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
//