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Y6461_DICDI
ID   Y6461_DICDI             Reviewed;         798 AA.
AC   Q86HW6; Q551K8;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable serine/threonine-protein kinase DDB_G0276461;
DE            EC=2.7.11.1;
GN   ORFNames=DDB_G0276461;
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AAFI02000015; EAL69184.1; -; Genomic_DNA.
DR   RefSeq; XP_643126.1; XM_638034.1.
DR   AlphaFoldDB; Q86HW6; -.
DR   SMR; Q86HW6; -.
DR   STRING; 44689.DDB0229347; -.
DR   PaxDb; Q86HW6; -.
DR   EnsemblProtists; EAL69184; EAL69184; DDB_G0276461.
DR   GeneID; 8620531; -.
DR   KEGG; ddi:DDB_G0276461; -.
DR   dictyBase; DDB_G0276461; -.
DR   eggNOG; KOG1989; Eukaryota.
DR   HOGENOM; CLU_352497_0_0_1; -.
DR   InParanoid; Q86HW6; -.
DR   OMA; EYENETN; -.
DR   Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR   PRO; PR:Q86HW6; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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   SMART; SM00220; S_TKc; 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   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..798
FT                   /note="Probable serine/threonine-protein kinase
FT                   DDB_G0276461"
FT                   /id="PRO_0000362059"
FT   DOMAIN          54..324
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          330..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          659..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        330..413
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        185
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         60..68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   798 AA;  88840 MW;  39A551539F6F9CF0 CRC64;
     MNRFLEFSNN FLEVAGNTIN NISSKSITDN VGNVWGNITG GRVGQVYDIN GRRVTEVKLV
     AEGGFGFVYL VRDDYNNMYA LKRMFIQERE RLEAMKNEID VMQKLRNNPN IVKLEGFKIN
     ENRNTRETEV LMLMEYCSGG SVLDIMNARG EFTRLEEREI LAIFSDVCNG VLAMHQQQPP
     IAHRDLKIEN VLYCEHSNRY KLCDFGSSTI KTFNTATERG KAEDDINMFT TLFYRAPEMV
     DLYRGQIIDE KVDVWALGCL LFKMAFYVDP FDGGSLQIIN NNYKIPDNSK YSNNFHKLIQ
     FILVADPTQR PSINDLLNYL NEIRGSSRRG LQTFSSNNNN SNNNSNNNSN NNSNNNSVNN
     SSNSINRPIR TSSSSNSTPN FNSPNTNNNN YNNNNNNSKN YGNTPNSTPP NAKKNIFDIL
     GDDTTSSTSN SNNSPSVSRN NINNNSNNFN NNNNNNNNNN NNNNNNNNNN NNNNTNNNNS
     NNNNYNNNNN KFDEFESWGN TPLQHPSPSN SNSNVIINNT NSSGKNNQNK SNSGNGNFFD
     NDFEFEGFVS PTTNGSTNFE VNTTNTNVSL NSSTHSSSSF NNSSNNNNTN NSSVSVGSSI
     NNSGTRLMNN SSGSLPQSRQ SSFNSTPQQQ QQQFNSSTNS GSYNNLTSSF NNLNISTSSS
     ASISSSGGVS NNSDNSWNVT LTPSQSNKNS TGNLKPLNNN NNNNNNNNNR FANNTNSSRD
     YSFDFSSPNT SNNNDFGSFV QPSSSSSLNT THFSKPNYNV NLNQTTSMTN NYNNNNYNNN
     NNSNNNNNNS KVFDFGIL
 
 
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