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Database: UniProt
Entry: A0A2G5VT59_9PELO
LinkDB: A0A2G5VT59_9PELO
Original site: A0A2G5VT59_9PELO 
ID   A0A2G5VT59_9PELO        Unreviewed;       471 AA.
AC   A0A2G5VT59;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=Cnig_chr_I.g443 {ECO:0000313|EMBL:PIC54974.1};
GN   ORFNames=B9Z55_000443 {ECO:0000313|EMBL:PIC54974.1};
OS   Caenorhabditis nigoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC54974.1, ECO:0000313|Proteomes:UP000230233};
RN   [1] {ECO:0000313|Proteomes:UP000230233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA   Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA   Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT   "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT   competition proteins.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PIC54974.1}.
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DR   EMBL; PDUG01000001; PIC54974.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5VT59; -.
DR   STRING; 1611254.A0A2G5VT59; -.
DR   Proteomes; UP000230233; Chromosome i.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006974; P:DNA damage response; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   InterPro; IPR038980; ATM_plant.
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   PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR   PANTHER; PTHR37079:SF5; SERINE/THREONINE-PROTEIN KINASE ATM-LIKE ISOFORM X1; 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; 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   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          137..452
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
FT   DOMAIN          439..471
FT                   /note="FATC"
FT                   /evidence="ECO:0000259|PROSITE:PS51190"
SQ   SEQUENCE   471 AA;  54326 MW;  4A83ABC1D544CDBA CRC64;
     MCFFFEQIQI PAQPLKSAVE RTFKEPFESE SLADNRYADT RRVQKIGSVP NVKDLNILKV
     MNKRLENTKK KEIAKLQVKE NIRIQRVERD GKTMLVWPRD LKIFKCKLDQ LPIPTISQKI
     GAPGDLSTSN LITWRSYKDV FSLADGLSSP IIWEIQGCDG RWYKTVWKKE DVRQDVLVEQ
     MFDVTNNMLE KRALRTYNVV PLDTECGIIE FCGGSVSLKE LLCGTNREGG LHKEMCSDEP
     SATQASRMMK EVQSDTSEMR RRVFVEVCQQ YSPVFRHFFY RQFPTAHIWR QKIDTYRESL
     ATWSVVCYIV GLGDRHASNI LFDQKECTFV HIDLGMILEY SKRSLPVPEQ VPFRITRDVL
     DPLLIEGIEN GRLAEDCTKI MEKLEQNNKV ILGVASAILR ETMSNFREAE QSSGRPSYIS
     EMAIGRLRDK LRGTDDGVTA QSSNLQIRRL LRDATSSDNL SRMFFGWMPF L
//
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