ID F4EUT7_SELS3 Unreviewed; 818 AA.
AC F4EUT7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 OrderedLocusNames=Selsp_1152 {ECO:0000313|EMBL:AEC00112.1};
OS Selenomonas sputigena (strain ATCC 35185 / DSM 20758 / VPI D19B-28).
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=546271 {ECO:0000313|EMBL:AEC00112.1, ECO:0000313|Proteomes:UP000011124};
RN [1] {ECO:0000313|EMBL:AEC00112.1, ECO:0000313|Proteomes:UP000011124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35185 / DSM 20758 / VPI D19B-28
RC {ECO:0000313|Proteomes:UP000011124};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Selenomonas sputigena DSM 20758.";
RL Submitted (APR-2011) 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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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}.
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DR EMBL; CP002637; AEC00112.1; -; Genomic_DNA.
DR RefSeq; WP_013740793.1; NZ_GG698596.1.
DR AlphaFoldDB; F4EUT7; -.
DR KEGG; ssg:Selsp_1152; -.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000011124; Chromosome.
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; 1.10.10.2480; -; 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; 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; 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; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
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:UP000011124}.
FT DOMAIN 293..462
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 54..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..444
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT REGION 793..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302..309
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 348..352
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 402..405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 818 AA; 88676 MW; 0F7D689FC144556F CRC64;
MSKYRVYELA KEFHTESKVV LDILTRNKFR VANHMSSVGE EERAVVARAF APKKTVSDAP
KAPVTDAARK ASQNKPRQQA QGQPQKNAND RKQNRSSNGS ASAAATNRPR QGGAPQQKRG
QGAASSNGSN ATKRPPQDKR GGNTNQRNNN AQGSNRNRSG NAAGAGNANN AGGWNNRGGV
NNRGKFGNKN NRGRNNQRQK QQAPKVEIAH PTHIKVGESI AVKDLASKMS YTATEVIKKL
MLMGIMATIN QEIDYETAAL VAIEFGVTCE ELPPETDPTE IPEIEDDPKS LVVRPPVVTV
MGHVDHGKTS LLDAIRKTSV STHEAGGITQ HIGAYQVMCQ GKKIVFLDTP GHEAFTAMRA
RGAQVTDIAI LVVAADDGVM PQTVEAINHA KSAGVPIIVA INKIDKPGAN PEHVKQELSE
HELIPEDWGG DTIMVPVSAK QKQGINDLLE MVLLVAEVKE LKANPNRDAR GVIIEAQLDK
GRGPVATVLV QNGTLRIGDS IIAGTTFGKV RAMINDRGEN VKKAGPSVPV EVLGLSDVPE
AGDVLASLDE KLARSIASKR IEKKRTELIR SKKVSLDDLF QQIQDGNIKD LNIVIKADVQ
GSVEALANSL LSLNKNDEVR VNIVHSGVGA VNESDVMLAT ASNALIIAFN VRPDANARRV
ADAESIDIRT YRVIYDALND VKDAMSGMLA PKYKEVVQGK VEIRQVMKFS KALVAGSYVL
EGKITNSSKI RILRDNIVAF DGELDSLRRF KDDVKEVAAG YECGITIKDY RDFQEGDIIE
AYTMEEIETS ITEANKEAAK RRDQQEQTKK DSPAENDA
//
