ID K0BCD1_9ARCH Unreviewed; 586 AA.
AC K0BCD1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 59.
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=NSED_00970 {ECO:0000313|EMBL:AFS82006.1};
OS Candidatus Nitrosopumilus sediminis.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=1229909 {ECO:0000313|EMBL:AFS82006.1, ECO:0000313|Proteomes:UP000006100};
RN [1] {ECO:0000313|EMBL:AFS82006.1, ECO:0000313|Proteomes:UP000006100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR2 {ECO:0000313|EMBL:AFS82006.1,
RC ECO:0000313|Proteomes:UP000006100};
RX PubMed=23209211; DOI=10.1128/JB.01869-12;
RA Park S.J., Kim J.G., Jung M.Y., Kim S.J., Cha I.T., Ghai R.,
RA Martin-Cuadrado A.B., Rodriguez-Valera F., Rhee S.K.;
RT "Draft Genome Sequence of an Ammonia-Oxidizing Archaeon, "Candidatus
RT Nitrosopumilus sediminis" AR2, from Svalbard in the Arctic Circle.";
RL J. Bacteriol. 194:6948-6949(2012).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; CP003843; AFS82006.1; -; Genomic_DNA.
DR AlphaFoldDB; K0BCD1; -.
DR STRING; 1229909.NSED_00970; -.
DR KEGG; nir:NSED_00970; -.
DR PATRIC; fig|1229909.8.peg.203; -.
DR eggNOG; arCOG01560; Archaea.
DR HOGENOM; CLU_002656_3_3_2; -.
DR Proteomes; UP000006100; Chromosome.
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; 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 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 1..214
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 70..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 586 AA; 65270 MW; C475CD6BD767140F CRC64;
MAVLGHVDSG KTSLLDRIRG TGVQGREAGG ITQHIGASFL PTETIKEMCG PLYKKLEQAE
NKVPGILVID TPGHEVFTNL RSRGGSAADI AILVVDVNRG FQPQTNESLK ILQSRKVPFV
VALNKCDQIS GWRKSETQFI SQAIKEQDAS IQADLDQKIY DVVGTLSILG YKSEAFYRVE
DFKSEIAIVP ISARSGVGIP ELLSVLVGLT QQYLQKRLNQ DEKEPRGIVL EVKDEVGLGQ
TANIILIDGI IRKEDSIVVA KRDAVIVTKP KALLLPKPLD EMRDPRDKFK PVPQVEAAAG
LKIASPDLEG VLPGSTLYVA RNNEEIEKYT KLIESEMKSV FVDTETNGVI LKCDTIGSLE
AIMEMLKRSQ VPVSKADIGP VTRRDVIEAK AIKEKDRHLG VVLAFNVKIL PDAKEESETN
HIKLFEDKVI YSLIDNYNAW VEEDSANEED AMFAELTPIS KFTFMKGMVF RNNNPAVFGV
RVDVGNLKHK IPFMNMKGHK VGYIHQLQLD KKTVSSAKAG DEVACSVKDV TIGRQIFEEE
VYYTFPPSHE AKQILKKFMH KLSPEEQEVF NDIVRIQREI EPVYAY
//
