GEFX_DICDI
ID GEFX_DICDI Reviewed; 960 AA.
AC Q55EC7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=RasGEF domain-containing serine/threonine-protein kinase X;
DE EC=2.7.11.1;
DE AltName: Full=Ras guanine nucleotide exchange factor X;
DE AltName: Full=RasGEF domain-containing protein X;
GN Name=gefX; ORFNames=DDB_G0269298;
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 DEVELOPMENTAL STAGE.
RX PubMed=16086850; DOI=10.1186/gb-2005-6-8-r68;
RA Wilkins A., Szafranski K., Fraser D.J., Bakthavatsalam D., Mueller R.,
RA Fisher P.R., Gloeckner G., Eichinger L., Noegel A.A., Insall R.H.;
RT "The Dictyostelium genome encodes numerous RasGEFs with multiple biological
RT roles.";
RL Genome Biol. 6:R68.1-R68.12(2005).
CC -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. {ECO:0000250}.
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 -!- DEVELOPMENTAL STAGE: Clearly expressed during growth and development.
CC Expression culminates at 8-12 hours of development and is still clearly
CC detectable at 18 hours of development. {ECO:0000269|PubMed:16086850}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL71999.1; -; Genomic_DNA.
DR RefSeq; XP_645854.1; XM_640762.1.
DR AlphaFoldDB; Q55EC7; -.
DR SMR; Q55EC7; -.
DR STRING; 44689.DDB0229854; -.
DR PaxDb; Q55EC7; -.
DR EnsemblProtists; EAL71999; EAL71999; DDB_G0269298.
DR GeneID; 8616798; -.
DR KEGG; ddi:DDB_G0269298; -.
DR dictyBase; DDB_G0269298; gefX.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_307855_0_0_1; -.
DR InParanoid; Q55EC7; -.
DR OMA; IDREVSM; -.
DR PhylomeDB; Q55EC7; -.
DR PRO; PR:Q55EC7; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; 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 GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48366; SSF48366; 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.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Guanine-nucleotide releasing factor; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..960
FT /note="RasGEF domain-containing serine/threonine-protein
FT kinase X"
FT /id="PRO_0000354061"
FT DOMAIN 21..274
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 437..565
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 712..957
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 314..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 960 AA; 107769 MW; 0EB63003194DE7AE CRC64;
MAEADPGLPT QAIWDIPFES LEFNEKIGKG SFGSVFRGCY LGLDVAIKKI EKADDPEYLK
YIDREVSMLQ SLRHPFIVNF SGICVHSSGL YIVTEFVSGG DVRQLLKKTP PIGWDKRVSI
AVDLAKAMVF LHAKKIIHRD LKSKNILLDE FQRIRLCDFG FARMSEQTKK SRHMTMCGTE
GWVAPEILLG MSYDTSCDVF SYGVVLAELI TGRKPGVDLW VRSPETCFDI NPEELKQKSI
PGCPSELISV CVECCLYEPL TRPKFDEILS QLKVCQNNLK VATAAAAAAA AAAAAAAAVV
STPTIQTPII QTPNISFSPN NSNNNNNNNN NISNISPDIT TGIQQINLSS SGGSNNSSPS
TPPQGSQLVS LAQSRRNTMS LHRKSMELNL VDGQLSTTPP PTSPIQSRPH KPSDSIWKIA
AKPKHVGYQT LKRKQGPCYA ALTSHITKMI ERATSDYYYD TSYIQDFLLA YRCFAPPQQI
FELLLSRYIA NSPDNFTNDI NGWKKVQRVI QLRVIIFFKR WIDYYPQDFL EEAMEDNLNE
FDKISAQQNS STALLLGTTI SNNELLIDPK LMTELQKKRS ELELLIQINS PSDFINNNNN
NNNNPVNNIN NINNNNSVNS SSSNNNNNNN NNNSNNNNNN NNNNNNNNNN NNGLNIINIA
AANQSKMMLQ NGNNRYSVLV TSNGIGNGEE PYPVSIIPPP TTSEYLDVKD IHSTELARQI
TIINSFYFNR IKAREFIEYI WEKCGEESTT TPYVGTSFVE VVPAENIHKF VRKCNNLARF
VSTEILKQTK LQKRVATIER FIEAAEKCLA NNDYAAVFSI VEPLVDQSIE RLSDTWRNVS
QRNLATFEHL KSIVSKENDH KKYRELLPDA KPPCIPNIHL LLDELSFIET SSPRLLPGGI
VNFFHYRQLS RKILQSQQLQ SHCFRPIPSI QKVLTKPPSE LFDDELIKNN SLKCEPPVSL
