Y0019_DICDI
ID Y0019_DICDI Reviewed; 908 AA.
AC Q54XY6;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable serine/threonine-protein kinase DDB_G0278521;
DE EC=2.7.11.1;
GN ORFNames=DDB_G0278521;
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 type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000023; EAL68433.1; -; Genomic_DNA.
DR RefSeq; XP_642416.1; XM_637324.1.
DR AlphaFoldDB; Q54XY6; -.
DR SMR; Q54XY6; -.
DR STRING; 44689.DDB0230019; -.
DR PaxDb; Q54XY6; -.
DR EnsemblProtists; EAL68433; EAL68433; DDB_G0278521.
DR GeneID; 8621621; -.
DR KEGG; ddi:DDB_G0278521; -.
DR dictyBase; DDB_G0278521; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_319913_0_0_1; -.
DR InParanoid; Q54XY6; -.
DR OMA; NIANGMN; -.
DR PhylomeDB; Q54XY6; -.
DR PRO; PR:Q54XY6; -.
DR Proteomes; UP000002195; Chromosome 3.
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; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
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 ANK repeat; ATP-binding; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..908
FT /note="Probable serine/threonine-protein kinase
FT DDB_G0278521"
FT /id="PRO_0000358900"
FT TOPO_DOM 1..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..908
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 258..289
FT /note="ANK 1"
FT REPEAT 300..326
FT /note="ANK 2"
FT REPEAT 330..361
FT /note="ANK 3"
FT REPEAT 362..391
FT /note="ANK 4"
FT REPEAT 395..424
FT /note="ANK 5"
FT REPEAT 495..524
FT /note="ANK 6"
FT DOMAIN 530..817
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 461..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 677
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 536..544
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 908 AA; 102365 MW; 762A49B22F998F55 CRC64;
MSNNKIIESL AILYLNNYIN DNDIYSLSLI NREFHINIIK DDYFYSTINK NYLFLYIKIF
KLLSIKVKLN PNWINIINNN NNINNNNNNN NNNNNNNNNN NNNKIKLIKN NFSVISERLN
FLIQCKFNLH RYLDNNDLFI TILRGEKLST LDRIICFSII YSQDQILLFL LNFILSNINC
NNNNNNNNNN NNNNNNNNIS NISNSNRLLA NNSYNIQFNQ QIPTQNELIN LNKCLQFSTS
TTTTTTTTMV PPFNENILKV YPIYFAIVKV IGGGSLVRFL LSILPNVYNI TNVNCKLPIT
NRSALFYSTT REMTLLLLQL GCNIHDMDYK GMLPIHYHSL NGHVDVVKCL IDDSTINALD
QSNNTPLNLA SLSGNLSLAK ILLNSGARLS IDNLNGRYPI HNACVNGNID LIRYFLELYS
KMNSTTLLPS TTTTTTTTTT TMTTTTTTAI TTTTATTIQN NSNNLTNSNS SSVGGLRISN
GGNTQQQSIQ IPDKENNTPI DLLVLNNHFT IAIELLKYEG YIVGKEEFNF KTARKIGAGA
FGDVYLVEWR NKNVAVKRVK IEKILESGKS YQWIRDKFIL EAVLMVKLSN FSSFVKLYAT
CIEEKELLLV LEFCDNGSLY TILNTIPIGG AGANNNNNNN NNNDIIQSLP SINTLSLNIA
NGMNYLHSLK PQIIHRDLTS QNILIDRNGI AKIADFGISR FKNDIGDKTM TSIGNPRFRS
PEVTKGQKYS EKVDVFGFGM ILYEMFTRRV PFHDYEQIAA SFKIANAERP PLPQTIDHRW
SNLIQICWDQ NPNNRPSFDQ ILTIIQNLPI ANIPKFLVPL QQNQNQIQNQ NQNQNQNNGK
LDLSTSSSSI TNLNNAVTAK LSLSTSGGLF SGDSDYTVGT CSGYDIGYDN DGDIIDYSSD
QNDSDLYD
