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Database: UniProt
Entry: A0A2K5IBZ1_COLAP
LinkDB: A0A2K5IBZ1_COLAP
Original site: A0A2K5IBZ1_COLAP 
ID   A0A2K5IBZ1_COLAP        Unreviewed;       727 AA.
AC   A0A2K5IBZ1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000014173.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000014173.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_011812837.1; XM_011957447.1.
DR   AlphaFoldDB; A0A2K5IBZ1; -.
DR   STRING; 336983.ENSCANP00000014173; -.
DR   Ensembl; ENSCANT00000037096.1; ENSCANP00000014173.1; ENSCANG00000030529.1.
DR   GeneID; 105522855; -.
DR   KEGG; cang:105522855; -.
DR   CTD; 4528; -.
DR   OMA; DEIICFE; -.
DR   OrthoDB; 169393at2759; -.
DR   Proteomes; UP000233080; Unplaced.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080}.
FT   DOMAIN          178..355
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   COILED          453..487
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   727 AA;  81727 MW;  8742BD78E514BC7B CRC64;
     MNQKLLKLEN LLRFHTIYRQ LHSLCQRRAL RQWRHGFSSA YPVWTAQLYA WPWPTEMLIG
     AALSQYRLLV TKKEERPWKS QLSSTKSKQV VEVWIGMTVE ELARAMEKNT DYIYEALLNT
     AIDIDSLEAD SHLDEVWIKE VIMKAGMKLK WSKLKQDKVK KNKDAVRRPQ ADPALLTPRS
     PVVTIMGHVD HGKTTLLDKL RKTQVAAMEV GGITQHIGAF LVSLPSGEKI TFLDTPGHAA
     FSAMRARGAQ VTDIVILVVA ADDGVMKQTV ESIQHAKDAQ VPIVLAINKC DKTEADPERV
     KKELLAYDVV CEDYGGDVQA VPVSALTGNN LMALAEATIA LAEMLELKAD PNGPVEGTVI
     ESFTDKGRGP VTTAIIQRGT LRKGCVLVAG NCWAKVRLMF DENGKTIHEA HPSMPVGITG
     WRDLPSAGEE ILEVESEPRA REVVDWRKYE QEQEKGKEDL KIIEEKRKEH QEAYRKAREK
     YSNVQWKKRS YLQYLERKEQ TSLKPKEKME RDSNVLPVII KGDVDGSVEA ILNIIDTYDA
     SHECELELVH FGVGDISAND VNFAETFNGV IYGFNVNVGK VIQQSAAKKG VKIKLHKIIY
     RLVEDLQEEL SSRLPCAVEE HPVGEASILA TFSITEGKKK VPVAGCRVQK GQLEKQKKFK
     LTRNGHVIWK GSLTSLKHQK DDISIVKTGM DCGLSLDEEN MEFKVGDRIV CYEEKQIQAK
     TSWDPGF
//
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