EI2BG_SCHPO
ID EI2BG_SCHPO Reviewed; 458 AA.
AC P56288;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable translation initiation factor eIF-2B subunit gamma;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit gamma;
GN Name=tif223; ORFNames=SPAC4D7.09;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-
CC bound GDP for GTP. {ECO:0000250}.
CC -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta
CC and epsilon. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC {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; CU329670; CAB11281.2; -; Genomic_DNA.
DR PIR; T38800; T38800.
DR RefSeq; NP_594962.2; NM_001020393.2.
DR PDB; 5B04; X-ray; 2.99 A; E/F=1-458.
DR PDB; 6JLY; X-ray; 3.50 A; E/F=1-458.
DR PDB; 6JLZ; X-ray; 3.35 A; E/F=1-458.
DR PDBsum; 5B04; -.
DR PDBsum; 6JLY; -.
DR PDBsum; 6JLZ; -.
DR AlphaFoldDB; P56288; -.
DR SMR; P56288; -.
DR BioGRID; 280036; 6.
DR DIP; DIP-61960N; -.
DR IntAct; P56288; 3.
DR STRING; 4896.SPAC4D7.09.1; -.
DR iPTMnet; P56288; -.
DR MaxQB; P56288; -.
DR PaxDb; P56288; -.
DR PRIDE; P56288; -.
DR EnsemblFungi; SPAC4D7.09.1; SPAC4D7.09.1:pep; SPAC4D7.09.
DR GeneID; 2543622; -.
DR KEGG; spo:SPAC4D7.09; -.
DR PomBase; SPAC4D7.09; tif223.
DR VEuPathDB; FungiDB:SPAC4D7.09; -.
DR eggNOG; KOG1462; Eukaryota.
DR HOGENOM; CLU_016743_3_0_1; -.
DR InParanoid; P56288; -.
DR OMA; LLQAWMV; -.
DR Reactome; R-SPO-72731; Recycling of eIF2:GDP.
DR PRO; PR:P56288; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:PomBase.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:PomBase.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:PomBase.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IDA:PomBase.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..458
FT /note="Probable translation initiation factor eIF-2B
FT subunit gamma"
FT /id="PRO_0000156082"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:5B04"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6JLZ"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 128..134
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:5B04"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:5B04"
FT TURN 222..226
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 230..245
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:5B04"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:5B04"
FT TURN 261..266
FT /evidence="ECO:0007829|PDB:5B04"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:6JLY"
FT TURN 284..289
FT /evidence="ECO:0007829|PDB:6JLZ"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 424..427
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:6JLZ"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:5B04"
SQ SEQUENCE 458 AA; 50462 MW; 242987543BE43021 CRC64;
MSLYEHAALP LASSPSILGP ISGGRNRGNI QLQSIPIEFQ AVVFAGFGNS LYPLTGSDAL
PKALLPIGNK PMLHYPLYWL EAAGFTSAIL ICMEEAEAHI NAWLRSGYEG HMRIHVEAPT
ILDDSKSSAD ALRAVSHLIK NDFVCLSCDS IVGLPPIYGL DKFRLDNPSA LAVYSPVLKY
EHITSQSKEI DAKQLIGIEE KTSRLLYAKS SADVGSDFTF RMSLLWKHPR VTLNTNLSDA
HIFVFKHWVI DLIREKESIS SIRGDLIPYL VKCQYQKSFT VRENIQRFLS SPNNIDNYDG
GLSSQEIKIN ALIAKDGIIC SRANNLPNYF ELNKCIAKLT PEQRLVDVTV SERALVGADC
MVNEGTTIKD NSNIKKSIIG KNCVIGKGVV VSNSILMDNI VVEDGVRLES CIVASGAQIG
AKSKLRECEI GVDHRVEAGR IARGERLVDM EKIETDMD
