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GLKA_DICDI
ID   GLKA_DICDI              Reviewed;         473 AA.
AC   Q55C57;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Probable serine/threonine-protein kinase glkA;
DE            EC=2.7.11.26;
DE   AltName: Full=Glycogen synthase kinase-like kinase A;
GN   Name=glkA; ORFNames=DDB_G0270218;
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-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC         COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC         Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000005; EAL72459.1; -; Genomic_DNA.
DR   RefSeq; XP_646624.1; XM_641532.1.
DR   AlphaFoldDB; Q55C57; -.
DR   SMR; Q55C57; -.
DR   STRING; 44689.DDB0216280; -.
DR   PaxDb; Q55C57; -.
DR   EnsemblProtists; EAL72459; EAL72459; DDB_G0270218.
DR   GeneID; 8617596; -.
DR   KEGG; ddi:DDB_G0270218; -.
DR   dictyBase; DDB_G0270218; glkA.
DR   eggNOG; KOG0658; Eukaryota.
DR   HOGENOM; CLU_000288_181_20_1; -.
DR   InParanoid; Q55C57; -.
DR   OMA; MTIPDTM; -.
DR   PhylomeDB; Q55C57; -.
DR   PRO; PR:Q55C57; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR   GO; GO:0004672; F:protein kinase activity; IDA:dictyBase.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005977; P:glycogen metabolic process; ISS:dictyBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0010629; P:negative regulation of gene expression; HDA:dictyBase.
DR   GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:dictyBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; HDA:dictyBase.
DR   GO; GO:1905511; P:positive regulation of myosin II filament assembly; IMP:dictyBase.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0043087; P:regulation of GTPase activity; IMP:dictyBase.
DR   GO; GO:0043520; P:regulation of myosin II filament assembly; IMP:dictyBase.
DR   GO; GO:0019932; P:second-messenger-mediated signaling; IMP:dictyBase.
DR   CDD; cd14137; STKc_GSK3; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR039192; STKc_GSK3.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
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..473
FT                   /note="Probable serine/threonine-protein kinase glkA"
FT                   /id="PRO_0000358885"
FT   DOMAIN          91..366
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        208
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         97..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   473 AA;  52554 MW;  72E4295165642D0D CRC64;
     MTIPTDNNSS NNKGYNDNNN NNNNNNNNNN NNNNNNNNNN KEHPNINNNN NNNNNNNNNN
     IKESSSSNSN HSSSQSSSTA TVNSNPKVYP YEIIKQVGQG TFGKVYEAKN QDNKRVAIKK
     VEKSNHFISR EYDILKIVAH PNCLRILDMF YTAEDNKKMQ NLVFDFIPYT LASLLKKRQL
     SINFIKVLFY QLCQAIKHIH SKAICHRDIT PNNILLSSKG ELTLADFGSA KILESNHTSM
     SYICSRYYRA PELLVGCSNY TTKIDIWSIG CILAEMLIGK PLFPGTNSND QLGRIIEVLG
     SPTKDDMEAM KPSKPYHLQL PNINPKFFES LHNVEDKTVV DLLSKIFIFD PVKRASIDEI
     IAHPFLRDVN INSLELFDEM KCFSVSGNGK SSLTTNSTSS SSTTANMTSL ASSSSNNKTT
     CSETYLSRLP TSAITSSSNL KSIDNSNNGK SSSSSNNIPS LNNSNNGVIT NTI
 
 
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