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Database: UniProt
Entry: A0A091DDS9_FUKDA
LinkDB: A0A091DDS9_FUKDA
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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
//
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