ID G8F2B6_MACFA Unreviewed; 1737 AA.
AC G8F2B6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN ORFNames=EGM_19782 {ECO:0000313|EMBL:EHH61430.1};
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 {ECO:0000313|Proteomes:UP000009130};
RN [1] {ECO:0000313|EMBL:EHH61430.1, ECO:0000313|Proteomes:UP000009130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH61430.1,
RC ECO:0000313|Proteomes:UP000009130};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00009903}.
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DR EMBL; JH329992; EHH61430.1; -; Genomic_DNA.
DR eggNOG; KOG0606; Eukaryota.
DR Proteomes; UP000009130; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR015022; MAST_pre-PK_dom.
DR InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24356:SF136; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 2; 1.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR Pfam; PF08926; DUF1908; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50106; PDZ; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 454..727
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 728..796
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 1046..1134
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 114..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1009..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1137..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1189..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1359..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1606..1662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1288..1303
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1567..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHH61430.1"
FT NON_TER 1737
FT /evidence="ECO:0000313|EMBL:EHH61430.1"
SQ SEQUENCE 1737 AA; 189444 MW; 8206768519693276 CRC64;
KDVVTGLSPL LFRKLSNPDI FSSTGKVKLQ RQLSQDDCKL WRGNLASSLS GKQLLPLSSS
VHSSVGQVTW QSSGEASNLV RMRNQSLGQS APSLTAGLKE LSLPRRGSFC RTSNRKSLIV
TSSTSPTLPR PHSPLHGHTG NSPLDSPRNF SPNAPAHFSF VPARRTDGRR WSLASLPSSG
YGTNTPSSTV SSSCSSQEKL HQLPFQPTAD ELHFLTKHFS TESVPDEEGR QSPAMRPRSR
SLSPGRSPVS FDSEIIMMNH VYKERFPKAT AQMEERLAEF ISSNTPDSVL PLADGALSFI
HHQVIEMARD CLDKSRSGLI TSQYFYELQE NLEKLVQDAH ERSESSEVAF VMQLVKKLMI
VIARPARLLE CLEFDPEEFY HLLEAAEGHA KEGQGIKCDI PRYIVSQLGL TRDPLEEMAQ
LSSCDSPDTP ETDDSIEGRG ASLPSKKTPS EEDFETIKLI SNGAYGAVFL VRHKSTRQRF
AMKKINKQNL ILRNQIQQAF VERDILTFAE NPFVVSMFCS FETKRHLCMV MEYVEGGDCA
TLLKNIGALP VDMVRLYFAE TVLALEYLHN YGIVHRDLKP DNLLITSMGH IKLTDFGLSK
IGLMSLTTNL YEGHIEKDAR EFLDKQVCGT PEYIAPEVIL RQGYGKPVDW WAMGIILYEF
LVGCVPFFGD TPEELFGQVI SDEIVWPEGD DALPPDAQDL TSKLLHQNPL ERLGTGSAYE
VKQHPFFTGL DWTGLLRQKA EFIPQLESED DTSYFDTRSE RYHHMDSEDE EEVSEDGCLE
IRQFSSCSPR FSKVYSSMER LSLLEERQTP PPTKRSLSEE KEDRSDGLAG LKGRDRSWVI
GSPEILRKRL SVSESSHTES DSSPPMTVRR RCSGLLDAPR FPEGPEEASS ALRRQPQEGI
WVLTPPSGEG ASGPVAERPG EQRPKLDEEA VGRSSGSSPA METRGRGTPQ LAEGATAKAI
SDLAVRRARH RLLSGDSTEK RTTRPVNKVI KSASATALSL LIPSEHHTCS PLASPMSPHS
QSSNPSSRDS SPSRDFLPAL GSVRPPIIIH RAGKKYGFTL RAIRVYMGDS DVYTVHHMVW
HVEDGGPASE AGLRQGDLIT HVNGEPVHGL VHTEVVELIL KSGNKVAIST TPLENTSIKV
GPARKGSYKA KMARRSKRGR GKDGQESRKR SSLFRKIAKQ VSLLHTSRSL SSLNRSLSSG
ESGPGSPTHS HSLSPRSPTQ GYRVTPDAVH SVGGNSSQSS SPSSSVPSSP AGSGHTRPSS
LHGLAPKLQR QYRSPRRKSA GSIPLSPLAH TPSPPPPAAS PQRSPSPLSG HVAQAFPTKL
HLSPPLGRQL SRPKSAEPPR SPLLKRVQSA EKLAAALAAS EKKLATSRKH SLDLPHSELK
KELPPREVSP LEVVGARGVL SGKGALPGKG VLQPAPSRAL GTLRQDRAER RESLQKQEAI
REVDSSEDDT EEGPENSQGA QELSLAPHPA VSQSVAPKGT EESGEEETFP SRDPRSLGPV
VPSLLTGITL GPPRRESPSG PHRRLGSPQA VEEAASSSSP GPNLGRSGAT DPIPSEGCWK
AQHLHTQALA ALSSSTSGLT PTSSCSPPSS TSGKLGMWSW KFHIEGPDRA SPSRKATMAG
GLVNLQDLET TTPAHPKNLS PREQGKTQPP SARPPCEDPS QGWLWESECA QAVKEDPALS
ITQVPDASGD RRQDVPCQGC PLTQESESSL LWRGQEPGGH QKHRDLALVP DELLKQT
//
