HPSNLKLDRV TGKIIHVDFG
DCFEVAMKRE KYPERVPFRL TRMLTYAMGV SNIEGSFRIT CDNVMRVLRD NKESVMAVLE
AVSFLSISKL KIPY
//
