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Database: UniProt
Entry: A0A0W1R753_9EURY
LinkDB: A0A0W1R753_9EURY
Original site: A0A0W1R753_9EURY 
ID   A0A0W1R753_9EURY        Unreviewed;       600 AA.
AC   A0A0W1R753;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Probable translation initiation factor IF-2 {ECO:0000256|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=AUR64_14085 {ECO:0000313|EMBL:KTG08935.1};
OS   Haloprofundus marisrubri.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloprofundus.
OX   NCBI_TaxID=1514971 {ECO:0000313|EMBL:KTG08935.1, ECO:0000313|Proteomes:UP000054387};
RN   [1] {ECO:0000313|EMBL:KTG08935.1, ECO:0000313|Proteomes:UP000054387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB9 {ECO:0000313|EMBL:KTG08935.1,
RC   ECO:0000313|Proteomes:UP000054387};
RA   Zhang G., Stingl U., Rashid M.;
RT   "Haloprofundus marisrubri gen. nov., sp. nov., an extremely halophilic
RT   archaeon isolated from the Discovery deep brine-seawater interface in the
RT   Red Sea.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Function in general translation initiation by promoting the
CC       binding of the formylmethionine-tRNA to ribosomes. Seems to function
CC       along with eIF-2. {ECO:0000256|ARBA:ARBA00024852, ECO:0000256|HAMAP-
CC       Rule:MF_00100, 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|HAMAP-Rule:MF_00100,
CC       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:KTG08935.1}.
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DR   EMBL; LOPU01000029; KTG08935.1; -; Genomic_DNA.
DR   RefSeq; WP_058582088.1; NZ_LOPU01000029.1.
DR   AlphaFoldDB; A0A0W1R753; -.
DR   STRING; 1514971.AUR64_14085; -.
DR   OrthoDB; 30957at2157; -.
DR   Proteomes; UP000054387; Unassembled WGS sequence.
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; cd03703; aeIF5B_II; 1.
DR   CDD; cd16266; IF2_aeIF5B_IV; 1.
DR   CDD; cd01887; IF2_eIF5B; 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_A; IF_2_A; 1.
DR   InterPro; IPR029459; EFTU-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR004544; TF_aIF-2_arc.
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; TIGR00491; aIF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF14578; GTP_EFTU_D4; 1.
DR   Pfam; PF11987; IF-2; 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; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00100}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00100}.
FT   DOMAIN          13..228
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          142..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         22..29
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         138..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   600 AA;  65258 MW;  EA788A4CCAE952A6 CRC64;
     MSDTDQPPQS ETLRTPIVAV LGHVDHGKTS LLDKVRGSAV SEGEAGAITQ HIGATAVPLE
     TVSSMAGSLV DPDDFDLPGL LFIDTPGHHS FSTLRSRGGA LADIAILVVD VNDGFQPQTV
     EALDILKRTG TPFVVAANKV DTTPGWNPQD GSPIKPSYDG QSDRARQMLD TNLYEIIGQL
     SDEGLSADLY WRVQNFQKNI GVIPVSALTG EGIPDLLAVL MGLSQRYMKA EMAVDIAGPG
     AGTVLEVKEE RGFGATLDVV LYDGTVREGD TIVVGGTNGP IITEIRALLQ PQPLAEIRTE
     KRFERVDEVK AAAGVKIAAP DLDAAMAGAP VRVVRSRDTD EVIRDVQAEL AEIEVNTEEE
     GVVVKADTLG SLEAMANALK EAEIPILRAE VGDVAPRDVA VAGTAREDEH KVILAFNVDI
     LPNAEDELDH SEVKLFDDDV IYQLIEEYEE FVDERKRAQQ ETVLDKIVRP ARFRILQDHV
     FRQNDPAVVG VEIMSGTLKN NMRVVKFDGD KPTRVGQLSG IQEQGEDVKQ IRAGNRVSVA
     IDGPTVGRQI EEGDELWVEL PEKHAKILEQ ELSGEIPADE LEALQGYLDK HRRRDPFWGK
//
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