IF2G_SCHPO
ID IF2G_SCHPO Reviewed; 446 AA.
AC Q09130;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit gamma;
DE Short=eIF-2-gamma;
DE EC=3.6.5.3;
GN Name=tif213; ORFNames=SPBC17G9.09;
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 [MRNA].
RX PubMed=9079882; DOI=10.1007/s004380050375;
RA Erickson F.L., Harding L.D., Dorris D.R., Hannig E.M.;
RT "Functional analysis of homologs of translation initiation factor 2gamma in
RT yeast.";
RL Mol. Gen. Genet. 253:711-719(1997).
RN [2]
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).
CC -!- FUNCTION: As a subunit of eukaryotic initiation factor 2 (eIF-2),
CC involved in the early steps of protein synthesis. In the presence of
CC GTP, eIF-2 forms a ternary complex with initiator tRNA Met-tRNAi and
CC then recruits the 40S ribosomal complex and initiation factors eIF-1,
CC eIF-1A and eIF-3 to form the 43S pre-initiation complex (43S PIC), a
CC step that determines the rate of protein translation. The 43S PIC binds
CC to mRNA and scans downstream to the initiation codon, where it forms a
CC 48S initiation complex by codon-anticodon base pairing. This leads to
CC the displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-
CC 5-mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release
CC of Pi, which makes GTP hydrolysis irreversible, causes the release of
CC the eIF-2-GDP binary complex from the 40S subunit, an event that is
CC essential for the subsequent joining of the 60S ribosomal subunit to
CC form an elongation-competent 80S ribosome. In order for eIF-2 to
CC recycle and catalyze another round of initiation, the GDP bound to eIF-
CC 2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP
CC exchange factor (GEF) eIF-2B. {ECO:0000250|UniProtKB:P32481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P32481};
CC -!- SUBUNIT: Eukaryotic translation initiation factor 2 (eIF-2) is a
CC heterotrimeric G-protein composed of an alpha, a beta and a gamma
CC subunit. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-
CC tRNAi form a multifactor complex (MFC) that may bind to the 40S
CC ribosome. {ECO:0000250|UniProtKB:P32481}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; U37354; AAC49675.1; -; mRNA.
DR EMBL; CU329671; CAB52807.1; -; Genomic_DNA.
DR PIR; T39732; T39732.
DR RefSeq; NP_595898.1; NM_001021805.2.
DR AlphaFoldDB; Q09130; -.
DR SMR; Q09130; -.
DR BioGRID; 276290; 14.
DR STRING; 4896.SPBC17G9.09.1; -.
DR iPTMnet; Q09130; -.
DR MaxQB; Q09130; -.
DR PaxDb; Q09130; -.
DR PRIDE; Q09130; -.
DR EnsemblFungi; SPBC17G9.09.1; SPBC17G9.09.1:pep; SPBC17G9.09.
DR GeneID; 2539738; -.
DR KEGG; spo:SPBC17G9.09; -.
DR PomBase; SPBC17G9.09; tif213.
DR VEuPathDB; FungiDB:SPBC17G9.09; -.
DR eggNOG; KOG0466; Eukaryota.
DR HOGENOM; CLU_027154_0_1_1; -.
DR InParanoid; Q09130; -.
DR OMA; NIGMVGH; -.
DR PhylomeDB; Q09130; -.
DR Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SPO-72649; Translation initiation complex formation.
DR Reactome; R-SPO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-SPO-72731; Recycling of eIF2:GDP.
DR PRO; PR:Q09130; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISO:PomBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IGI:PomBase.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IGI:PomBase.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Hydrolase; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..446
FT /note="Eukaryotic translation initiation factor 2 subunit
FT gamma"
FT /id="PRO_0000137447"
FT DOMAIN 21..227
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 30..37
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 58..62
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 114..117
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 170..173
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 205..207
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 33..38
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 170..173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 205..207
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
SQ SEQUENCE 446 AA; 48781 MW; F4B493F6EBF48139 CRC64;
MAENLDISEL SPIHPAIISR QATINIGTIG HVAHGKSTVV KAISGVHTVR FKNELERNIT
IKLGYANAKI YKCSNEECPR PGCYRSYSSN KEDHPPCEIC NSPMNLVRHV SFVDCPGHDI
LMATMLNGAA VMDAALLLIA GNESCPQPQT SEHLAAIEIM QLKHIIILQN KVDLIRESAA
EEHYQSILKF IKGTVAENSP IVPISAQLKY NIDAILEYIV KKIPIPVRDF TTAPRLIVIR
SFDVNKPGAE VDDLKGGVAG GSILTGVLRL NDEIEIRPGI VTKDDDGRIR CQPIFSRIIS
LFAEHNDLKI AVPGGLIGVG TTVDPTLCRA DRLVGQVLGS KGNLPEVYTE LEINYFLLRR
LLGVKSGDKN TTKVQKLAKN EVLMVNIGST STGGRVMMVK ADMAKILLTA PACTEIGEKV
ALSRRIEKHW RLIGWAKVVE GKTLKV
