GenomeNet

Database: UniProt
Entry: GEFX_DICDI
LinkDB: GEFX_DICDI
Original site: 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   27-MAR-2024, entry version 108.
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 (Social amoeba).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000005; EAL71999.1; -; Genomic_DNA.
DR   RefSeq; XP_645854.1; XM_640762.1.
DR   AlphaFoldDB; Q55EC7; -.
DR   SMR; Q55EC7; -.
DR   STRING; 44689.Q55EC7; -.
DR   PaxDb; 44689-DDB0229854; -.
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; KRWIDYY; -.
DR   PhylomeDB; Q55EC7; -.
DR   Reactome; R-DDI-5673000; RAF activation.
DR   Reactome; R-DDI-5674135; MAP2K and MAPK activation.
DR   Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   CDD; cd13999; STKc_MAP3K-like; 1.
DR   Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR   Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1.
DR   PANTHER; PTHR46485:SF4; LIM DOMAIN KINASE 1; 1.
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; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48366; Ras GEF; 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
//
DBGET integrated database retrieval system