Y0652_DICDI
ID Y0652_DICDI Reviewed; 637 AA.
AC Q54RP7;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0283065;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0283065;
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; AAFI02000049; EAL65976.1; -; Genomic_DNA.
DR RefSeq; XP_639304.1; XM_634212.1.
DR AlphaFoldDB; Q54RP7; -.
DR SMR; Q54RP7; -.
DR STRING; 44689.DDB0220652; -.
DR PaxDb; Q54RP7; -.
DR EnsemblProtists; EAL65976; EAL65976; DDB_G0283065.
DR GeneID; 8623875; -.
DR KEGG; ddi:DDB_G0283065; -.
DR dictyBase; DDB_G0283065; -.
DR eggNOG; KOG1035; Eukaryota.
DR HOGENOM; CLU_429895_0_0_1; -.
DR InParanoid; Q54RP7; -.
DR OMA; TTHINDE; -.
DR PhylomeDB; Q54RP7; -.
DR PRO; PR:Q54RP7; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..637
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0283065"
FT /id="PRO_0000362040"
FT DOMAIN 236..629
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 36..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 479
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 242..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 637 AA; 70252 MW; 757E65CEC27E4B46 CRC64;
MWKFTSSATK RIGNSLSSNN NNGSLLFSLN FNGSNNNNNN ESSKPITAAN TQNNSTTKSI
DNNNNNTNNS NSNNNNNDNI KNNNKFNRAS HRSNITLVAI NNKDISQMTN LLADSGISVS
KISNKKISLA SKINTLNKLN SSLLHLNSIN NSLTNSNNNN DNNNLIDNNN NDNYNNDSIS
SSSSSSSLSE SSQTLSSASS SASSSSSSTL SSSSSVSSKS LNNNNNNNNS RFNNEFNDVR
VLGKGGFGIV FQCCNIFDQM EYAVKRIKVN QKIPTKELME VRAMARLNHP NIVRYYGSWI
EEEIITNNSI DHYGENDNNL FENIDSFPSS SYSSVSAAAS SSSLVSNSSN SYSNNKATYI
SNSSSSSSSS SSCSYSIGNG NLSISECTND DNNNYNQLKQ KKFSLYIQME LCKYSTLRNL
INEINNIKSI TSIQSTSSIA NPIGTNILIS LDIKQCREIT RQILVALKYI HSQGFVHRDI
TPDNVFVCQS PFGIKIGDFG LATTIESLTV DSNNNNNNNI NNNNNNNKKV GGLGTYLYSS
NEQEQGDNYN QKTDLYSVGV IFFEMLSQFK TTMERSTTLS KLKKSLSVLK TNPNLKQKYP
NDTDFIDHLI QSFATRPFSN QISTDYDNFP PKNFLIN
