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PDPKA_DICDI
ID   PDPKA_DICDI             Reviewed;         686 AA.
AC   Q54TW2;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable serine/threonine-protein kinase pdkA;
DE            EC=2.7.11.1;
DE   AltName: Full=3-phosphoinositide-dependent protein kinase A;
DE   AltName: Full=Pdk-class protein kinase A;
GN   Name=pdkA; ORFNames=DDB_G0281471;
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   -!- DOMAIN: The PIF-pocket is a small lobe in the catalytic domain required
CC       by the enzyme for the binding to the hydrophobic motif of its
CC       substrates. It is an allosteric regulatory site that can accommodate
CC       small compounds acting as allosteric inhibitors.
CC       {ECO:0000250|UniProtKB:O15530}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PDPK1 subfamily. {ECO:0000305}.
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DR   EMBL; AAFI02000041; EAL66717.1; -; Genomic_DNA.
DR   RefSeq; XP_640699.1; XM_635607.1.
DR   AlphaFoldDB; Q54TW2; -.
DR   SMR; Q54TW2; -.
DR   STRING; 44689.DDB0216243; -.
DR   PaxDb; Q54TW2; -.
DR   EnsemblProtists; EAL66717; EAL66717; DDB_G0281471.
DR   GeneID; 8623085; -.
DR   KEGG; ddi:DDB_G0281471; -.
DR   dictyBase; DDB_G0281471; pdkA.
DR   eggNOG; KOG0592; Eukaryota.
DR   eggNOG; KOG0605; Eukaryota.
DR   HOGENOM; CLU_000288_63_9_1; -.
DR   InParanoid; Q54TW2; -.
DR   OMA; GYPSIRA; -.
DR   PhylomeDB; Q54TW2; -.
DR   Reactome; R-DDI-114604; GPVI-mediated activation cascade.
DR   Reactome; R-DDI-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-DDI-165158; Activation of AKT2.
DR   Reactome; R-DDI-202424; Downstream TCR signaling.
DR   Reactome; R-DDI-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   Reactome; R-DDI-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-DDI-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-DDI-5218920; VEGFR2 mediated vascular permeability.
DR   Reactome; R-DDI-6804757; Regulation of TP53 Degradation.
DR   PRO; PR:Q54TW2; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:dictyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030295; F:protein kinase activator activity; IDA:dictyBase.
DR   GO; GO:0004672; F:protein kinase activity; IMP:dictyBase.
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:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0098630; P:aggregation of unicellular organisms; IMP:CACAO.
DR   GO; GO:0043327; P:chemotaxis to cAMP; IGI:dictyBase.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:1905303; P:positive regulation of macropinocytosis; IMP:dictyBase.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; IGI:dictyBase.
DR   CDD; cd01262; PH_PDK1; 1.
DR   CDD; cd05581; STKc_PDK1; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR033931; PDK1-typ_PH.
DR   InterPro; IPR039046; PDPK1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF14593; PH_3; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 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..686
FT                   /note="Probable serine/threonine-protein kinase pdkA"
FT                   /id="PRO_0000358890"
FT   DOMAIN          69..449
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          593..682
FT                   /note="PH"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          100..144
FT                   /note="PIF-pocket"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   REGION          211..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        216..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        192
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         79..81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         147..149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
FT   BINDING         210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:O15530"
SQ   SEQUENCE   686 AA;  75562 MW;  C4FCC7FE8539A842 CRC64;
     MENIVITNTS GGGGGGVPSS STDPPNNTTT TTATASAIDL NMSLSPFLSS PSLSSPSIQS
     AKKKTIEDFI IGKVLGEGSY GAVVLGTEKE TQQQYAIKIL EKKQIIKENK IKYVQIEKEI
     FCKSNHPNIV KLFFTFRSEQ CLYYVLELCS QGDLLHQIKK VGSFDYRSCQ YYVAEIISGL
     EHLHSLGIVH RDLKPENILM SSDLHVKITD FGTGKILPPP QSSQQQQQQQ QQQQQLPTNS
     SGNLSSLLNN VNNLSVSTDL TQQQQNRTSS VDSASTTDSM ISPNLQPTTT TTNNNNNNNN
     NNNNNNNNTA AGSNTNTNTN TNINTNINAN INNIKTTEIP KLTRNNSFVG TAEYVSPELI
     SNKETSTDSD LWALGCIIYQ MASGRVPFRG KTEFLTFQKV SNRELVYPIN MNPVIKDLVE
     KLLVIKPTDR LGSSSTPGGF DNLKAHPFFQ DFNWSSLSNM SHPPPPIQPP QEKIIFDGDE
     LFSPSLDCTT PRNNNVDENH QQNSCNNNNN NNNNINNINN NNNSSSNNIS NSNSNSNSSN
     NLNISNGNLS TPRSSSSSSS QQPTQRSGSS GGSRDGGSSS NNISKWLNNG ENVIYQGLVW
     KRKGFSIKKR QLILTDTPRL IYIDPKKMEL KGEIPWSDSI KPKLKSNNNF VIKTPKRKYL
     LEDVAHNPQK WVDSIKSVIL SSGSSN
 
 
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