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EI2BE_DICDI
ID   EI2BE_DICDI             Reviewed;         707 AA.
AC   Q54RF3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Translation initiation factor eIF-2B subunit epsilon;
DE   AltName: Full=eIF-2B GDP-GTP exchange factor subunit epsilon;
GN   Name=eif2b5; ORFNames=DDB_G0283163;
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).
CC   -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-
CC       bound GDP for GTP.
CC   -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta
CC       and epsilon.
CC   -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000051; EAL65820.1; -; Genomic_DNA.
DR   RefSeq; XP_639192.1; XM_634100.1.
DR   AlphaFoldDB; Q54RF3; -.
DR   SMR; Q54RF3; -.
DR   STRING; 44689.DDB0234243; -.
DR   PaxDb; Q54RF3; -.
DR   PRIDE; Q54RF3; -.
DR   EnsemblProtists; EAL65820; EAL65820; DDB_G0283163.
DR   GeneID; 8623968; -.
DR   KEGG; ddi:DDB_G0283163; -.
DR   dictyBase; DDB_G0283163; eif2b5.
DR   eggNOG; KOG1461; Eukaryota.
DR   HOGENOM; CLU_012507_1_0_1; -.
DR   InParanoid; Q54RF3; -.
DR   OMA; HYLYDKD; -.
DR   PhylomeDB; Q54RF3; -.
DR   Reactome; R-DDI-72731; Recycling of eIF2:GDP.
DR   PRO; PR:Q54RF3; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:dictyBase.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:dictyBase.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR   CDD; cd04197; eIF-2B_epsilon_N; 1.
DR   CDD; cd11558; W2_eIF2B_epsilon; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035543; eIF-2B_epsilon_N.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR003307; W2_domain.
DR   InterPro; IPR044123; W2_eIF2B_epsilon.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF00483; NTP_transferase; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   PROSITE; PS51363; W2; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Transferase.
FT   CHAIN           1..707
FT                   /note="Translation initiation factor eIF-2B subunit
FT                   epsilon"
FT                   /id="PRO_0000328350"
FT   DOMAIN          516..693
FT                   /note="W2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT   REGION          489..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..526
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..707
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   707 AA;  80253 MW;  3CFF8227A5370760 CRC64;
     MSKNDKKNKQ SGSSNMDQLK SEDILQAVVL GDSFDRKFAP ITLEKPRTLL PLVNIPLLDY
     TLEFLAASGV QQIFVFCCAH ASQIKEYIQS SRWHDLPGVQ VICMTGSNCR TTGDALRGVY
     DAQVIQSDFI LISGDVVSNM NLQKALQIHK DRRELDKNNI MTMVYKQASS THRTRSKQDD
     TVIWCNRDTM QVVCYDNSPS KKKSSISVEL FQKHPSIQMR YDLIDCHIDI CSPEVLALFN
     DNFDFADIRK DFIHDILTSD LLDYKLSAYV LQGEYAARVK DLRTYHSVSK DIIHRWTFPM
     VPDNNFMCNS SYSLSRQMIY KEKNVKLLGD CLISDETVIG TQTEIGAGSI VSHSTIGRNC
     IIGKNVKING SYIWDDVTIQ DNAIIDHSII CNGSIIKSSS IIGRGSIIGF NVYIGQSKTL
     EPFSKITMAQ YNEDEDDEEL LEEYFKEINL NDDNNNNNNN NNENNKTNRW LMENELYNEL
     VPRINDSIHD DIESDESGDE GDKSGGKIKN NKNNDDNPIE PDSVKFHREV GDTIRRGIIE
     KLPLENIQLE INGLKFAYDR DGLDCLTSIL PVLLESSSSS SSTTDSVTPK ELQQFIAGRI
     SAFSPLLVKF SSEDSMVDLI FKIQDFCDEN EKFKVVFQPI LHQLYENDVI SEEAIFEWAE
     EIEGDEEDDG FYLKKCKGFI DWLKSAEEES DDSDDSDDDD DDSDESD
 
 
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