ID   PIM3_COTJA              Reviewed;         323 AA.
AC   Q9PU85;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Serine/threonine-protein kinase pim-3;
DE            EC=2.7.11.1;
DE   AltName: Full=qpim;
GN   Name=PIM3; Synonyms=PIM-3;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10713710; DOI=10.1038/sj.onc.1203355;
RA   Eichmann A., Yuan L., Breant C., Alitalo K., Koskinen P.J.;
RT   "Developmental expression of Pim kinases suggests functions also outside of
RT   the hematopoietic system.";
RL   Oncogene 19:1215-1224(2000).
CC   -!- FUNCTION: Proto-oncogene with serine/threonine kinase activity that can
CC       prevent apoptosis and promote cell survival and protein translation.
CC       {ECO:0000250}.
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   -!- 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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. PIM subfamily. {ECO:0000305}.
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DR   EMBL; AJ130845; CAB62386.1; -; mRNA.
DR   RefSeq; XP_015707762.1; XM_015852276.1.
DR   AlphaFoldDB; Q9PU85; -.
DR   SMR; Q9PU85; -.
DR   GeneID; 107308404; -.
DR   KEGG; cjo:107308404; -.
DR   CTD; 415116; -.
DR   OrthoDB; 930292at2759; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017348; PIM1/2/3.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF037993; STPK_Pim-1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..323
FT                   /note="Serine/threonine-protein kinase pim-3"
FT                   /id="PRO_0000086536"
FT   DOMAIN          40..291
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         46..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   323 AA;  36597 MW;  E2A4FA20B6F6396C CRC64;
     MLLSKFGSLA HICSPASMDH LPVKILPPVK VEKEPFDKVY QVGSVLGSGG FGTVYAGSRT
     ADGLPVAVKH VVKERVTEWG TIGGVMVPLE IVLLKKVGSG FRGVIKLLDW YERPDGFLIV
     MERPELVKDL FDFITEKGAL DEDTARGFFR QVLEAVRHCY GCGVVHRDIK DENLLVDLRT
     GELKLIDFGS GALLKDTVYT DFDGTRVYSP PEWIRYHRYH GRSATVWSLG VLLYDMVCGD
     IPFEQDEEIL RGRLYFRRRI SPECQQLIKW CLSLRPSDRP TLEQIFDHQW MHKSEVVKSE
     DCDIRLRTLD TDVSSTSSSN ESL