PDPKB_DICDI
ID PDPKB_DICDI Reviewed; 908 AA.
AC Q54PK9;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=3-phosphoinositide-dependent protein kinase B;
DE EC=2.7.11.1;
DE AltName: Full=Pdk-class protein kinase b;
GN Name=pdkB; ORFNames=DDB_G0284489;
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16596165; DOI=10.1371/journal.pgen.0020038;
RA Goldberg J.M., Manning G., Liu A., Fey P., Pilcher K.E., Xu Y., Smith J.L.;
RT "The dictyostelium kinome -- analysis of the protein kinases from a simple
RT model organism.";
RL PLoS Genet. 2:E38-E38(2006).
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; AAFI02000066; EAL65171.1; -; Genomic_DNA.
DR RefSeq; XP_638523.1; XM_633431.1.
DR AlphaFoldDB; Q54PK9; -.
DR SMR; Q54PK9; -.
DR STRING; 44689.DDB0216246; -.
DR PaxDb; Q54PK9; -.
DR PRIDE; Q54PK9; -.
DR EnsemblProtists; EAL65171; EAL65171; DDB_G0284489.
DR GeneID; 8624616; -.
DR KEGG; ddi:DDB_G0284489; -.
DR dictyBase; DDB_G0284489; pdkB.
DR eggNOG; KOG0592; Eukaryota.
DR HOGENOM; CLU_000288_63_9_1; -.
DR InParanoid; Q54PK9; -.
DR OMA; RNANTVW; -.
DR PRO; PR:Q54PK9; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0004676; F:3-phosphoinositide-dependent protein kinase activity; ISS: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; IGI: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: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:0051897; P:positive regulation of protein kinase B signaling; IGI: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; 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; 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..908
FT /note="3-phosphoinositide-dependent protein kinase B"
FT /id="PRO_0000341968"
FT DOMAIN 271..527
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 764..902
FT /note="PH"
FT REGION 53..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..346
FT /note="PIF-pocket"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT REGION 538..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 281..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 349..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 355
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
FT BINDING 412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:O15530"
SQ SEQUENCE 908 AA; 102361 MW; 90818D4040A73658 CRC64;
MINGRYQKED VVNNNNNLNL NLIEKTLNDL TIKNNTNINN NNTNNKNTNY YNNNNFNNNN
NNNNNNNNNN NNINNNNNNN KYLNNSHNNN NNNNNNNNNN NNNNNNNNNN EINNNNNNVL
SHSSLSGKGG STTYETTSYT TSITSSRDTG TISTSYESSS SSSSSSSSSL YDDDEYSDYS
DSSDSIDSYV NHRQALSKSQ QQQHLQQQQD QPQPLHSSMG AISNEKPPSP TNQQQQQQHH
HPKHNIELPK TSSFGLQPNS SIPHKKSRSD FDFIRTIGKG AYGKVKLVIE KETQLIFASK
ILNKKLIIKE KKAKYVNTEK TILDSLDNPN IVKLFYTFQD ENNLYFILEY CPNGDLLGAL
KKAGCFSIDV VRFYAAEILI ALEYLHGKGI AHRDLKPENI LLGKNQHLKL SDFGSAKQLS
IGSHHKGSRS GSFCGTAEYV CPELLTEKSA GVEADIWSYG CLLYQLVSGK LPFKGFNEYQ
TFLLITKREF SYPDNFDKCC MNLIDQLLDL DPYKRPTISE IKNHEFFSSI QDWSSIPSQT
PPPIEQMVPQ SPFPSPNSSL RLKKRSLSVG SPINSSLTYL SQPPIKPLNL DNSNIDYNDF
ENNQIISNNN NNNNNTTTTT TTTTTSANTS GSTNNTLYFT SPNVTSPPTS MSSNNTPRYI
NPLPTQSTTT TTTKPAYSST PSSTILKSTP PPPILSSCSS NNLLGKSSNQ QYQPFQFHQQ
QQQQQQQQQR ERSSTTTPSP TFLSNHHNQH QKNLQQSFSS IDKSSFSTSS PMSSPRILLK
PTELVLMDKD RKRNIREQQQ IDQYQWSRFL LPNDEIILAC GITEKRSGLI TKKRQLIITD
TPRIFYVDPV KMTQKGEITV DGSLSAQQKS SKHFIINSKG RSRHFYDLDG QSKLWVDLIN
ELNMLSFK
