IF5_SCHPO
ID IF5_SCHPO Reviewed; 395 AA.
AC Q09689;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable eukaryotic translation initiation factor 5;
DE Short=eIF-5;
GN Name=tif5; ORFNames=SPAC2F7.05c;
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).
CC -!- FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal
CC initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent
CC joining of a 60S ribosomal subunit resulting in the release of eIF-2
CC and the guanine nucleotide. The subsequent joining of a 60S ribosomal
CC subunit results in the formation of a functional 80S initiation complex
CC (80S.mRNA.Met-tRNA[F]) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA90492.1; -; Genomic_DNA.
DR PIR; T38553; S58149.
DR RefSeq; NP_592976.1; NM_001018376.2.
DR AlphaFoldDB; Q09689; -.
DR SMR; Q09689; -.
DR BioGRID; 278125; 3.
DR STRING; 4896.SPAC2F7.05c.1; -.
DR iPTMnet; Q09689; -.
DR MaxQB; Q09689; -.
DR PaxDb; Q09689; -.
DR PRIDE; Q09689; -.
DR EnsemblFungi; SPAC2F7.05c.1; SPAC2F7.05c.1:pep; SPAC2F7.05c.
DR GeneID; 2541629; -.
DR KEGG; spo:SPAC2F7.05c; -.
DR PomBase; SPAC2F7.05c; tif5.
DR VEuPathDB; FungiDB:SPAC2F7.05c; -.
DR eggNOG; KOG2767; Eukaryota.
DR HOGENOM; CLU_026663_1_0_1; -.
DR InParanoid; Q09689; -.
DR OMA; YRYKMEK; -.
DR PhylomeDB; Q09689; -.
DR Reactome; R-SPO-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:Q09689; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; ISO:PomBase.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IBA:GO_Central.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; ISO:PomBase.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:PomBase.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0042256; P:mature ribosome assembly; ISO:PomBase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
DR PROSITE; PS51363; W2; 1.
PE 3: Inferred from homology;
KW GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..395
FT /note="Probable eukaryotic translation initiation factor 5"
FT /id="PRO_0000212526"
FT DOMAIN 228..384
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 146..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..395
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 395 AA; 44944 MW; 18F49CB3CC8C2D11 CRC64;
MATINIRRDV KDSFYRYRMP KLQSKIEGKG NGIKTVIPNM SDIAKALGRP PLYVTKFFGF
ELGAQTTIIA DMDRYIVNGA HDAGKLQDLL DVFIRRFVLC ASCQNPETEL SINKKDQTIS
YDCKACGYRG VIDGRHKLTG VIVKNPPAKK KSHKHKRDSP VAEEEDGAED ELTRRIRQEA
AELPTAEVVN DEDWAVDTSE EAVRARVQEL EGNMKDSLTL SDLRGDEEEA ESSRYDQFGE
WLEDNYPGVS DVEIYKKMKE ENIHHKSKAI VVLVQCIITS PYVGEFEKHG ALFKKLCTTD
KHERALLGGF ERLMENTELV HIDVVPKVLL EIYQNDLVSD DMFEKWGAKA SKKYVSRETS
KKIHEAAEPF LTWLAEASDE SESEDEEEEE EDDDE
