EI2BB_SCHPO
ID EI2BB_SCHPO Reviewed; 393 AA.
AC Q9UT76;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable translation initiation factor eIF-2B subunit beta;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit beta;
GN Name=tif222; ORFNames=SPAC343.14c;
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 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-108 AND SER-112, AND
RP IDENTIFICATION BY 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 -!- INTERACTION:
CC Q9UT76; P56286: tif211; NbExp=2; IntAct=EBI-16198490, EBI-16198594;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB52277.1; -; Genomic_DNA.
DR PIR; T38663; T38663.
DR RefSeq; NP_593435.1; NM_001018868.2.
DR PDB; 5B04; X-ray; 2.99 A; C/D=1-393.
DR PDB; 6JLY; X-ray; 3.50 A; C/D=1-393.
DR PDB; 6JLZ; X-ray; 3.35 A; C/D=1-393.
DR PDBsum; 5B04; -.
DR PDBsum; 6JLY; -.
DR PDBsum; 6JLZ; -.
DR AlphaFoldDB; Q9UT76; -.
DR SMR; Q9UT76; -.
DR BioGRID; 279470; 9.
DR DIP; DIP-61959N; -.
DR IntAct; Q9UT76; 3.
DR STRING; 4896.SPAC343.14c.1; -.
DR iPTMnet; Q9UT76; -.
DR MaxQB; Q9UT76; -.
DR PaxDb; Q9UT76; -.
DR PRIDE; Q9UT76; -.
DR EnsemblFungi; SPAC343.14c.1; SPAC343.14c.1:pep; SPAC343.14c.
DR GeneID; 2543035; -.
DR KEGG; spo:SPAC343.14c; -.
DR PomBase; SPAC343.14c; tif222.
DR VEuPathDB; FungiDB:SPAC343.14c; -.
DR eggNOG; KOG1465; Eukaryota.
DR HOGENOM; CLU_016218_4_3_1; -.
DR InParanoid; Q9UT76; -.
DR OMA; TSHTSYA; -.
DR PhylomeDB; Q9UT76; -.
DR Reactome; R-SPO-72731; Recycling of eIF2:GDP.
DR PRO; PR:Q9UT76; -.
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:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:PomBase.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:PomBase.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IDA:PomBase.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR Gene3D; 1.20.120.420; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR027363; M1Pi_N.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Translation regulation.
FT CHAIN 1..393
FT /note="Probable translation initiation factor eIF-2B
FT subunit beta"
FT /id="PRO_0000317323"
FT REGION 105..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 28..45
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 51..68
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 73..96
FT /evidence="ECO:0007829|PDB:5B04"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6JLY"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 170..184
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:5B04"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 342..346
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:5B04"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 378..385
FT /evidence="ECO:0007829|PDB:5B04"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:5B04"
SQ SEQUENCE 393 AA; 43221 MW; 19F324EF0135628B CRC64;
MSTINVEHTY PAVSSLIADL KSRKVQGPFA VAVETALVMR QVISQTRWST VDQLIDTVRA
VGSTLVKAQP TEFSCGNIIR RILRLIREEY QELLKTADEN EKLIVSSSNS SSPSQKRDIP
SNEKLVQSHE PVSVQMYSSM LNLLGRPTLE SPTHSKTVGD SRVTGGMDMR AVIISGIQDV
IDELDKINTD IEVQSMDHLH SNEIILTQGC SKTVEAFLRF AAKKRKFSVI VAEGFPNNQK
GSHAMAKRLA QAGIDTTVIS DATIFAIMSR VNKVILGTHA ILGNGGLVTY SGAQLVAQAA
RHHATPVVVC SGIYKLSPVY PYDLESIIQL SSPDKIMSFN EGDLISRAEI LNPYYDYIPP
DLVDLFITNL GGYPPSYLYR IMNDTYDASD TIL
