ID A0A5Q4C3X7_9PEZI Unreviewed; 1006 AA.
AC A0A5Q4C3X7;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 02-APR-2025, entry version 18.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN Name=IFM1 {ECO:0000313|EMBL:TQN73244.1};
GN ORFNames=CSHISOI_02263 {ECO:0000313|EMBL:TQN73244.1};
OS Colletotrichum shisoi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum destructivum species complex.
OX NCBI_TaxID=2078593 {ECO:0000313|EMBL:TQN73244.1, ECO:0000313|Proteomes:UP000326340};
RN [1] {ECO:0000313|EMBL:TQN73244.1, ECO:0000313|Proteomes:UP000326340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-2018a {ECO:0000313|EMBL:TQN73244.1,
RC ECO:0000313|Proteomes:UP000326340};
RX PubMed=31527702;
RA Gan P., Tsushima A., Hiroyama R., Narusaka M., Takano Y., Narusaka Y.,
RA Kawaradani M., Damm U., Shirasu K.;
RT "Colletotrichum shisoi sp. nov., an anthracnose pathogen of Perilla
RT frutescens in Japan: molecular phylogenetic, morphological and genomic
RT evidence.";
RL Sci. Rep. 9:13349-13349(2019).
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:TQN73244.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PUHP01000110; TQN73244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q4C3X7; -.
DR OrthoDB; 361630at2759; -.
DR Proteomes; UP000326340; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 FunFam; 2.40.30.10:FF:000008; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.10050:FF:000001; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.300:FF:000019; Translation initiation factor IF-2; 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; IPR053905; EF-G-like_DII.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd.
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; PF22042; EF-G_D2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:TQN73244.1};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000326340};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 484..652
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 29..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 752..779
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 45..54
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..150
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1006 AA; 109705 MW; 4E7357AC24C0298A CRC64;
MLRCRIWNER SSAYVCAFCR HPALSRPNDL GRRNYWHTSK PPSNGTGGLG GWGSNNGVKA
PKSSGIPPGP RGPVAGGGWG QPLMGKGSSS EAPNYDGQQA STGRESSLDG LLLPHELAAR
QQLEAQKAAQ PKALLITRNV AKHTTPKSRH LGGLEGGLGG SNISRTPLVT MARKSLGGEE
KPLSGRDWRH RHEGERTSTS TPIPHNRHNG RDVNRTIPTE NLPQQQQRGL DEPNALGTGE
WGQLSRKATD GSSADVPRST GSKPGLSKQD FLTQFHDQVS SKYNQEDKKS RASTSDFGHS
KNNSSQKTEQ VVDESTKPQR RTREIDESYE ISRDPRRRDK AGGRRGDAYE SFRGVKKSAA
QQRWEDENEE WEDNGAGREA QRRRKKSEAE ARRLALEKAA APNILLPEFI SIANLGTALK
LKPQEFLRSL SEMGFEDITE DSIMTGETAA LVAQEFGFEP TVDTGGVRDL RPRPPPEDVL
ALPPRPPVVT IMGHVDHGKT TLLDYLRKSS VAAQEHGGIT QHIGAFMVKM SEGKLITFLD
TPGHAAFLTM RQRGANVTDI VVLVVAADDS VKPQTIEAIK HAKTANVPII VAINKCDKED
AKPDQVKADL ARHGVEIEDF GGDVQVVCVS GKTGQGMSDL EENIVTLADI QDMRAEEDGL
AEAWVLEASV KPYGKSANVL VKRGTLRPGD FIVAGTAWAR VRLLRNEAGQ ELEKAPPGTP
VEVLGWRDEL PAAGDEILQA PDEGRAKTAV DYREEMRARE TSSKQLAEQE QREREAKAAA
EVAAEIEAAG AEGGEVIATK VINFMVRGDV VGSVEAVCAT INEIGNNEVK PRILRSSAGQ
ISESDVEHAE ASSSVIANFN CAVPAHVKHL AEEKGVRILE HSVIYHLADE VKQVMSEYLA
DKVTSKVNGE AEILQIFPIN IKGRTYKNIA GCKVRNGTVT RSTSVRILRK GEKVFDGKID
TLKHGKKDVN EVRKGTECGI AFDGFTDLQV GDRIQTYEEV REKRSL
//
