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Database: UniProt
Entry: A0A024GJI9_9STRA
LinkDB: A0A024GJI9_9STRA
Original site: A0A024GJI9_9STRA 
ID   A0A024GJI9_9STRA        Unreviewed;      2930 AA.
AC   A0A024GJI9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=BN9_076520 {ECO:0000313|EMBL:CCI46697.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI46697.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI46697.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI46697.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC       {ECO:0000256|ARBA:ARBA00010769}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCI46697.1}.
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DR   EMBL; CAIX01000137; CCI46697.1; -; Genomic_DNA.
DR   STRING; 65357.A0A024GJI9; -.
DR   InParanoid; A0A024GJI9; -.
DR   OrthoDB; 8448at2759; -.
DR   Proteomes; UP000053237; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00892; PIKKc_ATR; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
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   PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR   PANTHER; PTHR11139:SF72; SERINE-PROTEIN KINASE ATM; 1.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM01343; FATC; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 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:UP000053237};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1790..2452
FT                   /note="FAT"
FT                   /evidence="ECO:0000259|PROSITE:PS51189"
FT   DOMAIN          2550..2872
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          2898..2930
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   2930 AA;  336362 MW;  B5D19FD5DFCCB829 CRC64;
     MPLQTDIDSL VQLLEQHKNS HEERKPRLTS HAAYIAHQVE TCSALLLEGC GTILRKLQSI
     LPNMLKLISS IDPEVAPKIL RHLCKLFMIA LDENTCPHIH LAFITPSYKT ARSDELEGDQ
     ESSVQLSGFG TLYLYLVSFY CNQTYRQVRG DLLAVLEEFG MILQQYDPAA LAHILDDTLM
     NIQQCLLQEK EQVRRGKCVL YPTTAIHMFR TADGALSQNN KKHILCGCDI SGNMEEKRSR
     ARQLEQLLPS IKFAPDEKES ESRELWEAYA ITLIKNHPTV LSCGNINKRY VFETIKRVYR
     FEQKKLGNRR VYETTLNLLY AVFSEFVSSD QALIEFGCFY FGTIDWKHNV DYGITTHVAI
     ITQLERNSCN HSVSHFIWKS FDKWLLKMIE SDFFKEPQYQ ETAKTWIRVS IMFLQQYIDS
     NGPLSTIAKY RFTTMLDIIR PRLDSDEEFF HEIARILHRT FGEDSTFLAK FMRILHTSLA
     ISAIESRKRK RQLVKEREKM YTLSPTEQNS SQIHLQLAKW FLTQPDQGSH NARNADDTFL
     EAFRLLGPLC WSRAATSFPE TESVRALILD RFDRATIDLS SDITEKRFRL VLMNLTLLLF
     LVDDMQLQSR ANMYSTILSL IQTRKKLDRG YSIGTTWKAM CELAQILQNL PKGEIPSMPA
     TCTSYLLLPY LVWMRSKPLR SLISEKWEDS IPLRVSCGGW SLISELNVQF ESILYSPLLI
     IFLAREGVAS AEEVAEYLLE RIRLLMRENG KLTPELQTVL CKTVCAVVCL TYSTKYDTKQ
