ID G7PBP1_MACFA Unreviewed; 1610 AA.
AC G7PBP1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHH63908.1};
DE Flags: Fragment;
GN ORFNames=EGM_16980 {ECO:0000313|EMBL:EHH63908.1};
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:EHH63908.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH63908.1};
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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DR EMBL; CM001282; EHH63908.1; -; Genomic_DNA.
DR eggNOG; KOG0612; Eukaryota.
DR Proteomes; UP000009130; Chromosome 7.
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: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; cd20865; C1_MRCKbeta; 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; IPR020454; DAG/PE-bd.
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:SF34; SERINE_THREONINE-PROTEIN KINASE MRCK BETA; 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 PRINTS; PR00008; DAGPEDOMAIN.
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 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 18..284
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 285..355
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 967..1017
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1037..1156
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1182..1455
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1525..1538
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 403..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1553..1610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 668..749
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 825..880
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 403..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHH63908.1"
FT NON_TER 1610
FT /evidence="ECO:0000313|EMBL:EHH63908.1"
SQ SEQUENCE 1610 AA; 183205 MW; 4CD0D0F8C0DD291A CRC64;
AKPFTQLVKE MQLHREDFEI IKVIGRGAFG EVAVVKMKNT ERIYAMKILN KWEMLKRAET
ACFREERDVL VNGDCQWITA LHYAFQDENH LYLVMDYYVG GDLLTLLSKF EDKLPEDMAR
FYIGEMVLAI DSIHQLHYVH RDIKPDNVLL DVNGHIRLAD FGSCLKMNDD GTVQSSVAVG
TPDYISPEIL QAMEDGMGKY GPECDWWSLG VCMYEMLYGE TPFYAESLVE TYGKIMNHEE
RFQFPSHVTD VSEEAKDLIQ RLICSRERRL GQNGIEDFKK HAFFEGLNWE NIRNLEAPYI
PDVSSPSDTS NFDVDDDVLR NTEILPPGSH TGFSGLHLPF IGFTFTTESC FSDRGSLKSI
MQSNTLTKDE DVQRDLEHSL QMEAYERRIR RLEQEKLELS RKLQESTQTV QSLHGSSRAL
SNSNRDKEIK KLNEEIERLK NKIADSNRLE RQLEDTVALR QEREDSTQRL RGLEKQHRVV
RQEKEELHKQ LVEASERLKS QAKELKDAHQ QRKLALQEFS ELNERMAELR AQKQKVSRQL
RDKEEEMEVA TQKVDAMRQE MRRAEKLRKE LEAQLDDAVA EASKERKLRE HSENFCKQME
SELEALKMKQ GGRGAGATLE HQQEISKIKS ELEKKVLFYE EELVRREASH VLEVKNVKKE
VHDSESHQLA LQKEILMLKD KLEKSRRERH NEMEEAVGTI KDKYERERAM LFDENKKLTA
ENEKLCSFVD KLTAQNRQLE DELQDLAAKK ESVAHWEAQI AEIIQWVSDE KDARGYLQAL
ASKMTEELEA LRSSSLGSRT LDPLWKVRRS QKLDMSARLE LQSALEAEIR AKQLVQEELR
KVKDANLTLE SKLKDSEAKN RELLEEMEIL KKKMEEKFRA DTGLKLPDFQ DSIFEYFNTA
PLAHDLTFRT SSASEQETQA PKPETSPSMS VAASEQQEDM ARPPQRPSAV PLPTTQALAL
AGPKPKAHQF SIKSFSSPTQ CSHCTSLMVG LIRQGYACEV CSFACHVSCK DSAPQVCPIP
PEQSKRPLGV DVQRGIGTAY KGHVKVPKPT GVKKGWQRAY AVVCDCKLFL YDLPEGKSTQ
PGVIASQVLD LRDDEFSVSS VLASDVIHAT RRDIPCIFRV TASLLGAPSK TSSLLILTEN
ENEKRKWVGI LEGLQSILHK NRLRNQVVHV PLEAYDSSLP LIKAVLTAAI VDADRIAVGL
EEGLYVIEVT RDVIVRAADC KKVHQIELAP REKIVILLCG RNHHVHLYPW SSLDGAEGSF
DIKLPETKGC QLMATATLKR NSGTCLFVAV KRLILCYEIQ RTKPFHRKFN EIVAPGSVQC
LAVLRDRLCV GYPSGFCLLS IQGDGQPLNL VNPNDPSLAF LSQQSFDALC AVELESEEYL
LCFSHMGLYV DPQGRRARAQ ELMWPAAPVA CSCSPTHVTV YSEYGVDVFD VRTMEWVQTI
GLRRIRPLNS EGTLNLLNCE PPRLIYFKSK FSGAVLNVPD TSDNSKKQML RTRSKRRFVF
KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG DGMQVLMDLP LSAVPPSQEE
RPGPAPTNLA RQPPSRNKPY ISWPSSGGSE PGVTVPLRSM SDPDQDFDKE
//
