ID A0A087SNM0_AUXPR Unreviewed; 1792 AA.
AC A0A087SNM0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=F751_4594 {ECO:0000313|EMBL:KFM27324.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM27324.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM27324.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM27324.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
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}.
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DR EMBL; KL662144; KFM27324.1; -; Genomic_DNA.
DR RefSeq; XP_011400291.1; XM_011401989.1.
DR STRING; 3075.A0A087SNM0; -.
DR GeneID; 23615985; -.
DR KEGG; apro:F751_4594; -.
DR eggNOG; KOG0891; Eukaryota.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:KFM27324.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924};
KW Transferase {ECO:0000313|EMBL:KFM27324.1}.
FT DOMAIN 816..1156
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1756..1792
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1163..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1669..1696
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1792 AA; 185975 MW; 901A0EFA9D30B727 CRC64;
MEPPCSPDTY IPASLRPSES MSNTMPVGPA ATDRRILVIQ RALSASVGAH RMQKLDLRHP
LTLVRVVVSD EFGVDPQLAA LGLLGALLES QAGQKLLTQH MGVLWNDLVC AMWKGPPTNV
RVSTGLRTFL TSLAGLLMPD PGPVGGSMAD LLYQWFVPVL TRGWAKRGEE LTPLQVQSSL
QVLLGGITGE CPQRGAKETM EHPPALHADF RNMVDLLLGW GLDPSFPPAL RLFFLLRRAP
RCWLADLAWA RSLLASLALD ARWRPGPDGT GPALVVLCCM LPIWHGLAGS PDAHIVDEAR
AGAAATLARL RLRDLAADPA VALAQLNDLV LILRGLGSLL GGPGEEAGAA RGLHEIGDKG
VGVEADEWLP CTDRIQATLR SDGWQARCGG DRRPPDLAWS LELAPAPGPL AELRAQAAAL
LLRALALAAP RSASAAGSVL EDLAALLTPC DGHIDHGVAR QARSASGRLL GLAAHPVWAV
RSMAAWVYAA SQVTPCTEVQ ACAEALRSGG AAVRGPSGGA GAGERDAREG RRVLLTRLWC
LEAQCRGIPD AAYDRPAFHV LADAVVGAAA ADADEALMRT VLLQPALHAP LVRGPVEGLE
TTPRTLSPGD PDTLAALLSH GVEALARACV AARLRSSAGS AAELFGSLEA ALGACSPGDE
PREAHAAARG DELYPAPARA FFASNIGELR GRFARLRAPA LAAAEALRLD AHVAAASYAA
VLGSGGAGLP QALRLALEEL HAEACAELGD EAGLATALEA CRSLARWTAA AFLQEDRRKD
GAPCAVAAGA DARALALSGP TWHEPGCEHV RVAGFASGTV DVLQTKTRPK LVHLLGEDGV
ARPFLLKGRE DAAAHAWLLR LADLTRRAAA SASPTLRDAA PAYGLLPLGP RAALVQWLPR
VTPLMELHSR AAAAAARQAA LAGEAAAAAR DGRAFDPAVE RGVPRPPRAA EAFKAALRAQ
GVDPAAPRAE WPASALRAVF ARLQHGAASD FIAARLLAGA WGPGDWVGTG WVLGVGDRHL
DNILLRERDG RLTHVDFDLV FDRGRELNVP ETVPFRLTRC MLLALGPVGA GGPFAGACHA
TLGALRSHAD VMLGALGVAL DDPGIRWRVE GAQAGVSGLW AKVAVARADA LRLTSAARTL
ERLLPRMEHA LMPLGMHMLG AAATKKAQDA GTTELEKGSK ADRHAQDATT VAASATGAAA
AAAATARSAA AKARERAEAA GAALAREHPR LQTALAESEV AAVAHAQLLD SLLGPSHGGA
AALVQAVDPG AAPALALGPM VAGWRGVPPD ALARARLQAA GTDAELAGLL DRRGHCTLVL
AEALARYRGV AALLPPGTIR GHCTLVLAEA LARYRGVAAL LPPGTIVRTT FPARGAEAAR
AALGVSLGEA CARGGDGAVV RATAAHLRDL AEACRQMVEG KGGAGREAVR EAGGRSRSPP
QAWPGLEAGA APGSEQQSLR SASDPDSDLD ALLGRSQRLV LGWGSLALDL RPAFPSDLLW
GEGRLAWLAP AVQGMDALTT AAAELRLATL TPNDLHALER MMGVLPELTS ECGEVVDDLS
RFDSSTLSLY DQEGAWGGPA AAAFAGVLPD ILAVPPRLAA LGERIAELRA AASAARGAGR
AGGSAPRPAS VRELIPVLLA EAAEIATSCD AWQAATPALL TLADEHRGRA RLLMASAKAE
EERRGLRDEV AAAAADIAAL AAGKSLEHGA EAAARPVPPM EADLAAAPRP VATSLFQAQP
RAKPEWIRAT MQRVGGRMQG HQPVEVEVAG LVRQATNPSA LAAMYEGWMA WV
//
