ID A0A2I0M996_COLLI Unreviewed; 747 AA.
AC A0A2I0M996;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN Name=MTIF2 {ECO:0000313|EMBL:PKK26248.1};
GN ORFNames=A306_00008196 {ECO:0000313|EMBL:PKK26248.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK26248.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK26248.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK26248.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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:PKK26248.1}.
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; AKCR02000027; PKK26248.1; -; Genomic_DNA.
DR RefSeq; XP_005513214.1; XM_005513157.1.
DR AlphaFoldDB; A0A2I0M996; -.
DR STRING; 8932.A0A2I0M996; -.
DR GeneID; 102086254; -.
DR KEGG; clv:102086254; -.
DR CTD; 4528; -.
DR InParanoid; A0A2I0M996; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000053872; 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; 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; 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 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:PKK26248.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872}.
FT DOMAIN 199..369
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 174..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 82864 MW; D2795161F99A9B38 CRC64;
MGAAAGRSRC GAVPLAAAGE EMNRGLILKF ASLVRFRGAC RQLRTLSHRK AARAQWKPVR
PSAHPPCSAL LYPPLWQKDK LMSIALAQRR HLATKEEAKK KKKKILVTRG EVEIRQKMTV
EELARAMGKD VDHIYEALLY TDVDLDSLEP DSVLYEDHIK LIVKKSGMKY KSAKLKEEKE
RENTDAVKRP PADPAALTPR PPVVTILGHV DHGKTTLLDS LRKTQVASME AGGITQHIGA
FLVHLPSGEK ITFLDTPGHA AFSAMRARGT HVTDIVILVV AAEDGVMEQT IESIQHAKNA
GVPIILAINK CDKPEADPER VKKELLAHDV VCEEFGGDVQ AVNISALKGE NLMVLAEATV
ALAEMLELKA DPTGLVEGTV IESRKDKGKG PVTTAIIQRG TLRKGCVLVA GKTWAKVRFM
FDENGKAVDA ASPGVPVEIM GWKEVPSAGD EMLEVESEQR AQEVVAWRTY VEQQEKVKKD
MEVIEAKQKE HRMEYEKKQQ KLAHLTWRQR KAVLYKEKKH LMFLKPKERT EMDKNVLSVI
VKGDVDGSVE AILNILDSYD ADDECKLDII HFGMGDISET DIGLAETFNG VVFGFSVKAN
ESIKQLAAKK GIKIKLHNVI YKLIEDLKEE LNSKLPPAVV ENTIGEASVL DIFSVTVGKT
KIPVAGCRVQ KGLLDKKMKF KLIRKGDVIW KGYLSSLKHH KDDVQVIKMG MDCGLSLDKN
IEFNIGDEII CYEEKEVQQT TSWDPGF
//
