GenomeNet

Database: UniProt
Entry: W7WIN7_9BURK
LinkDB: W7WIN7_9BURK
Original site: W7WIN7_9BURK 
ID   W7WIN7_9BURK            Unreviewed;       458 AA.
AC   W7WIN7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
GN   Name=infB_2 {ECO:0000313|EMBL:EWS59744.1};
GN   ORFNames=Y694_02452 {ECO:0000313|EMBL:EWS59744.1};
OS   Methylibium sp. T29-B.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=1437443 {ECO:0000313|EMBL:EWS59744.1, ECO:0000313|Proteomes:UP000019360};
RN   [1] {ECO:0000313|EMBL:EWS59744.1, ECO:0000313|Proteomes:UP000019360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T29-B {ECO:0000313|EMBL:EWS59744.1,
RC   ECO:0000313|Proteomes:UP000019360};
RA   Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT   "Genome sequencing of the loss-of-function mutant Methylibium sp. T29-B.";
RL   Submitted (DEC-2013) 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:EWS59744.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AZSN01000059; EWS59744.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7WIN7; -.
DR   PATRIC; fig|1437443.4.peg.2484; -.
DR   Proteomes; UP000019360; 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   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 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; 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; PF04760; IF2_N; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
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          66..233
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          385..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..458
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   458 AA;  49742 MW;  D26485C706F72866 CRC64;
     MSVKASEVIK QLMKLGQMVT INQQLDQETA MILVEEMGHK AFTAKLDDPD AFLEDDVEVT
     DVPLEPRAPV VTVMGHVDHG KTSLLDYIRT TRVAAGEAGG ITQHIGAYHV ETPRGMITFL
     DTPGHEAFTA MRARGAKATD LVILVVAADD GVMPQTKEAI HHAKAAEVPL IVAINKIDKP
     GTNLERVRSE LIAEQVVPED FGGDSPFVQV SAKTGQGIDE LLEQVLLQAE VLELQAQVAA
     PAKGLVIEAQ LDKGRGPVAT VLVQSGTLKR GDVVLAGSTY GRVRAMLDEN GKPATEAGPS
     IPVEIQGLTE VPQAGDEFMV LSDERRAREI ATFRSGKYRD VKLSKQQAAK LENMFETMGQ
     GEVQTLPLII KPTCRARRRR WAPRCSSSAR PRSRCRSSTQ RWAASARATS TWPSRRRPSS
     SASMCGPMPV RASWPRATTS TCATTTSFTT RSTRSSRR
//
DBGET integrated database retrieval system