Y1516_DICDI
ID Y1516_DICDI Reviewed; 965 AA.
AC Q54EG9;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0291516;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0291516;
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AAFI02000177; EAL61742.2; -; Genomic_DNA.
DR RefSeq; XP_635271.2; XM_630179.2.
DR AlphaFoldDB; Q54EG9; -.
DR STRING; 44689.DDB0231196; -.
DR PaxDb; Q54EG9; -.
DR EnsemblProtists; EAL61742; EAL61742; DDB_G0291516.
DR GeneID; 8628215; -.
DR KEGG; ddi:DDB_G0291516; -.
DR dictyBase; DDB_G0291516; -.
DR eggNOG; KOG4721; Eukaryota.
DR HOGENOM; CLU_306845_0_0_1; -.
DR InParanoid; Q54EG9; -.
DR PhylomeDB; Q54EG9; -.
DR PRO; PR:Q54EG9; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ANK repeat; ATP-binding; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..965
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0291516"
FT /id="PRO_0000362043"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 271..301
FT /note="ANK 1"
FT REPEAT 310..339
FT /note="ANK 2"
FT DOMAIN 459..739
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 114..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 587
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 465..473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 760
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 905
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 909
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 965 AA; 112249 MW; 4687BAF992763538 CRC64;
MDFKENSIYI NVMDKIYARE KEVLSQNQDF QENNLSRISL ILNYEDFSLK FDESLHGYSF
GYVTNPFGLK LHSPFTETVR FDGAEKYIYM KRILGVPSNE TQLCNYQHQN FEEKDSQKEL
LPSPQQLTPP TSLPSLPLLP LPQAPEQNEE QQLTQPPSPP SIPPPPPQKK QIQIFITPSG
IVSQKIQNFF RDTQIKSTDP VNCSLDHSIK KNYSLEEIYE NNKNYMDKNN NFLHFLFTFI
DKITIKDLDH FEKEINRVHN IKKLINQQNM KGETPLHSLI INNSESCLKK LVIAKINHMG
IFDYSKCDNL NKNLLAHAIE KGDIDVIRLV LIGGCPLKMS PRSKLFKKNF KIYRQQIYRV
FEIKEFLTKI GFNQYIPMFL EFEFKNININ YLIESFKFKL NINEDEILLW KLLTEPYKNL
DFKSFCSEYQ IKHQNDLISE TMANHFINVC QLNPHFGYID FHTQIGSAGN ASVFEGTYKG
IPIACKEMPV SGTYEQSVDS IKEIAAVGQI KKLGCATVVE TIGVLKYNQK LFLVMVKEKC
NLLSFLCNKS EILKMQREGI WTSIFKISKD ILKGLVSLRE AGMYHRDFKT ANFLVSNTGK
ILISDFGTSR DENEKRLNTF AKTIGTMWYR CPRLGDCSED EKTLTHYNEK SEIYSLGIIL
WELVCVAMTG TYISPKIPLF QNEVDFLIWI HKDYRFSFPV GTPQSFVKLI TRMCLPFRDR
RPTVRQVLDN VKAIKKEFLS NRGIEGEQTY SGLECWREFN FSKQNVTRIS ISNLHNTEYK
VVNKYDYASY NNKNSLLMKR YLDNSNFVVE LINPNGLFRF KSFFEKEKLL YLKLKSTYKD
EYYFDMSQFL TTIIQIHQIT VIYYKMLQKY RELRLLRNNN NINKNKNNNN NNNNNNNNNN
NINNNNTFNN STNNNSNDNI NIPYDFNNNN NNNNNSCNNS KKFKSISEST SALGLEASSS
SSSSS
