Y9847_DICDI
ID Y9847_DICDI Reviewed; 2230 AA.
AC Q55GG4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0267686;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0267686;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 -!- 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;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73296.1; -; Genomic_DNA.
DR RefSeq; XP_647220.1; XM_642128.1.
DR AlphaFoldDB; Q55GG4; -.
DR SMR; Q55GG4; -.
DR STRING; 44689.DDB0229847; -.
DR PaxDb; Q55GG4; -.
DR EnsemblProtists; EAL73296; EAL73296; DDB_G0267686.
DR GeneID; 8616024; -.
DR KEGG; ddi:DDB_G0267686; -.
DR dictyBase; DDB_G0267686; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_230907_0_0_1; -.
DR InParanoid; Q55GG4; -.
DR OMA; KFAIEMV; -.
DR PRO; PR:Q55GG4; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
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:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50132; RGS; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..2230
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0267686"
FT /id="PRO_0000355158"
FT DOMAIN 991..1119
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 1949..2208
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1725..1771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1802..1848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1905..1929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2069
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1955..1963
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1976
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 2230 AA; 246462 MW; 518A0F5758542392 CRC64;
MEPNNNISNS NNGGSGIDGD GKEDSIYSYG YSSTTNSYNG VGNNSNLDKD DLDVFSLLDS
ITNTSYLLKP PPKIQKPPSP FSYPIELDQE EASLKEQELK LLELRLELQN TIIANSLINN
NNNSNNNNND NNNNNNNNNN NNNNNNNIQL NNSSLTPPII NISLPTTPST VNLTPKKPNL
YINTKLPNEN DDIIITPIVP LSGTITPPIP VDSPISFAET EQIIVVPQLQ LLDEIINTTD
NIGGGAAEKL QNIDPEIIIK LETEIKISSD EKENKEGGQV ENKEEKEKLD QKLENENENE
KVKEKEKEDE KEEQQVKVKE KEKEKENENE KNHNDKNDDD DDDEDNEKDK ISKTTVSVSI
KVSNENTPII NATDSSSNSI NSSSNNSIAT TPGRLSSSGL INHKKYDEFI EPTFFLSTAS
IGLNRLKSSN GASGSNSGNV SPSGPTPILS TLFQKNNSKQ DLLKNSSENS FCNNNNNNNN
NNNNNNNNNN NNNNNNNNSN NSNINNNNNN NSSNNNNNNN NNNNNNNNNN NNNNNNNNNN
NNNNNNNNNN NNNNINGFST IKSSSSSSPT NSPSSSLNIM NFFNTGSISS IVGSGSSSLG
KGSSKKIKDS YSNNNNNSST ADLSEQVLLA NMDNPFSSIP GRIKKNLDRR GATIANPQQL
TSLIKSGNTA KLQKFFGLEK EDLLAVNIIQ QQQLQLQHQH QQHQQAHQHQ HQQQQQHQQQ
LKSRSNTTNT PLMMFSVSEN NSPNNSPPVS PPSSPMLSPL SSSPPSWISG TSPARKLRGR
AATGSLLSGS SSNNNTTTTT TTTTSNSNSL SNNNRSNSFV DSRPFLPPVK TMPNIGGGQY
NTTPPLLPSQ TGDHVVKTPK DYHRKPKLLI AKLLKNNSLY MEKEKEKEKE KEKNESSKLD
IKNFAASGGQ LSLSSNQIIS NNSNSSSNNN NNNNNNNNNN NNNNNGLSNN IVINNSNNNS
NNNSASSSPT SSNSGYLNES NFILSSSSKE SLSALMKDRI GYDLFKIFCK ELVNKQGTNL
VNILLFIEEV ESFQSGIFNT DQLVLEETDR IFYKFILEST AAEFDINIPK RYFYQINHHI
KEKIPNKYVF EKVLKALKDE TSADAFKRFC ILHSTTNGTS APTNSTTIHS PSLAVPLSSS
SWNGLSKETS NSLVNNNTTP NTSTASPSIT ASSSSTSINN NTTTATATTV TTPVIVHQRH
HSSTVSGHYG GHRNHLQHVK LSHSNSPSPS SSPPDSYTSN QPLIFNGSPL GVSGSDYSFN
KFGNNSLVPP NLNISQASGG GSGNSNNNNN NELIINIKGL SPPTSHISSP PLSPRLSMIR
PHFTNGSMKS SLFQQQLQPT GSINSSPINN HQVSGGCGGD QTTELQTETL DDFIPHGVAF
GFKRGACKPP CDCLTYQSEG DKGGACLNCG HYPALHKNLG KISNSNNSID IDSLQQQQQH
QQIHHQSNLL PNTLLNLSNV TMASGALSPS TLNQQQHQIL QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QHQQHQQFQP NPSPSPPLTP SSNSIIQPSQ QQQPQQIVNT LINSSSDNTL
VLPTIPNITN TPPSPTQTLP LPSSSSSSLV IPNSNINSSP TSPSLSYNNN SNSNSNAGVG
SIPLSFNEIV NSNNSPNINN NGIINTSSNN NINNTNASIN GSANQLFNNP MTFSGNEIVL
PPIVQSSGGS LFTDSPLSSP KRIHFHNGIG NGDLLNNRAV LHSTVSNNNN INSNNNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNSNNNNG NDSLAILQKL IANGGSLKNA IYSLNNRSNS
SNNLMSNNNI NNSNIPNRLL NNRSNSSNSL MSSNNKNNYN NYNSNNNHIY SNEELTEIHQ
QQQLQQQQQQ QQQLQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQENNTTT TTTTTSNRPF
RSNNPTISQE LDTKVLMNFN NWAIDGEEIV FLNKLGEGTS AKVYRATWRN QEVAVKVLRS
EPESQKLLDF LKELEIMSSL RSPHVVYFYG MVLDPKICMI MEYCSNQTLY HLMHLQMNFT
WDWVFKFAIE MVRGVNCLHS WKPVIVHRDL KSLNLLVSDN WTIKVADFGL SRFATAKSAS
NRTTRGTFAY CAPEVFYGIH TTKGDIFSIG IILWELAVRC IKSKYEKPFS EFKHIQYDFQ
ILVQTSKFNL RPTIPQNCPE AFSNLISNCW ESSPDNRPSC PEILDSLLDM EKKYTENKRK
WDKIREKPKK
