ID G7PMU6_MACFA Unreviewed; 1312 AA.
AC G7PMU6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=EGM_05061 {ECO:0000313|EMBL:EHH55791.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH55791.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH55791.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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DR EMBL; CM001288; EHH55791.1; -; Genomic_DNA.
DR eggNOG; KOG0587; Eukaryota.
DR Proteomes; UP000009130; Chromosome 13.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 16..280
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 999..1286
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 297..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..328
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..862
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1312 AA; 150299 MW; 8ACE2A3CF90FB41D CRC64;
MITPPLLPLQ DPAGIFELVE VVGNGTYGQV YKGRHVKTGQ LAAIKVMDVT EDEEEEIKLE
INMLKKYSHH RNIATYYGAF IKKSPPGHDD QLWLVMEFCG AGSITDLVKN TKGNTLKEDW
IAYISREILR GLAHLHIHHV IHRDIKGQNV LLTENAEVKL VDFGVSAQLD RTVGRRNTFI
GTPYWMAPEV IACDENPDAT YDYRSDLWSC GITAIEMAEG APPLCDMHPM RALFLIPRNP
PPRLKSKKWS KKFFSFIEGC LVKNYTQRPS TEQLLKHPFI RDQPNERQVR IQLKDHIDRT
RKKRGEKDET EYEYSGSEEE EEEVPEQEGE PSSIVNVPGE STLRRDFLRL QQENKERSEA
LRRQQLLQEQ QLREQEEYKR QLLAERQKRI EQQKEQRRRL EEQQRREREA RRQQEREQRR
REQEEKRRLE ELERRRKEEE ERRRAEEEKR RVEREQEYIR RQLEEEQRHL EVLQQQLLQE
QAMLLECRWR EMEEHRQAER LQRQLQQEQA YLLSLQHDHR RPHPQHSQQP PPPQQERSKP
SFHAPEPKVH YEPADRAREV EDRFRKTNHS SPEAQSKQTG RVLEPPVPSR SESFSNGNSE
SVHPALQRPA EPQVQWSHLA SLKNNVSPVS RSHSFSDPSP PKFAHHHLRS QDPCPPSRSE
VLSQSSDSKS ETPDPTQKAW SRSDSDEVPP RVPVRTTSRS PVLSRRDSPL QGSGQQNSQA
GQRNSTSSIE PRLLWERVEK LVPRPGSGSS SGSSNSGSQP GSHPGSQSGS GERFRVRSSS
KSEGSPSQRL ENAVKKPEDK KEVFRPLKPA VRIDLTALAK ELRAVEDVRP PHKVTDYSSS
SEESGTTDEE DDDVEQEGAD ESTSGPEDTR AASSLNLSNG ETESVKTMIV HDDVESEPAM
TPSKEGTLIV RQTQSASSTL QKHKSSSSFT PFIDPRLLQI SPSSGTTVTS VVGFSCDGMR
PEAIRQDPTR KGSVVNVNPT NTRPQSDTPE IRKYKKRFNS EILCAALWGV NLLVGTESGL
MLLDRSGQGK VYPLINRRRF QQMDVLEGLN VLVTISGKKD KLRVYYLSWL RNKILHNDPE
VEKKQGWTTV GDLEGCVHYK VVKYERIKFL VIALKSSVEV YAWAPKPYHK FMAFKSFGEL
VHKPLLVDLT VEEGQRLKVI YGSCAGFHAV DVDSGSVYDI YLPTHIQCSI KPHAIIILPN
TDGMELLVCY EDEGVYVNTY GRITKDVVLQ WGEMPTSVAY IRSNQTMGWG EKAIEIRSVE
TGHLDGVFMH KRAQRLKFLC ERNDKVFFAS VRSGGSSQVY FMTLGRTSLL SW
//
