ID A0A091DDS9_FUKDA Unreviewed; 1544 AA.
AC A0A091DDS9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=H920_10296 {ECO:0000313|EMBL:KFO28435.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO28435.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO28435.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO28435.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KN122776; KFO28435.1; -; Genomic_DNA.
DR STRING; 885580.ENSFDAP00000022169; -.
DR eggNOG; KOG0612; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20866; C1_MRCKgamma; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR CDD; cd05597; STKc_DMPK_like; 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:SF22; SERINE/THREONINE-PROTEIN KINASE MRCK GAMMA; 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; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFO28435.1};
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:UP000028990};
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 71..337
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 338..408
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT DOMAIN 874..923
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 943..1062
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1088..1362
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1433..1446
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 462..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 627..672
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 745..793
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1472..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1544 AA; 171622 MW; A908A1397E2DE10E CRC64;
MEQRLRALEQ LVRGEAGSDP GLDGLLDLLL GLHHELSSAP LRRERNVAQF LSWATPFVKK
VKELRLQRDD FEILKVIGRG AFGEVAVVRQ RDNGQIFAMK MLHKWEMLKR AETACFREER
DVLVKGDSRW VTTLHYAFQD EEYLYLVMDY YAGGDLLTLL SRFEDRLPPE LAQFYLAEMV
LAIDSLHQLG YVHRDVKPDN ILLDMNGHIR LADFGSCLRL NNSGMVDSSV AVGTPDYISP
EILQAMEEGQ GHYGPQCDWW SLGVCAYELL FGETPFYAES LVETYGKIMN HEDHLQFPSD
MPDVPASAQD LIRQLLCRQE ERLGRGGLDD FRNHPFFEGV DWEQLASSTA PYIPELQGPV
DTSNFDVDDD TLNHPDTLPP PSHGSFSGHH LPFIGFTYTS GRPESSSEVA AAREWKLRCW
EEEKVELSWE CQGDPSDHQE LARLQKEVET LRERLAEMLR DSKASLSQRD ESPADSPGQV
SDLQLEKSQL QQELAEVQAG LQAQAQELCR AQSLQEELLL RLREAQEKEA ATTSQIQALS
SQLEEVWNVR KELENQVAFL SQELTRLQGQ ERSLEKDSSQ TKTDHVAPET NGPGSSEVGA
HEAQLIKEVA ALREQLEQAC RCGPSGKEEA LCQLREENQR LSREQERLAE ELEQELQSKQ
RLEGERRETE SNWEAQITDI LSWVNDEKVS RGYLQALATK MAEELESLRN VGTQTITTRP
LDHQWKARRL QKMEASARLE LQSALDAEIR AKQGLQERLT QVQEAQLQAE RRLEEAEKQN
QALQQELAAL REELRGRGPG DAKPSNSLIP FLSFRSTEKD SAKDSGISGD TPRPGAEPEL
KPEGRRSLRM GAVFPWVPAV TATPAEGPPA KPGSHTLRPR SFPSPTKCLC CTSLMLGLGR
QGLGCDACGF FCHSTCAPQA PLCPTPPDHL RTALGVHPET GTGTAYEGFL SVPRPSGVRR
GWQRVYAALS DSRLLLFDAP DPRASPASTA LLQALDVRDP QFSATPVLAS DVIHAQSRDL
PRIFRVTASQ LTVPPTMCTV LLLAESKGER ERWLQVLGEL QRLLLEARPR PRPVYTLKEA
YDNGLPLLPH TLCAAVIDQE RLALGTEEGL FVIHLHSNDI FQVGECRRVQ QLALSPSAGL
LVVLCGRGPS VRLFALTELE STEVAGAKIP ESRGCQVLAA GRILQARTPV LCVAVKRQVL
CYQLGPGPGP WQRRIRELQA PAPVQSLGLL GDRLCVGAAG AFALYPLLNE AAPLALGAGL
VPEELPPSRG GLGEALGAVE LSLNELLLLF TTAGVYVDGA GRKSRSHELL WPVAPIGWGY
TAPYLTVFCE NSIDVFDVRR AEWVQTVPLK KVRPLNAEGS LFLYGTEKVR LTYLRNLLAE
KDEFNIPDLT DNSRRQLFRT KSKRRFFFRV SDEQRTQQRR EMLKDPFVRS KLISPPTNFN
HLVHVGPNDG RPSARAPEEK GRGARGSGPQ RPHSFSEASR LSASMGSGSL PKDADSTVKR
KPWTSLSSES VSCPQGSLSP AASLIKVSER PRSLPPAPES ESSP
//