ID KXCB_DICDI Reviewed; 1125 AA.
AC Q54C71;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Kinase and exchange factor for Rac B {ECO:0000303|PubMed:16762450};
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase kxcB {ECO:0000312|EMBL:EAL60914.1};
GN Name=kxcB {ECO:0000312|EMBL:EAL60914.1};
GN Synonyms=RacGEF {ECO:0000312|dictyBase:DDB_G0293124};
GN ORFNames=DDB_G0293124;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000312|EMBL:EAL60914.1}
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] {ECO:0000305}
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 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. {ECO:0000250|UniProtKB:Q869N2}.
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DR EMBL; AAFI02000199; EAL60914.1; -; Genomic_DNA.
DR RefSeq; XP_629348.1; XM_629346.1.
DR AlphaFoldDB; Q54C71; -.
DR SMR; Q54C71; -.
DR STRING; 44689.Q54C71; -.
DR PaxDb; 44689-DDB0229973; -.
DR EnsemblProtists; EAL60914; EAL60914; DDB_G0293124.
DR GeneID; 8629072; -.
DR KEGG; ddi:DDB_G0293124; -.
DR dictyBase; DDB_G0293124; kxcB.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG4424; Eukaryota.
DR HOGENOM; CLU_279836_0_0_1; -.
DR InParanoid; Q54C71; -.
DR OMA; CIGTPCY; -.
DR PRO; PR:Q54C71; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR23257:SF753; KINASE AND EXCHANGE FACTOR FOR RAC B-RELATED; 1.
DR PANTHER; PTHR23257; SERINE-THREONINE PROTEIN KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 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..1125
FT /note="Kinase and exchange factor for Rac B"
FT /id="PRO_0000371249"
FT DOMAIN 380..571
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 601..822
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 848..1117
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 50..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 971
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 854..862
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 876
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1125 AA; 125581 MW; 44BA6AEF81C36A06 CRC64;
MELSEPKQRF ESLLSLFEDV ANKRYSGDFS VKKNINAPQV PPRSYSLFNV TGGNVSSYNN
QQQQQNNNNN NNNNNNNNNN NNNNNNNNNN NSGEISSNNS TPSILFSPTP TSTAPPAPPQ
PTTPPNTGFH NRPLSININQ QPIGGVNNNN NNNNKDSPSN KPLRLSGSPP TASINGNQIE
QLQRELRNEK EAHQQTKYLL NSFADENKKL SNDCQLWRAK YFKLLTKNTK LKVIFDHFQS
IMNESDSVPG EGSLVHSTSY NSSSSSSSGG GGNITPRKLS LAGGGKFDDA PQSASALLKI
HHQRNQSTGS AFSNTIYNGE EKTRDTISYN ERPKRQTVGS STFFPPPPSR ATSTSSIQVN
SDPQEIEQLT EEQYLEMLEK RRQVSLQILQ TEKEYAFYLN IIVEEFLQPL KNESNLSNNP
FISKAQVKQL FGDTEVILGS SKLLAEDLEN VLLDGTSNPI GLGDCFLKIC DYFKLYASYV
KNYYTSISVL NKLKEESHKF QAFIQEKEQI LLDSNFTDLG ALLVLPVSRI GQYTSMINYL
FSLTPQSHPD YEPFKKAVIK MKSTVDYVKE KIRDNDSQNK VRIIQNQMTG KFENLNLPHR
RYVREGMLTE SGKGSNSNQY YCFLFNDIFV LSTPIKKSNQ FSFKKKISLS EAEVTMISDP
EDRPIFQISI QNIDSQQDNS PNMLSLNGIQ NAINNMTNND SKSKNNNNNN SNGNNNNNNI
NSNSNSNNNS VIDIKSSGVL INNGGGSGFI SNNNGITNVN SNNNNNNNIN SNNNINGNNN
NGNNSVNYSN GEDNNDRECF TFIADSNRDR EDWIQAIHAN IISSKKRNET RKPEDIEKGG
IDFSVSDIKL CEQIGSGGSG CTVHRCTVDG FTCAVKVLKL KNTSPFLVEQ FISEITIMVK
LSHQNIAKYL GHRLSGNQLW LFMEFYPHSL KDVITKRTSP FPATEVIWMA LEIAKGLEFL
HTQKNPIIHR DLKPGNIMCS LDDKGRVCSI RVCDFDTSKE LGNGVTLKTC IGTPCYMAAE
VLNVADGGNS GYSLKADIWS FAMLCFEIIS LLPPYHQFQH LQSIEMIING TCPPLPTDLI
QPKLLQPLIE LLVTCIDLNP NHRPNASQLV QKLTKMLKNT GMMTE
//