     STTAGVMRRS GCILCHSNEN SRLNFSNYQV FITLIKDEDQ KKSTEAIMAR TELLCTILRH
     LETSFMSTDD LIIIINDFLL GLSCEHKAAH RLIIASIGLL PQCLTLLDSV SMSIHREGFG
     PEVVSLFREL LKSMENENDQ SRLHLVVRSI GAICRNCDKS NQAQMELLLL LMIQLVIFWS
     YHQWRPEVAA IFYNAIKRIE NHHKLSWRRL CRNFPQQIYV PLIGKLLKYK TVCDFLHTFL
     NDSVDPRTFL LASAPHTLPK YVAEQDEERL HLFQLALNEF QGTKLGSGES EDSNQSDVSS
     ISDIILAQIE HIFKELIMQH IEHGDIGVEG TAWEFLFRYL PPKTTIRDVI FHSPIRVMNL
     LVWELGGERF ETARRAFTQT LSYMYQDGSG EESESIPKDD TDQVFYPISR HYFLAVMTVL
     STKIKTKDCL NEFGSSTRLR AVTCVGRLLE CLLLDKRGSK TALYGRTRGQ FVDPFVPKIM
     ATLKILWIDD DIKLKEHGIR AWSTFVQLLS DKALGSNILA ILVSTLPYLG IQPEESAYSS
     DTTSSTKKDQ PEHEQSIKGI VVELLEYIFV EKRSELRKSF PRVPLLPKIP ELSNVHAVLE
     EEMGDCYSRP IEELISDLID ILRHWDSTVR ELALKQVYQC FIHRQNDVQG LIQSDFDPFI
     HGTIAELMAT ILRLTKTEIK TENKLLCAMC LGAIGAIDAA HMPIHMSSSL TSASKQTGEY
     TTKELACVLI ESLLVDELRA APDSTDSLAF AIQELLRFLG ELTTDPDVQS SNQSGEKGDL
     PGWMKDRFES RNVLQYIEPY WSTGYTLSLS SDNNGQAPAE YDQNSTLYER CGKTYEDWIA
     EWCKRLIHLS QPPEQKIFWA STAAVSSCPQ VARFLLPYLI QNVLRTGNSQ VYQEVKREIL
     SVITNRDQYN ETIFTSSAHA EIGGVISQSQ YEDTYPNYAL ETHNDNHSRH HQCAQTLFST
     LDELNDWVWA QEKKRNLTNG SNNTTNGLSE LDDQEKENLE EFLKDIPSRL LSNAAYSIRA
     FARAVQYFEI HLRQQSNSLE CQYANTLDPS PVPLSVIMSN ISHVQLLYSS VNETDALVGL
     ATIRRKNRAE SGEDQSNMIV QSIKLTDLLY KIVDYEQLAQ WEDALVCYEQ ALQQIHALPT
     QFGIHNVSES HHGDQWNGEV KTLREKLYVG TVRCLIQLGR LESALQQING IVSTEPSFME
     SLHQHALECT WRLSRWELLS DLLQSDKTNF STENNSVAQD PTQQLWSFPF FSRQKDVNGD
     TSHIKFVRVL HNLHTKDAKA LSTNLRTARL EIMGPLAAAL GESYQRAYPM LHRLHFLHEV
     EQGFAALSKV YDVSDESQRA DVWKRHCNWE SRYALIANSL RFRDPILALR RVLATKADLL
     TDLSSNWLQY AKVARKEGFI RTATNAVMHA DLLCNPSASM EQAKLLIQQN RMYEALQTIE
     PVEIDTSKLE FDAEHSALNA KRLLLATNWM QQFGLRQGKQ IIERYRAVIR LNPTCEKGYF
     HLAKYFEYLL ATAYPSLHLN EERANDTSLS IAPDSGFHQL LINLMRNYIS TLKHGTKYVY
     QALPRLLTLW FEYGELLHAG ALRKNKTMRQ MECAGLRENN WSSIVLSDIA QLIEEAMEIL
     PVYVWLVGFP QVLSRICHPN PQVVEGVKQI IIKVLTHYPA QSMWPIVGLS RSLNAQRRNR
     SRETIAYAQR IFVAREDQDN ATSFSEVMRL AEELISLAAH DPKNQRKMHI RLSRMRTKVL
     LPIQANLTVS FPHSTHWDPP SERHVYINTF ADKADVLMTK EKPKRIEMLA SDGKYYPFLC
     KREKTGDLRK DARMMEFNNM INKFLQKDTD ARKRKLRLRT YAVVCLNEES GLMEWVQQTR
     AMRQLIGQIH KTELGFIQPF RLTHEIRDQF LAMQKKYAQD TKLMAAYFQQ KILTLPVFKP
     RFHQWFHNNF SDPTAWFEAR STFTRSTAVW SMVGHIIGLG DRHGENILID CTNGECVHVD
     FDCLFDKGLK LAKPEIVPFR LTPNMIDAFG ITGYEGVFRC VSEIIMRLLR NNRDALKNVL
     ESFIHDPLVE WGRRGKGVQG SMSSTTIPEI SSERSKEETR IILKTIDDRL RGIYNLGDAI
     RPLVSPSQRR MLPENEGFPL SVPGQVNKLI QEATSTENLA QMYIGWMPFL
//
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