ID A0A397SCL9_9GLOM Unreviewed; 956 AA.
AC A0A397SCL9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=C1645_785046 {ECO:0000313|EMBL:RIA84033.1};
OS Glomus cerebriforme.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Glomus.
OX NCBI_TaxID=658196 {ECO:0000313|EMBL:RIA84033.1, ECO:0000313|Proteomes:UP000265703};
RN [1] {ECO:0000313|EMBL:RIA84033.1, ECO:0000313|Proteomes:UP000265703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM 227022 {ECO:0000313|EMBL:RIA84033.1,
RC ECO:0000313|Proteomes:UP000265703};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) 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:RIA84033.1}.
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DR EMBL; QKYT01000522; RIA84033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397SCL9; -.
DR STRING; 658196.A0A397SCL9; -.
DR Proteomes; UP000265703; 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.
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:UP000265703}.
FT DOMAIN 407..576
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 125..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 675..709
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 131..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 956 AA; 107681 MW; 4720C0BE9149C816 CRC64;
MPSVIPRRKV KLFHNTTKLM KERPNPAADD WLIVDPDADI SSSQLQKARA YMKFDKLNPN
KWEKPKSLLI KQTEINPSGR NEDDSLFSFR SNNGKDSHLF GTKWDKPNTF NLSESSKDIM
VKRNRPKHKS GGLNNSKSYR ENLSGTNRFS DEYKNSRGKN NERIEIFNDG FRKNWTGSKN
LEGPDHKTMK SREKSLGLIE KEKVQPRLSQ IDQLRKEVGI ESDKKVDFVS ALTELKAFQE
INVEEEDDSS VFRTRQKFFS KKDKLAGTSE HRKPKFFKKE RDLLEKEEGY FDIDYRFDRP
KQKIRTHQIE QKLQREIFIP DAISVSNLAK MIGVHLGEQF RFFSFAASFE QKLQNLGIES
VSHDHLLNAE EASLIAMEYD LNPVVNSEAA IDLFSKPKPA DMSKYPLRPP IVAVLGHVDH
GKTTLLDTLR KSSVAAGEAG GITQHIGAFS VSLASRRTIT FLDTPGHAAF SAMRARGTHV
TDIVVLVVAA DDGVMPQTLE AIKHAKDAEV PMVVAINKID RYNANSQKVR EALLANGVEL
EEYGGETQCV EVSGLTGQGL DQLEEAIVTL AELSDLRAEV DIEAEGAVIE SQVEKGKGYV
ATVLVKRGTL KQGDVIVAGT TWCKVRMMTD EKSQIVKNAL PGTPVKITGW KELPIAGDEV
IQATDEELAK IVVANRELKR SRDQQLKDLE VINEKRRQRK QELETQRANF RSFKKEVWMF
HQGLLKEYPI AKQNINEEKP SSDTNIREIK ELNVVVKADV SGTSEAVVDA LHGLGNKEVR
VNVVDSGVGD ITESDIHMAN IAKAIVLGFN VKADKKVQLQ ARVDNVDMKF FKVIYHLLDE
VKEQLSKLLP PILEKHVTGE ATILQIFRIN VKGKEFKSVA GCRVTNGAIF KNQKVRILRN
NNQIWEGSLE TLKQVKKDIN EAKKGIECGI SFEGFTDFEE GDFIQSIVVK EIPRSL
//
