ID A0A437AKJ5_9MICR Unreviewed; 1669 AA.
AC A0A437AKJ5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=TUBRATIS_18420 {ECO:0000313|EMBL:RVD91690.1};
OS Tubulinosema ratisbonensis.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Tubulinosematoidea;
OC Tubulinosematidae; Tubulinosema.
OX NCBI_TaxID=291195 {ECO:0000313|EMBL:RVD91690.1, ECO:0000313|Proteomes:UP000282876};
RN [1] {ECO:0000313|EMBL:RVD91690.1, ECO:0000313|Proteomes:UP000282876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Franzen {ECO:0000313|EMBL:RVD91690.1,
RC ECO:0000313|Proteomes:UP000282876};
RA Polonais V., Peyretaillade E., Niehus S., Wawrzyniak I., Franchet A.,
RA Gaspin C., Reichstadt M., Belser C., Labadie K., Delbac F., Ferrandon D.;
RT "Draft genome sequence of the microsporidian Tubulinosema ratisbonensis.";
RL Submitted (OCT-2018) 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:RVD91690.1}.
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DR EMBL; RCSS01000442; RVD91690.1; -; Genomic_DNA.
DR STRING; 291195.A0A437AKJ5; -.
DR VEuPathDB; MicrosporidiaDB:TUBRATIS_18420; -.
DR Proteomes; UP000282876; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; 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; 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 PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF72; SERINE-PROTEIN KINASE ATM; 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; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:RVD91690.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000282876};
KW Transferase {ECO:0000313|EMBL:RVD91690.1}.
FT DOMAIN 1367..1661
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1637..1669
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
SQ SEQUENCE 1669 AA; 200579 MW; 33E8341BD3AC4171 CRC64;
MDKNYRKNLC IKQIESIPCY KTYLECLNKV TSKKVINTII YSIIDKEIDT NHLYSFLLQK
IRNNLLFYSK CIQSDFHLLL KRKPIREEEY LFAVEFYKEI PIKSIDTFPS FLNFYIYSTN
HYFYKFENIL PNFQSMLEKE IFFGYFFDLI KFYQTNKVHK ETFLNLKEVV YASDYKEKNL
MLYLIYTFLG EDETKLNLKP LLQAELHLNY IEFYNPLLIH NPNLSDYVGL FLCYKNKVNN
FCSICGKNVE YFTEFFNVKK EYFENYINNF LNTELNFTNK HLKNLLKHDK RFLTVKNFRL
ILFYALYKNE DYFYELLNYF QINQETEAII LEGFKKFYKD IKSFKSIFKF VRNIQRNEKI
AYTIFVILYK HFSSSNSFMK LKIKNYFFLE EKEFLNLKGK MIEHVYLNNN TSLNTNELIL
NDLACMLNFN VFDFIKNNMF FIFPVSLHSV KYSQEEMTAN IFYLFIRNIL NNVDDLLGYD
KKEVTCSNEY QIISYILLLD YSKCVLLSQF LEEPFEIFLC KNITPILFNL RTIYFDCKIH
PNILEIFKFI ILILEEKCCV KDLFDFSEVT EVLEFYLECF IFSNPFIEND FIFKNEENFI
NLYQNLRKFK NIILPYLPIN ILQNIFNITD ILFSKNINSE KGKVFLFEKI IDLNQNNLEN
EKLITEIFKR KIYSKKISEF LSNFKNTNKF CILQEVKKDY YFEGDINSFN DLSLFLISVL
IDNMNYDKQY IYYFSIQETI KYIDNLTLSK FYNSVKGFLK TKYFLHINLE QTNFVYTKNI
TYSKFMHSFL VYALNDLFIL HNEFYELTKF AILLDDKAKE IYLFLIVKFL IYKKEKDFLR
KINKIFLQLI NEKNSFIDKR IVKFFLNLFF FCEKSIFECE NVLEMSLMVQ DDYFVIYLIE
ELIRKNNFNL EYFLKYKDFL MYSSFMINKF NYIKGIQSSL DLFDLTHLFY NFCMEKNYIL
AKKCLPKNED NSNLERILKM NKETDLEIDL IEKVVEEIFL EKWDDSFLEK FKKTIFYSEN
LTLDSKLEKF KFFNDIKLFF ENKPIELTDC DFKIYENLCL VLEKKNFKEN LHKFSLEIKK
RKINKLMNNN EIETVLEEIT DLLVKGEYGI LYAKSKLLLK INKKVEAKLC LKKLLKLFSE
KKLENDFLRI KATILYCEIM QSSLEYENAI KNINNSEKLY FLQGKFYEEK EIGKSIISFI
KSVKFGKKYY QESIPLIFHL FFTNNFKNTL VENEMTDFIN KTDLNDLLPY FTQIIPKIAS
DSFELIIKLL IRFYNEIPHK TFWDSFNFIN SSSNEIKLRM EEAIKKIKFD SRVLLSSYTN
VSQIFIKIAS SKLKTSKLKY SDIXKKEIKF DSVTLPNLQM NYFIEQIEEE ITVYCSLQAP
KRIEIIGSDG KKYFFLCKPN DDLRMDGRFI DLCNLLNQSF EKNEESVKIK LYKVIPFTHK
TGIIEWIDGL TSLKDLIYKF GGKGEVHSVI NKFRNKKKIG LREFKCLKIT PVLYKWLEEK
NNPKEWFYAR ERFIQSYAVM NMIGWFMGLG DRHCENIMFD KNYXTVHVDL NCLFDKAKTF
LVPEKVPFRL TLNILNAFGI LKTEGCYRET MENVLNILVE KKNLIIANLL SFVYDPVFEW
KKMNPSTIIE VLKNKLEIKD VQNCVDELIK EATDENNLCE MYIGWMPFV
//
