ID A0A2K5ZJ89_MANLE Unreviewed; 1601 AA.
AC A0A2K5ZJ89;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=CDC42BPA {ECO:0000313|Ensembl:ENSMLEP00000027886.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000027886.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000027886.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. DMPK subfamily. {ECO:0000256|ARBA:ARBA00005719}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSMLET00000051438.1; ENSMLEP00000027886.1; ENSMLEG00000036737.1.
DR GeneTree; ENSGT01030000234517; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20864; C1_MRCKalpha; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF31; SERINE_THREONINE-PROTEIN KINASE MRCK ALPHA; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1601
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014462545"
FT DOMAIN 40..306
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 307..377
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 881..931
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 951..1070
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1096..1368
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1440..1453
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 1461..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..551
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 597..702
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 768..823
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1471..1518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1526..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1601 AA; 181520 MW; 6B6735B9AAFAB862 CRC64;
SLPVFICLYC SLLPGVSTQS NPAKPFTSKV KQMRLHREDF EILKVIGRGA FGEVAVVKLK
NADKVFAMKI LNKWEMLKRA ETACFREERD VLVNGDNKWI TTLHYAFQDD NNLYLVMDYY
VGGDLLTLLS KFEDRLPEDM ARFYLAEMVI AIDSVHQLHY VHRDIKPDNI LMDMNGHIRL
ADFGSCLKLM EDGTVQSSVA VGTPDYISPE ILQAMEDGKG RYGPECDWWS LGVCMYEMLY
GETPFYAESL VETYGKIMNH KERFQFPAQV TDVSENAKDL IRRLICSREH RLGQNGIEDF
KKHPFFSGID WDNIRNCEAP YIPEVSSPTD TSNFDVDDDC LKNSETMPPP THTAFSGHHL
PFVGFTYTSS CVLSDRSCLR VTAGPTSLDL DVNVQRTLDN NLATEAYERR IKRLEQEKLE
LSRKLQESTQ TVQALQYSTV DGPLTASKDL EIKNLKEEIE KLRKQVTELS HLEQQLEEAN
AVRQELDEAF RQIKAYEKQI KTLQQEREDL NKLEVHTEAL AAEASKDRKL REQSEHYSKQ
LENELEGLKQ KQISYSPGIC SIEHQQEITK LKTDLEKKSV FYEEELSKRE GIHANEIKNL
KKELHDSEGQ QLALNKEILI LKDKLEKNRR ESQSEREEFE SEFKQQYERE KVLLTEENKK
LTSELDKLTT LYENLSIHNQ QLEEEVKDLA DKKESVAHWE AQITEIIQWV SDEKDARGYL
QALASKMTEE LEALRNSSLG TRATDMPWKM RRFAKLDMSA RLELQSALDA EIRAKQAIQE
ELNKVKASNI ITECKLKDSE KKNLELLSEI EQLIKDTEEL RSEKGIEHQD SQHSFLAFLN
TPSDALDQFE TVDSTPLPVH TPTLRKKGCP GSTGFPLKRK THQFFVKSFT TPTKCHQCTS
LMVGLIRQGC SCEVCGFSCH ITCVNKAPTT CPVPPEQTKG PLGIDPQKGI GTAYEGHVRI
PKPAGVKKGW QRALAIVCDF KLFLYDIAEG KASQPSVVIS QVIDMRDEEF SVSSVLASDV
IHASRKDIPC IFRVTASQLS ASNNKCSILM LADSENEKSK WVGVLSELHK ILKKNKFRDR
SVYVPKEAYD STLPLIKTTQ AAAIIDHERI ALGNEEGLFV VHVTKDEIIR VGDNKKIHQI
ELIPNDQLVA VISGRNRHVR LFPLSALDGR ETDFYKLAET KGCQTITSGK VRHGALTCLC
VAMKRQVLCY ELFQSKTRHR KFKEIQVPYN VQWMAIFSEQ LCVGFQSGFL RYPLNGEGSP
YSMLHSNDHT LSFIAHQPMD AICAVEISSK EYLLCFNSIG IYTDCQGRRS RQQELMWPAN
PSSCCYNAPY LSVYSENAVD IFDVNSMEWI QTLPLKKVRP LNNEGSLNLL GLETIRLIYF
KNKMAEGDEL VVPETSDNSR KQMVRNINNK RRYSFRVPEE ERMQQRREML RDPEMRNKLI
SNPTNFNHIA HMGPGDGIQI LKDLPMNPRP QESRTVFSGS VSIPSITKSR PEPGRSMSAS
SGLSARSSAQ NGSALKREFS GGSYSAKRQP MPSPSEGSLS SGGMDQGSDA PARDFDGEDS
DSPRHSTASN SSNLSSPPSP VSPRKTKSLS LESTDRGSWD P
//
