ID A0A172RYG8_9ACTN Unreviewed; 920 AA.
AC A0A172RYG8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=SAMN02910314_01150 {ECO:0000313|EMBL:SEO77169.1};
OS Denitrobacterium detoxificans.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Denitrobacterium.
OX NCBI_TaxID=79604 {ECO:0000313|EMBL:SEO77169.1, ECO:0000313|Proteomes:UP000182975};
RN [1] {ECO:0000313|Proteomes:UP000182975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21843 {ECO:0000313|Proteomes:UP000182975};
RA Varghese N.;
RL Submitted (OCT-2016) 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|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000645}.
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; FOEC01000006; SEO77169.1; -; Genomic_DNA.
DR RefSeq; WP_066662720.1; NZ_FOEC01000006.1.
DR AlphaFoldDB; A0A172RYG8; -.
DR STRING; 79604.AAY81_06170; -.
DR KEGG; ddt:AAY81_06170; -.
DR PATRIC; fig|79604.3.peg.1248; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000182975; 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; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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|ARBA:ARBA00022490, 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:UP000182975}.
FT DOMAIN 421..590
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 71..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..572
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 71..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 430..437
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 476..480
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 530..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 920 AA; 100828 MW; 946B5FBC41F6DE0C CRC64;
MAIMRVHELA KELNMTSKEL LDRLAEMKIP AKSHASVLND AYVDKIRKNL APELKERAGI
IDDEEARKLA EEKAEAEAKK AEEEAERRAA VEAERAQREA ERAKRQQQAA ESEEDTEEAQ
ADQAPAVKRP PSPYANLAEQ IAAEKERVAR EAAEAKARAR MAAVQRDVAK KQAVEQRLHA
SRSKSSHKST EQAAAPKAPT RAVPTTSSRF DSLLSQIESE KQRLQQSKQE AAARAKAARG
NAPARGKKGR HNGHTFEPDV PELAGQQVES GEDRYAQMAV KAEKLQRDKV LSEARAAVAA
ASHEGEGRRR KRKEKRQAEA RERAEMEAIQ KGLDPSLVLD DSVIEIPQGA TVQKFAELLG
VAPNDVIKRL FMLGQVLTLT QSMSDDLIEL ISDDMGRKVR VVNPEEEYAV VYNDSEEDLK
PRPPVVTVMG HVDHGKTSLL DAIRETGVAE REAGGITQAI GASVVDLNGR QVTFIDTPGH
EAFTAMRARG ASITDVVVLV VAADDGVMPQ TVEAINHAKA ADVPIVVAVN KIDKPGATPD
RVRQELTEYG IIPEEWGGKN MFVDVSAKKR LHIDDLLETI LLQADVLELK ANPNADASGY
VIESKLDKGR GPVATVLVAR GTLHPGDTVV AGTSYGRVRA LIDPRGEHRD EAYPADPVEI
LGLNSVATAG DEFRVFEDER DARKLAEERA LRKRLKQQEA SHMSLDDLFN RIEEGKTTDL
NLVVKADVDG SIEALRGAFD KMDQSEVKIN IIHAAVGGIT ETDVTLAAAS DAIIIGFNVR
PMGKSKQMAE KEKVDIRLYR VIYQAIEDIN AARVGLLSPD IVEKDTGIVE VRETFKVPKV
GTIAGAYVME GEISRDDRVR IVRDGTVVYE GTIASLRRFK DDVKSVRSGY ECGIGIDGYQ
DIKVGDTIEG YKTVEVERTE
//
