IF2M_SCHPO
ID IF2M_SCHPO Reviewed; 686 AA.
AC O59683;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial;
DE Short=IF-2(Mt);
DE Short=IF-2Mt;
DE Short=IF2(mt);
DE Flags: Precursor;
GN ORFNames=SPBC1271.15c, SPBC2F6.01;
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: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; CU329671; CAA22205.1; -; Genomic_DNA.
DR PIR; T39351; T39351.
DR RefSeq; NP_595135.1; NM_001021043.2.
DR AlphaFoldDB; O59683; -.
DR SMR; O59683; -.
DR BioGRID; 276714; 3.
DR STRING; 4896.SPBC1271.15c.1; -.
DR MaxQB; O59683; -.
DR PaxDb; O59683; -.
DR PRIDE; O59683; -.
DR EnsemblFungi; SPBC1271.15c.1; SPBC1271.15c.1:pep; SPBC1271.15c.
DR GeneID; 2540181; -.
DR KEGG; spo:SPBC1271.15c; -.
DR PomBase; SPBC1271.15c; -.
DR VEuPathDB; FungiDB:SPBC1271.15c; -.
DR eggNOG; KOG1145; Eukaryota.
DR HOGENOM; CLU_006301_5_2_1; -.
DR InParanoid; O59683; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; O59683; -.
DR PRO; PR:O59683; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISO:PomBase.
DR GO; GO:0097177; F:mitochondrial ribosome binding; EXP:PomBase.
DR GO; GO:0003723; F:RNA binding; ISO:PomBase.
DR GO; GO:0003743; F:translation initiation factor activity; EXP:PomBase.
DR GO; GO:0070124; P:mitochondrial translational initiation; EXP:PomBase.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW GTP-binding; Initiation factor; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..686
FT /note="Translation initiation factor IF-2, mitochondrial"
FT /id="PRO_0000014482"
FT DOMAIN 169..344
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 178..185
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 203..207
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 226..229
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 280..283
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 316..318
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 178..185
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 226..230
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 280..283
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 686 AA; 75611 MW; 6F5B5CEDC6F3A5CD CRC64;
MAFLSACTSW RHVHNAGFTF ITKFPFVRNV HKLSYHISPL SSRFSLADIS VKENNHPNGP
QLRLQTHFFH SSSPMHATKG FRFPKSSTPL TLPAVLSVAS FANLLQIPTR RILRDLNRLG
IKDVFPEYLI TYEYSSLLAE EYGFDVQEAA AYSAPSPKSL NSKKDSGPLR PPVVTLMGHV
DHGKTTLLDA FRKSTIASTE HGGITQKIGA FTVPFDKGSK FITFLDTPGH MAFEAMRKRG
ANIADIVVLV VAGDDGVKPQ TVEAIKHIQS ADVPVVVALT KSDRPGTPIH KIYEQLLNNG
IQVEALGGET QIIPISAKTG KGIPELEAAI LTLAEIMEIR ASPRDPFQGW IVESSVTKGV
GSSATVVVKR GTVKKGMYLV AGKSWCKVRS LVDVNKKSIK QVLPGQAAQV YGWKDLPIAG
DLAYEVKSES EAKRILSDIY RQSNEQNFYE LAESQNEQRV SALAAKKSGP AAIQEETSVS
KSFNIIAKCE DTGSMEALSD YLKPLQFGKV KSRVLYTGVG PVTETDIERA ETSDAIIISF
GVSVPKATFR LAEKHNVKLL FHNVIYHLMD DVRKLFALRL PPILVQRVTG EAIISAIFDI
KAKRAVVHVA GCRVTNGTIE KSHKIRLVRN DKIIWSGEID SLKHLKEEVT SIKKGRECGI
LLKNFDEIVT GDKLQTFVEE YKPPDF
