ID   A0A0L1KNK6_9EUGL        Unreviewed;       723 AA.
AC   A0A0L1KNK6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN   ORFNames=XU18_3597 {ECO:0000313|EMBL:KNH05426.1};
OS   Perkinsela sp. CCAP 1560/4.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Prokinetoplastina;
OC   Ichthyobodonidae; Perkinsela.
OX   NCBI_TaxID=1314962 {ECO:0000313|EMBL:KNH05426.1, ECO:0000313|Proteomes:UP000036983};
RN   [1] {ECO:0000313|EMBL:KNH05426.1, ECO:0000313|Proteomes:UP000036983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1560/4 {ECO:0000313|EMBL:KNH05426.1};
RA   Tanifuji G., David V., Flegontov P., Gerasimov E., Hashimi H.,
RA   Logacheva M., Maruyama S., Onodera N., Gray M., Archibald J., Curtis B.,
RA   Cenci U., Lukes J.;
RT   "Draft genomes of Paramoeba pemaquidensis and its kinetoplastid
RT   endosymbiont Perkinsela sp. CCAP 1560/4.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KNH05426.1}.
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; LFNC01000246; KNH05426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L1KNK6; -.
DR   EnsemblProtists; KNH05426; KNH05426; XU18_3597.
DR   OrthoDB; 169393at2759; -.
DR   Proteomes; UP000036983; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
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; 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   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; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
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   PRINTS; PR00315; ELONGATNFCT.
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   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000313|EMBL:KNH05426.1};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036983}.
FT   DOMAIN          166..343
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          692..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  80537 MW;  9277817FFCC54C59 CRC64;
     MRRSLIFLHT QGSRMRPFSD GKSNSRYGDQ SYIRLTVGKL TSQMRAKIQN ERRKQGLPQV
     IDWKDFCEDA IAVPTSFGTL WCGPDDPRVE KFVKRREKME EQPLQVARGQ QEVDEIGKLE
     DHPNRAFFTT ATNLRDPMSV AEGLYRLGRI KSTEVEYTAT QIKYETRPPI VSIMGHVDHG
     KTTLLDTLRQ TNIAACEAGG ITQSIGAFQV RVPREGGKSD ELITFIDTPG HEAFAEMRKS
     GCSAADIIVL VISLSDGIQP QTREVISLAK SKNTPLVIAI NKIDKGGDMD LIIRELSGLG
     VSLESEGGDV LLSKISAKHK TNVEHLLQNI QLQSLMCELY TPTQARAEIT IIESKSKLVS
     GIVRCGTLRK GAWMVCGISF ARVEKILDDR GREIDQARVS APVAIEGFIV LPKPGNILLE
     VAGKHYANMF VALMRDVYGA EAQHEKYLQY LAADAQGKIY NRKPLNRVQS NSTVAFGLLI
     KAGTFGQLQA LLKLIYALPR IDSVELIIIN AEVDALDDDD ITNLSARQQP GGFILFGDVE
     NKTHMAIPSH LGFTKHDVVF HAVNWIKEQI VEHIPKDRAD VVHMEAVCKS TFAASQAGRG
     GNAGGCFVEK GKLHVAAKNI RLIRRGETVW EGRIKELRRF KEKVSYVEEG LECGIVLDDG
     FAFEVGDCLQ EYSIEWKEHD VDEIYQKAAA QEDEDRRLKE REQTDAVDEI DDESAELESL
     IHG
//