PAKE_DICDI
ID PAKE_DICDI Reviewed; 926 AA.
AC Q54B33;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Serine/threonine-protein kinase pakE {ECO:0000250|UniProtKB:Q869N2};
DE EC=2.7.11.1;
GN Name=pakE {ECO:0000312|EMBL:EAL60465.1}; ORFNames=DDB_G0293932;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL60465.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL60465.1};
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] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17659086; DOI=10.1186/gb-2007-8-7-r144;
RA Sawai S., Guan X.-J., Kuspa A., Cox E.C.;
RT "High-throughput analysis of spatio-temporal dynamics in Dictyostelium.";
RL Genome Biol. 8:R144.1-R144.15(2007).
CC -!- FUNCTION: May play a role in responding to changes in chemoattractant
CC levels. {ECO:0000269|PubMed:17659086}.
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 Evidence={ECO:0000250|UniProtKB:Q869N2};
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; Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q869N2};
CC -!- DISRUPTION PHENOTYPE: Mutants have an aberrant response to waves of
CC cAMP stimulation. {ECO:0000269|PubMed:17659086}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000250|UniProtKB:Q869N2}.
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DR EMBL; AAFI02000224; EAL60465.1; -; Genomic_DNA.
DR RefSeq; XP_628883.1; XM_628881.1.
DR AlphaFoldDB; Q54B33; -.
DR SMR; Q54B33; -.
DR PaxDb; Q54B33; -.
DR EnsemblProtists; EAL60465; EAL60465; DDB_G0293932.
DR GeneID; 8629499; -.
DR KEGG; ddi:DDB_G0293932; -.
DR dictyBase; DDB_G0293932; pakE.
DR eggNOG; KOG0574; Eukaryota.
DR HOGENOM; CLU_315567_0_0_1; -.
DR InParanoid; Q54B33; -.
DR OMA; CRCPNVL; -.
DR PRO; PR:Q54B33; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISS:dictyBase.
DR GO; GO:0046872; F:metal ion 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; ISS:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; HMP:dictyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:dictyBase.
DR InterPro; IPR011009; Kinase-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; 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; Coiled coil; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..926
FT /note="Serine/threonine-protein kinase pakE"
FT /id="PRO_0000363950"
FT DOMAIN 650..903
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 36..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 534..567
FT /evidence="ECO:0000255"
FT COMPBIAS 36..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 771
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 656..664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 926 AA; 104244 MW; 70DE9C885F85CF84 CRC64;
MEEDKDSDTL QILNDIINNE PNLEIYVKSK NNNYISSREL PTQDSSTKTS NITTPNNNNN
NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNTPT SLNSSWKSVV
PKRKIDTSSG AILNNNNNVG SPNNQSTSQT NHQQPPPQQL QQQQSLSSTS TPSISPPMLS
PSRRNVTSPN LTRSDPTVPI TNSRPTSPLT PPLSPQFQLN NLNFDDNNDH STTTTNNNNN
NNNNNSNNNN NNNRPKLMRE NSINKRSSLQ TLPVSSSSSS SAEDEILIKV WLPMEYTGQL
YKVRKFSGGS STLKVSSMLN SQLSPMYQSP KNKLFLNNEE KPIPSHLTLK DLSLSKYDIL
YLRREPEYEL IIPSSPQCGS LVMDKDIKID DMLIKIEHWL KDILDHAPHS TSQQQQQQLQ
QQPILHVDKH EYFTSLEDQQ LMSGHITNSS QYTLLKKLSV PTSNSRQTGK MSRGYYLRLY
DQKPISNYGI KIKDTLIFKK KILNRGLSID DAEGGIEITV LYSPLSMLPT TSDLDFEKEL
KENQQQLNNN NNNNNNNNNN NNNNNNNNNN NITTTTTTTT SSLINQTNEI LLPNLIKIDN
TSLLQDIKNE KKKRKSKRTP SSVGLPFNII HKTHVDFEYK WSGTSVEDTF EFKEKLGQGG
YGAVFKVLHR ETNFPLAIKV LSITPTRIKD IEKEIDLLKK CRCPNVLSYY GSISSKLTEL
WILMDHCAVG SINDMMKICC DTLDEEQIAV VTLNVLNGLG YLHSKGIVHL DVKAANILLT
EDKQIKIADF GVSQQLQTEY GQANVYIGSP LYMAPEVILK APYNSKADIW SLGITLIELA
EGRPPNRGLR SMNQLVEIPN MPPPKLSNPK DWSPCFNNFL ATCLVKDPVQ RPSVIDLLSH
DFIKNAKTTE VLSNLVKQTL SSRQSI
