Y8642_DICDI
ID Y8642_DICDI Reviewed; 1078 AA.
AC Q55F45;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0268642;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0268642;
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. Ser/Thr protein
CC kinase family. GCN2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000004; EAL72910.1; -; Genomic_DNA.
DR RefSeq; XP_646825.1; XM_641733.1.
DR AlphaFoldDB; Q55F45; -.
DR STRING; 44689.DDB0229432; -.
DR PaxDb; Q55F45; -.
DR EnsemblProtists; EAL72910; EAL72910; DDB_G0268642.
DR GeneID; 8616508; -.
DR KEGG; ddi:DDB_G0268642; -.
DR dictyBase; DDB_G0268642; -.
DR eggNOG; KOG1033; Eukaryota.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_286598_0_0_1; -.
DR InParanoid; Q55F45; -.
DR OMA; QYCEGKT; -.
DR Reactome; R-DDI-1169408; ISG15 antiviral mechanism.
DR Reactome; R-DDI-381042; PERK regulates gene expression.
DR PRO; PR:Q55F45; -.
DR Proteomes; UP000002195; Chromosome 1.
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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 3.
DR SMART; SM00220; S_TKc; 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.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1078
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0268642"
FT /id="PRO_0000362065"
FT DOMAIN 379..1031
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 31..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..507
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..626
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 796
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 385..393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1078 AA; 120092 MW; B2A4EAC68DC5F571 CRC64;
MINSLLEEES TAFAQVVRGI AISSDDYLKN DNIPKVNNNN NNNNNNNNNS NSNNNSSSND
YFNGRYNLVH SSVSIPSFDN FNFNSINSNN GNGNNSNSNS NSNSNSNSNS NSNSNSNSRD
EENERLRSEY KKIIKNNTSK LELTRSKSRI LVINSNSGEE EEEEEEVKTP TEVDSDNNNN
NNGSINKTNK KLKNHGNIVL SKSKSFIDTI DAMELVESCD DLFKQKKILL KMLISENFFQ
SNQLDQKKLS TFMKSVVDIE LMGVPSNILR SSQFKSLYLD YYRELFQNAL NVTNLKLGEN
NKVFGGGSDN NNNPLAIYQK PIKKEGSFLI DSSFFSNFYQ YQQLQQYQFL QQQQQQQQQQ
QKALPSSTFG NILRYQREFK EISKLGSGGF GSVYLSEYVL DGHKYAIKKV NFSISNNQSP
TNASSKIEKV VREVVALAKL DHINILRYHN AWLELDPKNN KPRSSSFSSV EGSLGTGNND
NDESDDSFFE DQDEDEDEDE DEDDVSNSNF SDSIKFKGGF KKSSCSNNSI SSNLKKKRND
KKYPFKRNLS ISFSLNDSVT NTNSQEYSIS EYFEKFNLTN NSESDESEIE ESDSDEIYSE
SESEESESEE SESDESEESE SDSDNIDFEN ENIKEMIKAL TISKSMIPFV KPIKKKKGKI
YNPSSGSGAS SGSGNSSSIG DSDSSEGNKP KGLTLSTKQL SNSQLIGINN LNNNNNNRNN
NNNNNNRNND KNSNSNNLRL KYTVYIQTQY CEGKTLRDLL ENPDFKNNSK TTILSLFKQI
ITGVNYIHSM GMIHRDLKPA NLFLSSGVIK IGDFGLVKDI TATTPSTTPL TNNTPSTTPI
DTTPTSSANT IPISTPPTST ITPTISVSPS KPLSSSLSST AATTHLNSSL GCTISSSSST
TTATATTSTT PFMFYNSISV NTVGVGTLTY ASPEQLSNKG VFGGGGYTNT WYTNKTDIYS
CGIILFEMIV GGFETQFERT THIKNLKNGI LPSWFTSKHP EESNLILRMI DINPDNRPTS
DQILSELLPI LIEASERDID HFDYEKLDQQ TLISIIKKKD LEIASLKKLL QNTGNNNK
