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Database: UniProt
Entry: A0A0A0EHX3_9RHOB
LinkDB: A0A0A0EHX3_9RHOB
Original site: A0A0A0EHX3_9RHOB 
ID   A0A0A0EHX3_9RHOB        Unreviewed;       830 AA.
AC   A0A0A0EHX3;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=ATO9_07780 {ECO:0000313|EMBL:KGM49895.1};
OS   Pseudooceanicola atlanticus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Pseudooceanicola.
OX   NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM49895.1, ECO:0000313|Proteomes:UP000030004};
RN   [1] {ECO:0000313|EMBL:KGM49895.1, ECO:0000313|Proteomes:UP000030004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-s11g {ECO:0000313|EMBL:KGM49895.1,
RC   ECO:0000313|Proteomes:UP000030004};
RX   PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA   Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT   "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT   seawater of the Atlantic Ocean and reclassification of Oceanicola
RT   batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT   nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT   Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT   Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT   comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT   flagellatus comb. nov.";
RL   Antonie Van Leeuwenhoek 107:1065-1074(2015).
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|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100}.
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|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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:KGM49895.1}.
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DR   EMBL; AQQX01000002; KGM49895.1; -; Genomic_DNA.
DR   RefSeq; WP_043747433.1; NZ_CP051248.1.
DR   AlphaFoldDB; A0A0A0EHX3; -.
DR   STRING; 1461694.ATO9_07780; -.
DR   eggNOG; COG0532; Bacteria.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000030004; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
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; IPR013575; IF2_assoc_dom_bac.
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; 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   Pfam; PF08364; IF2_assoc; 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.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000030004}.
FT   DOMAIN          328..498
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         337..344
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         384..388
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         438..441
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   830 AA;  89294 MW;  1B6722796CF5F765 CRC64;
     MSDNDGKKTL GVRGGGSRPG NVKQSFSHGR TKNVVVETKR KRVVVPKSGA GKSGGGAGSV
     GDPSKRPAGI TDAEMDRRLK AVQAAKAREA EEAAQREAEE KAREEERQRR REEAEAKERE
     EREREAALKA KQEEEERAKR DAEEAAKRAA AAAAQPAPPE DGAPARKTAP ANRGAERPAR
     ANDREDRGGR GKGDKSDGRR SGKLTLNQAL SGGEGGRQKS MAAMKRKQER ARQKAMGQNT
     VREKVVRDVQ VPEAIMVGEL ANRMAERVAD VVKALMQNGM MVTQNQTIDA DTAELIIEEF
     GHNIVRVSDA DVEDVIKEIE DKEEDLKPRA PVITIMGHVD HGKTSLLDAI RDAKVVAGEA
     GGITQHIGAY QVTTDGGQVL TFLDTPGHAA FTSMRARGAQ VTDIVVLVVA ADDAVMPQTI
     EAINHAKAAE VPMIVAINKC DKPEANPTKV RTDLLQHEVI VEEMSGEVQD VEVSAHTGQG
     LDELLEAIAL QAELLELKAN PDRAAQGAVI EAQLDVGRGP VATVLVQSGT LRQGDVFVVG
     EQWGKVRALV NDRGERVKEA GPSVPVEVLG LNGTPEAGDV LNVTSTEAQA REIAEYRENA
     AKEKRAAAGA ATTLEQLMQK AKEDENVTEM PILVKADVQG SAEAIVQAME KIGNDEVRVR
     VLHAGVGAIT ESDVGLAEAS GAPVFGFNVR ANAPARNAAN QKGVEIRYYS VIYDLVDDVK
     AAASGLLSAE IREKFIGYAQ IKEVFKVTGV GRVAGCLVTE GVARRSAGVR LLRDDVVIHE
     GTLKTLKRFK DEVSEVISGQ ECGMAFENYE DIRPDDVIEI FEREEIERTL
//
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