ID F9PHS9_9ACTO Unreviewed; 635 AA.
AC F9PHS9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
DE Flags: Fragment;
GN Name=infB {ECO:0000313|EMBL:EGV14222.1};
GN ORFNames=HMPREF9058_2712 {ECO:0000313|EMBL:EGV14222.1};
OS Actinomyces sp. oral taxon 175 str. F0384.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinomyces.
OX NCBI_TaxID=944560 {ECO:0000313|EMBL:EGV14222.1, ECO:0000313|Proteomes:UP000004281};
RN [1] {ECO:0000313|EMBL:EGV14222.1, ECO:0000313|Proteomes:UP000004281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0384 {ECO:0000313|EMBL:EGV14222.1,
RC ECO:0000313|Proteomes:UP000004281};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) 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|RuleBase:RU000644}.
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, ECO:0000256|RuleBase:RU000644}.
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:EGV14222.1}.
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DR EMBL; AFUR01000001; EGV14222.1; -; Genomic_DNA.
DR RefSeq; WP_009406299.1; NZ_AFUR01000001.1.
DR AlphaFoldDB; F9PHS9; -.
DR eggNOG; COG0532; Bacteria.
DR Proteomes; UP000004281; 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; IPR006847; IF2_N.
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; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR PRINTS; PR00315; ELONGATNFCT.
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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000256|RuleBase:RU000644};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU000644}.
FT DOMAIN 129..300
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGV14222.1"
SQ SEQUENCE 635 AA; 68422 MW; 12D7943AA76BCC2F CRC64;
FGRGGGAPRG RKSKRAKRQE FEQQSAPSIG GVIVPRGDGS TPVRVRQGAT LTDLAEKINA
NPAALVTVLF HLGEMATATQ SLDEDTFALL GAELGYNVQI VSPEDEDREL LESFDIDLEP
DEDDANLVPR PPVVTVMGHV DHGKTKLLDA IRSTDVVAGE AGGITQSIGA YQVRVNLNDE
ERPITFIDTP GHEAFTAMRA RGAEVTDIAI LVVAADDGVM PQTVEALNHA QAANVPIVVA
VNKIDKEGAN PDKIRGQLTE YGLVPEEYGG DTMFVDISAK QRLHIDELLE AVLLTADAAL
DLRANPDTEA RGVTIEAKLD KGRGAVSTIL VERGTLRVGD PIVAGSAYGR VRAMFNEHGE
NLTEAGPARP ALVLGLTNVP SAGDSFIVAP DDRTARQIAD KREAAERAAL LAKRRKRVSL
ENLTDVLKEG KVDTLNLILK GDSSGAVEAL EDSLLKIDVG EEVALRVIHR GVGAITQNDV
NLATVDSAVI IGFNVRPAER VSEIADREGV DMKFYSVIYN AIEDVEAAMK GMLKPVYEEV
ELGTAEIRQI FRSSKFGSIA GSIVRSGIIK RGTKARLVRD GVVINGDLSI ETLRREKDDV
TEVREGYECG INLGFKDLAE GDVIETWEMR EKPRD
//
