ID A0A2K5ZJC8_MANLE Unreviewed; 1659 AA.
AC A0A2K5ZJC8;
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:ENSMLEP00000027880.1};
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:ENSMLEP00000027880.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000027880.1}
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: Cell projection, lamellipodium
CC {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm
CC {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}.
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DR Ensembl; ENSMLET00000051432.1; ENSMLEP00000027880.1; ENSMLEG00000036737.1.
DR GeneTree; ENSGT01030000234517; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; 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:0007010; P:cytoskeleton organization; IEA:UniProt.
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; 1.20.5.340; -; 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; IPR031597; KELK.
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; PF15796; KELK; 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}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
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..1659
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014358895"
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 939..989
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1009..1128
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1154..1426
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1498..1511
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 904..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1519..1659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 404..632
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 678..783
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 849..904
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1529..1576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1584..1603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1659
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 1659 AA; 188646 MW; 8D901BAC08445F0C 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 NKELVQASER LKNQSKELKD AHCQRKLAMQ
EFMEINERLT ELHTQKQKLA RHVRDKEEEV DLVMQKVESL RQELRRTERA KKELEVHTEA
LAAEASKDRK LREQSEHYSK QLENELEGLK QKQISYSPGI CSIEHQQEIT KLKTDLEKKS
VFYEEELSKR EGIHANEIKN LKKELHDSEG QQLALNKEIL ILKDKLEKNR RESQSEREEF
ESEFKQQYER EKVLLTEENK KLTSELDKLT TLYENLSIHN QQLEEEVKDL ADKKESVAHW
EAQITEIIQW VSDEKDARGY LQALASKMTE ELEALRNSSL GTRATDMPWK MRRFAKLDMS
ARLELQSALD AEIRAKQAIQ EELNKVKASN IITECKLKDS EKKNLELLSE IEQLIKDTEE
LRSEKGMGTV DSTPLPVHTP TLRKKGCPGS TGFPLKRKTH QFFVKSFTTP TKCHQCTSLM
VGLIRQGCSC EVCGFSCHIT CVNKAPTTCP VPPEQTKGPL GIDPQKGIGT AYEGHVRIPK
PAGVKKGWQR ALAIVCDFKL FLYDIAEGKA SQPSVVISQV IDMRDEEFSV SSVLASDVIH
ASRKDIPCIF RVTASQLSAS NNKCSILMLA DSENEKSKWV GVLSELHKIL KKNKFRDRSV
YVPKEAYDST LPLIKTTQAA AIIDHERIAL GNEEGLFVVH VTKDEIIRVG DNKKIHQIEL
IPNDQLVAVI SGRNRHVRLF PLSALDGRET DFYKLAETKG CQTITSGKVR HGALTCLCVA
MKRQVLCYEL FQSKTRHRKF KEIQVPYNVQ WMAIFSEQLC VGFQSGFLRY PLNGEGSPYS
MLHSNDHTLS FIAHQPMDAI CAVEISSKEY LLCFNSIGIY TDCQGRRSRQ QELMWPANPS
SCCYNAPYLS VYSENAVDIF DVNSMEWIQT LPLKKVRPLN NEGSLNLLGL ETIRLIYFKN
KMAEGDELVV PETSDNSRKQ MVRNINNKRR YSFRVPEEER MQQRREMLRD PEMRNKLISN
PTNFNHIAHM GPGDGIQILK DLPMNPRPQE SRTVFSGSVS IPSITKSRPE PGRSMSASSG
LSARSSAQNG SALKREFSGG SYSAKRQPMP SPSEGSLSSG GMDQGSDAPA RDFDGEDSDS
PRHSTASNSS NLSSPPSPVS PRKTKSLSLE STDRGSWDP
//
