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Database: UniProt
Entry: A0A1D2X148_9EURY
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ID   A0A1D2X148_9EURY        Unreviewed;       613 AA.
AC   A0A1D2X148;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=NL43_06990 {ECO:0000313|EMBL:OED29656.1};
OS   Methanosphaera sp. WGK6.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=1561964 {ECO:0000313|EMBL:OED29656.1, ECO:0000313|Proteomes:UP000094737};
RN   [1] {ECO:0000313|EMBL:OED29656.1, ECO:0000313|Proteomes:UP000094737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WGK6 {ECO:0000313|EMBL:OED29656.1,
RC   ECO:0000313|Proteomes:UP000094737};
RX   PubMed=27022996; DOI=10.1038/ismej.2016.41;
RA   Hoedt E.C., Cuiv P.O., Evans P.N., Smith W.J., McSweeney C.S., Denman S.E.,
RA   Morrison M.;
RT   "Differences down-under: alcohol-fueled methanogenesis by archaea present
RT   in Australian macropodids.";
RL   ISME J. 10:2376-2388(2016).
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:OED29656.1}.
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DR   EMBL; JRWK01000014; OED29656.1; -; Genomic_DNA.
DR   RefSeq; WP_069593338.1; NZ_JRWK01000014.1.
DR   AlphaFoldDB; A0A1D2X148; -.
DR   STRING; 1561964.NL43_06990; -.
DR   PATRIC; fig|1561964.3.peg.1395; -.
DR   OrthoDB; 30957at2157; -.
DR   Proteomes; UP000094737; 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          3..220
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         76..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   613 AA;  68145 MW;  0FDC336724CC158E CRC64;
     MKTRSPIVSV LGHVDHGKTT LLDNVRGSTI AAREAGGITQ HIGATEIPMD VISSICGEFL
     EKMNIQEQLP GLFFIDTPGH EAFTTLRKRG GSLADLAILI LDVTEGFKPQ TYEALNILKS
     SKTPFVVAAN KIDNIPGWNS MKNTSFTESV QNQHSKVVFD LDQRLYEIVG TLHEEGFESE
     RFDRISNFAS QITIVPISAK TGEGLPELLT MLLGLAYQYL SEQLQIEENS PAAGTVLEVK
     EEKGLGLTID TILYDGVLNK EDHIMMLTKD NKIISTKIRS LLKPKPLEEI RESKTLFEDT
     DQIVAAAGVK IVAPHVDDVI AGSPLKVAND GDKSVEEELL SEVDNIRIQT NDVGIIVKAD
     TLGSLEALVN ILDSKDIPIK SAEIGDISRR DIINASIMHK EDEKYGVVIA FNVNILPSAE
     EELHDQEIKV FQDKVIYQLT EDYLEWVVTA KERQKKQKLA SIIRPSKIRI IPKLVFRHSK
     PAIAGIEVMS GIIEKGVTLI NEKGHEVGIV DSMEDNGESL QKTSRGSQVA MAISGAVFEK
     DFEEGDVLYV DMSERNFLAL GDELGDKLLE DELLTMDELR EIKQQIEDPN WGIINTDWSE
     LDTLDEDEYE DFY
//
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