ID A0A1S3IXE6_LINUN Unreviewed; 849 AA.
AC A0A1S3IXE6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN Name=LOC106168248 {ECO:0000313|RefSeq:XP_013402703.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013402703.1};
RN [1] {ECO:0000313|RefSeq:XP_013402703.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013402703.1};
RG RefSeq;
RL Submitted (NOV-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_013402703.1; XM_013547249.2.
DR AlphaFoldDB; A0A1S3IXE6; -.
DR STRING; 7574.A0A1S3IXE6; -.
DR EnsemblMetazoa; XM_013547249.2; XP_013402703.1; LOC106168248.
DR GeneID; 106168248; -.
DR KEGG; lak:106168248; -.
DR InParanoid; A0A1S3IXE6; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000085678; 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.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|RefSeq:XP_013402703.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678}.
FT DOMAIN 300..470
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 849 AA; 94891 MW; 757518A065316390 CRC64;
MCMIPYYLWQ TGKQVHKSCL TGRQAVLLMG NGLALQEYPV LNAGEILMAN MKKLWSLNRK
NLLGLVGQRS GCNMSPCRDL FQNHSIFELA PLSSLRALST CTFCLSNGNY PPKSYSVVPN
VCTGKTPRRE LSTKSYNFKK GTKKNNYSAL NNLEGEQFEK AKRNILKWRK SKFEDGQPSE
SMHWKKARGS NDITKKNMEA QPKPEFKEPV QIQTVTVASD GRMTLHDICE ATQMKLASVK
NALKAIKHQK KKHFNCDADH MVESIEDLKK IIEHLGFKAV TPQDKGINRR PPPDPAVLVK
RAPVVTIMGH VDHGKTTLLD ALRNTNVVAQ EFGGITQHIG AFQVTVSSGD VITFLDTPGH
AAFAKMRARG AMVTDIVVLV VAAEDGVMEQ TIESIMYAKE AKVPIIVAIN KIDKPSADVE
ATKNMLSEHG LVSEEFKGDT QFVPISALKK INLDKLQEAI LVESEIMELK GDPTGLVEGI
VIESNVDPQR GKIATVLIQR GVLKPGGYLV AGKCWGKVRY MLDHRQQPIR ETSLSMPVQV
VGWKELPEAG AEVIGTNSEK EALSIVEWNQ EHLSKDETLQ MHRDLNLKRQ EHRDSHSVKL
QKRLEMGRYT YGLVHNLEEF AHLKKKQSYW IDSGPSLNLV VKGDVAGSVE TLLSSFGGYQ
LEHLCPIKII HSGVGDITLR DLEMAETFNG VVFGFQVTAP VEIVDLAEKK EIPLKLHQVI
YHLFDDLKDE IVKKIPLVNE DKIIGKAEVM KMFKAAIGKH HSLAAGCYCS EGILDSKKHF
QLIREDEVVH EGQISNLRHF QSKVQTIKQG MECGLTFDDP KVQVNKGDII VCFERQQKRV
GKDDLDFGF
//
