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Y9719_DICDI
ID   Y9719_DICDI             Reviewed;         942 AA.
AC   Q54WD7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Probable serine/threonine-protein kinase DDB_G0279719;
DE            EC=2.7.11.1;
GN   ORFNames=DDB_G0279719;
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).
RN   [2]
RP   INDUCTION [LARGE SCALE ANALYSIS].
RX   PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA   Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA   Skelton J., Ivens A., Bozzaro S.;
RT   "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT   bacteria in Dictyostelium.";
RL   BMC Genomics 9:291-291(2008).
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   -!- INDUCTION: Down-regulated by phagocytic stimuli.
CC       {ECO:0000269|PubMed:18559084}.
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; AAFI02000032; EAL67634.1; -; Genomic_DNA.
DR   RefSeq; XP_641616.1; XM_636524.1.
DR   AlphaFoldDB; Q54WD7; -.
DR   SMR; Q54WD7; -.
DR   STRING; 44689.DDB0216331; -.
DR   PaxDb; Q54WD7; -.
DR   PRIDE; Q54WD7; -.
DR   EnsemblProtists; EAL67634; EAL67634; DDB_G0279719.
DR   GeneID; 8622194; -.
DR   KEGG; ddi:DDB_G0279719; -.
DR   dictyBase; DDB_G0279719; -.
DR   eggNOG; KOG0589; Eukaryota.
DR   HOGENOM; CLU_311785_0_0_1; -.
DR   InParanoid; Q54WD7; -.
DR   OMA; IEWAEHQ; -.
DR   PRO; PR:Q54WD7; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..942
FT                   /note="Probable serine/threonine-protein kinase
FT                   DDB_G0279719"
FT                   /id="PRO_0000362069"
FT   DOMAIN          4..617
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          109..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          675..703
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        487
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   942 AA;  105742 MW;  ACD5AA33B53B4746 CRC64;
     MNKYEVVKLI GVGGEAKALL VKRINSDKLY VMKQRMFFLL EEANEGLCEA MSLAKIQSPY
     IVRFEEVFLD NNSNMFSLCI VMEYCEGGDL MDNLFKRISD SFLKNSGLNN NQNNNNNNNN
     NLNSIVNNNI LNNNKNSKQS TTNTNSSGSN SSIASNTTNN NNNNNNINNN NNLKAYENFF
     SKYVPSETLK GVNQLVEPNC NKDNNKPIEI TTTDSPRIII NDNESTNNLN SQSDQILQFS
     ISSESSSFSN NDLINSPNSN DSNLHQSSSN SSICGDYSSP PNLEKISSPG TSTPYQKGSN
     GNTVNIRCSD IVVEAVSPIK TESIGCQIRS TTSPCTSGPT SPQMIPLNIV EQPPQSTSTS
     KTDSSPTGAD VKKTKMTWWK TYKSSKKDKK QTICSNACES FSNSTFFNDP SSHSQPQHQQ
     LHSSPQQLPQ SPRLKPNIES SLNINGNNNN NNCSTLLKLP RKLFYTWIYQ ICLGVQSIHK
     NHLVHLDLKS ENIFLSESQK IKIGDFGLAK KYENSMSGVA GTYYYLSPEI LLNKNYSRPA
     DIFSLGCIFY EMYTLNLLPL TKRSFGQELI EGKFDRKAFK QEFDDSDEPI ADLILDMLNL
     DQNLRPTIDL ILQNKLFERI SDINSSFNNL LNIVNNTGSS ITNSKSNSSN NLNNSNSNND
     IINNNNNNNS SNNINNNNIV NLNNSYNNKQ DKCEQRNKSL NQNGFLSTSS MGSISSSFNE
     HEFVRRQLEK NDLDAAADVL CEAFKEEPRF QFVSGATSDN LETKNKSIEL GQTIRKSFFT
     MCVRLMFDNK FMLWGCFDYE NKLIAVACWS TPGKSGAPPM TQLIVKILSM LPKFGFRTMK
     RIGKIMSNID KAMKNHDSKL DVYYLPYIGV SKEYRDLGVG QYLLKPVIEW AEHQRKTVKA
     VVFSQKQINF FSKLGLSVGH TEKITNLKGI NSIYVMSKNS QY
 
 
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