ID L9JK71_TUPCH Unreviewed; 899 AA.
AC L9JK71;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=TREES_T100003325 {ECO:0000313|EMBL:ELW49542.1};
OS Tupaia chinensis (Chinese tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW49542.1, ECO:0000313|Proteomes:UP000011518};
RN [1] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhang G., Fan Y., Yao Y., Huang Z.;
RT "Genome of the Chinese tree shrew, a rising model animal genetically
RT related to primates.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000011518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23385571; DOI=10.1038/ncomms2416;
RA Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT "Genome of the Chinese tree shrew.";
RL Nat. Commun. 4:1426-1426(2013).
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};
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DR EMBL; KB320992; ELW49542.1; -; Genomic_DNA.
DR AlphaFoldDB; L9JK71; -.
DR STRING; 246437.L9JK71; -.
DR eggNOG; KOG0612; Eukaryota.
DR InParanoid; L9JK71; -.
DR Proteomes; UP000011518; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR031597; KELK.
DR InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF31; SERINE_THREONINE-PROTEIN KINASE MRCK ALPHA; 1.
DR Pfam; PF08826; DMPK_coil; 1.
DR Pfam; PF15796; KELK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ELW49542.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011518};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 125..204
FT /note="KELK-motif containing"
FT /evidence="ECO:0000259|Pfam:PF15796"
FT DOMAIN 477..507
FT /note="Myotonic dystrophy protein kinase coiled coil"
FT /evidence="ECO:0000259|Pfam:PF08826"
FT REGION 641..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 78..265
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 311..416
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 641..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 101800 MW; FAF279074BF45664 CRC64;
MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE KNILEYLEWE
STQTVQALQY STVDGPLTAS KDLEIKNLKE EIEKLRKQIT EMSHLEQQLE EANSVRRELD
DAFRQIKAYE KQIKTLQQER EDLNKELVQA SERLKNQSKE LKDAHCQRKL AMQEFMEINE
RLTELHTQKQ KLARHVRDKE EEVDLVMQKV ESLRQELRRT ERAKKEVSIH TEALAAEASK
DRKLREQSEH YSKQLENELE GLKQKQISYS PGICSIEHQQ EITKLKTDME KKSIFYEEEL
SKREGIHANE IKNLKKELHD SEGQQLALNK EIMILKDKLE KTRRESQSER EEFENEFKQQ
YEREKVLLTE ENKKLTSELD KLTTLYENLS IRNQHLEEEV KDLADKKESV AHWEAQITEI
IQWVSDEKDA RGYLQALASK MTEELEALRN SSLGTRATDM PWKMRRFAKL DMSARLELQS
ALDAEIRAKQ AIQEELNKVK ASNIITEWDE DFSVSSVLAS DVIHASRKDI PCIFRVTASQ
LSASSSKCSI LMLADSENER SKWVGVLNEL HKILKKNKFR DRSVYVPKEA YDSTLPLIKT
TQAAAIIGYN APYLSVYSEN AVDIFDVNSM EWIQTLPLKK NPRPQESRTV FSGSVSIPSI
TKSRPEPGRS MSASSGLSAR SSAQNGSALK REFSGGSYSA KRQPMPSPSE GSLSSGGMDQ
GSDAPARDYD GEGKLRCHLT RMQGPRQALS PALAEARQSE HAAPVGGNLT WLQLQETRSV
VAFPPPLRAR SSHSAPHAPR ICLPTSQSPG GPARLAPPYG DPIGCVSDTG RTPRGVEERA
RPVLPAHSQS EPRAERTEPM GGRPSGRAQV FPFHLPEALF PSYESSAEGQ AVGPRACAL
//