ID D4AYG7_ARTBC Unreviewed; 931 AA.
AC D4AYG7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=ARB_01236 {ECO:0000313|EMBL:EFE31983.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE31983.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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. {ECO:0000256|ARBA:ARBA00025162}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFE31983.1}.
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DR EMBL; ABSU01000018; EFE31983.1; -; Genomic_DNA.
DR RefSeq; XP_003012623.1; XM_003012577.1.
DR AlphaFoldDB; D4AYG7; -.
DR STRING; 663331.D4AYG7; -.
DR GeneID; 9522700; -.
DR KEGG; abe:ARB_01236; -.
DR eggNOG; KOG1145; Eukaryota.
DR HOGENOM; CLU_006301_8_4_1; -.
DR OMA; DEIICFE; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
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; IEA:UniProtKB-KW.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF20; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866}.
FT DOMAIN 406..576
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 118..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 102414 MW; 1B78071E58590EFB CRC64;
MGYTRVWRSG VLYTRGVETA RGFASFASFS ETIAFYCRNV EVVYLANVFC CHRTETHQGN
STLHGFVLNV KRPIQSNLYL VLTATGNLAE PTLLRQDHDL PSRNRLLLKL HPVTGKHLAT
PETKNKASLQ LQGVGPLSNP YTGPLEESWQ ETGFRSISRK PRSSLDSQKQ DSSVSGSWQL
SGFRSLPPQS EQIRSSDLPS ESEAPPVRSK PRRDELDSGN YTNEDYVGRQ SSRAVRGRAR
DFTPSYEDAD KEFSSKPRKQ KGRRATTEDD LDEPPIRSNR RGASRGRDLD IMDRDLEYGV
GRPKRKDKKD KKKAAQRAQE QSGPTPIVLP DFISVGNLAD AINVRRTQFI KSLESLGFDD
VTNDHVLDSE TAGLIVTEFN FEPVAESNDI DLVAAPRPDD TSNLPARPPV VTIMGHVDHG
KTTLLDYLRK SSVVATEHGG ITQHIGAFSV TMPSGKQITF LDTPGHAAFL EMRKRGADVT
DIVILVVAAD DSVKPQTIEA IKHAKGADVP IIVAINKIDK EDINIDRVKQ DLARHNVSVE
DYGGDVQAIG VSGKTGQGML KLEEAVITLS EMLDLRADKE CNFEGWIIEA STKRAGRAAT
VLVRQGTLRP GDVIVAGTSW AKVRTLRNEA GIQVAEALPG TPVEVDGWRD QPVAGFEVLQ
APDEQRAKDV VAFRTEKEEV QRLGGDVEAI NQTRRETRER RQLQAALEEN GDTSTDAADK
GGPQPIPFIV KADVSGSAEA IVNAMSAVGN NEVFAKILRF SVGKIGESDI RHASAANAAV
ISFNQSVDPD IMKFAVAEEV DVLNHNIIYE LIDDVKMRLS EHLPPTVTQR VSGEAEIGEI
FEIKLKGKKT TFVAGCKVSN GVINRSHNVR VLRGKNIIYD GTLSSLKNVK KDVTEMRKGT
ECGMAFEGWA DFAVGDEIQT YEVVREKRLL D
//
