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Database: UniProt
Entry: Q55EC7
LinkDB: Q55EC7
Original site: Q55EC7 
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   01-OCT-2014, entry version 64.
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; Mycetozoa; Dictyosteliida; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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
RT   biological roles.";
RL   Genome Biol. 6:R68.1-R68.12(2005).
CC   -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- DEVELOPMENTAL STAGE: Clearly expressed during growth and
CC       development. Expression culminates at 8-12 hours of development
CC       and is still clearly detectable at 18 hours of development.
CC       {ECO:0000269|PubMed:16086850}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00135}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00168}.
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DR   EMBL; AAFI02000005; EAL71999.1; -; Genomic_DNA.
DR   RefSeq; XP_645854.1; XM_640762.1.
DR   ProteinModelPortal; Q55EC7; -.
DR   EnsemblProtists; DDB0229854; DDB0229854; DDB_G0269298.
DR   GeneID; 8616798; -.
DR   KEGG; ddi:DDB_G0269298; -.
DR   dictyBase; DDB_G0269298; gefX.
DR   eggNOG; COG0515; -.
DR   OMA; ETCFDIN; -.
DR   PhylomeDB; Q55EC7; -.
DR   Reactome; REACT_206101; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; REACT_206503; Sema3A PAK dependent Axon repulsion.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.840.10; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom.
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.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 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   SUPFAM; SSF48366; SSF48366; 2.
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; Complete proteome; Guanine-nucleotide releasing factor;
KW   Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    960       RasGEF domain-containing
FT                                serine/threonine-protein kinase X.
FT                                /FTId=PRO_0000354061.
FT   DOMAIN       21    274       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN      437    565       N-terminal Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00135}.
FT   DOMAIN      712    957       Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00168}.
FT   NP_BIND      27     35       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   COMPBIAS    282    298       Poly-Ala.
FT   COMPBIAS    320    331       Poly-Asn.
FT   COMPBIAS    596    604       Poly-Asn.
FT   COMPBIAS    607    616       Poly-Asn.
FT   COMPBIAS    620    623       Poly-Ser.
FT   COMPBIAS    624    652       Poly-Asn.
FT   ACT_SITE    140    140       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      48     48       ATP. {ECO:0000255|PROSITE-
FT                                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
//
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