KXCA_DICDI
ID KXCA_DICDI Reviewed; 1311 AA.
AC Q54GY6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Kinase and exchange factor for Rac A;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase kxcA;
GN Name=kxcA; Synonyms=RacGEF; ORFNames=DDB_G0289859;
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 IDENTIFICATION.
RX PubMed=16762450; DOI=10.1016/j.ejcb.2006.04.011;
RA Vlahou G., Rivero F.;
RT "Rho GTPase signaling in Dictyostelium discoideum: insights from the
RT genome.";
RL Eur. J. Cell Biol. 85:947-959(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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000149; EAL62530.1; -; Genomic_DNA.
DR RefSeq; XP_636021.1; XM_630929.1.
DR AlphaFoldDB; Q54GY6; -.
DR SMR; Q54GY6; -.
DR STRING; 44689.DDB0229867; -.
DR PaxDb; Q54GY6; -.
DR EnsemblProtists; EAL62530; EAL62530; DDB_G0289859.
DR GeneID; 8627347; -.
DR KEGG; ddi:DDB_G0289859; -.
DR dictyBase; DDB_G0289859; kxcA.
DR eggNOG; ENOG502RFNJ; Eukaryota.
DR HOGENOM; CLU_260725_0_0_1; -.
DR InParanoid; Q54GY6; -.
DR OMA; RRMSICG; -.
DR PRO; PR:Q54GY6; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043226; C:organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PF00612; IQ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50096; IQ; 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; GTPase activation; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1311
FT /note="Kinase and exchange factor for Rac A"
FT /id="PRO_0000354062"
FT DOMAIN 18..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 650..679
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 691..927
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT REGION 169..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1208..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 24..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1311 AA; 149141 MW; 6CD098B4FA899A5F CRC64;
MVGGLPNSSL WNIEYDDLVF KDIIGKGNFG CVYRGNYLGV EVAIKQIPSF DDPDYCKYTE
REVKALRYIR HPFVVHFFGA CKHESGFYLI TEFIEGLDLR RYLKSVPKPP KWLSRVNIAL
GVAKTFLFLH SKNLLHRDLK SKNILLDISR NQIKLCDFGF ARVGSQYSNG SDSSSSEDES
DSECVNGAAG GGGDDVYKNN GNGKPANYRL RRMSICGTPS FMPPEILLQQ KYDWSVDVFS
FGILCTELIT LKRPGKDYWV RSQNNGFDIN IEELNVNIPS PNDCPIQFYD LALKCCSYKH
TNRPMFSTIV TILESIKLQL ELFENQQQQQ QLQQQQQLQQ QQQQQQQQQQ QQQQQLQLQQ
QQSSESSSSS SSQPLVNNNN NNSNCNNNNF NNSSNNNNSI ANNDSISNVS TTTTSIPTTT
TTTTTTTTTT NNITAINGTS NKYLQPLSKH QQQQQRNQNS SIIDNNSLIG SSNTESMITS
FSISTFKERK KQSLNKLIRA NTINILIGQQ QQQQQQQQQQ QQQQQDNQSS SQNQLIEREG
VIKLDTTKYP NGWKEFGIDN STNKIWIIYQ SNIIKIGSNN NNNLIEMTCG TIIKLKKHSI
TLSIVDSNLI SGANIINVKS YLKDYPYVNK PIKVNQQQQQ QQQIITNNYE LNLIIKLQSR
IRGWLVRRRY KIFLSNWKLN NSNTSQSNKN QWIRLFNQLI SSELEYKKQL DQVIKSYLLP
IQSKFRINKP LLNYKEIGSI FSNIESLSEI HNELLKIVNQ ISKSPFFIMN FENEKDDRSN
QNNTSATTDI FGDSSIQFTN ISINTKDSSN QINSITQFIV KNISQIKNQY GIYAFNFKYS
TNIYNWCRLN PDFSIFCDTI RSQLNQQFPD QENDLASLLS LPINKIQKYL LVFEKLAQIT
PITHSEYKDI KSAFTLIRET SNYIQSQLEM SFEHSHIMSI DIMLQKKDNQ SLMQSGRWFI
RQGQFTELSS NKQYYLFLLS DICLITKPIK SKSSKYNNNN NINTNNNNNN LTSSATQTNS
NKDLSTSINQ STSNANSDNS GNNNNNLINS KYYYRLKTII NLKEEVSMRI NPDISNGVLF
IGPNKTYKWL LPNDEEAKDW VNDFERTTIL IYRNNPNGGG SNNNSIGGGG GGRGGSGNNS
NNGSIDLTEI NQIHHINNQA IPLSSSNNNI TNNNSINNNI IMNNNNNNNK DTEGKGFIKR
FRLSFSAGTS TPERKTSLVN MSPSTTSSLN NIDSNYNNNN NNVTNTPIKS VTSSPSIHYT
PVNDNNQQPQ LPSQPNEEFQ FTVPTTPSDK KKKRGSFSSK LKRLSITFSK D
