ID A0A013VJ17_9SPHN Unreviewed; 780 AA.
AC A0A013VJ17;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
DE Flags: Fragment;
GN ORFNames=BF95_24665 {ECO:0000313|EMBL:EXS68427.1};
OS Sphingobium sp. Ant17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1461752 {ECO:0000313|EMBL:EXS68427.1, ECO:0000313|Proteomes:UP000021537};
RN [1] {ECO:0000313|EMBL:EXS68427.1, ECO:0000313|Proteomes:UP000021537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ant17 {ECO:0000313|EMBL:EXS68427.1,
RC ECO:0000313|Proteomes:UP000021537};
RA Adriaenssens E.M., Cowan D.A.;
RT "Draft genome sequence of the aromatic hydrocarbon-degrading bacterium
RT Sphingobium sp. strain Ant17 isolated from Antarctic soil.";
RL Submitted (FEB-2014) 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:EXS68427.1}.
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DR EMBL; JEMV01000079; EXS68427.1; -; Genomic_DNA.
DR RefSeq; WP_043154390.1; NZ_JEMV01000079.1.
DR AlphaFoldDB; A0A013VJ17; -.
DR STRING; 1461752.BF95_24665; -.
DR PATRIC; fig|1461752.3.peg.4815; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000021537; 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 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 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 281..451
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 31..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EXS68427.1"
SQ SEQUENCE 780 AA; 84088 MW; 5861588BD5158073 CRC64;
PPRQQQPVRT TPPQSLMSRQ ELQAKLLREA EEARMNAQED ARRREDAARL AAIEAEKRRA
EDNRQAAETA ASAPAVEEAP APAPVVEEAP AAPQEAVAEP VAASAEADAG ASAAPTAAAA
PPPRRFTPVT PVKRPEPTKP ERAKKGEDNR RQAGKLTVTK ALADDDSARA RSLAALKRAR
EKERRAHYAG GSKTREKQSR DVIVPEVITV QELANRMAEK GADLVKSLFK MGQAVTLNQS
IDQDTAELLV EEFGHRIQRV SDADIEIGIE GEADAVEALK TRAPVVTIMG HVDHGKTSLL
DALRGTSVVS GESGGITQHI GAYQVTTKKG DVITFLDTPG HEAFSEMRAR GANVTDIVIL
VVAADDGLMP QTIEAINHTK AAGVPMIVAI NKVDKPDANP QKVRERLLSE EIVVEDMGGD
VQDVEVSALK KTGLDELIEK ILLQAELMEL TANPDRAAEG NVIEAQLDRG RGAVATVLVR
KGTLKVGDTF VIGAESGKVR ALINDKGQQV KSAGPSTPVE ILGLSGVPMA GDQMTVVENE
ARAREVAAYR QEQITRKRTA SVPTNFENMF SALSTKVIEY PVVIRGDVQG SVEAIVSALN
RISTDEIKVR ILSSGVGAIT ESDVTLASAS RAPLIGFNVR PNAKARPLAI REKISLRYYD
VIYDLLEEVR NEMAGQLAPE RIETIVGRAE VLQVFPAGKK DKAAGLLVME GIIRKGLNAR
LTRDDVIVSK TVIHSLRRFK DDVSEVRAGM ECGAVLQDTN DIKAGDTLEL FEVEERIRTL
//
