ID A0A0R0ARL1_9GAMM Unreviewed; 921 AA.
AC A0A0R0ARL1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=ARC20_08095 {ECO:0000313|EMBL:KRG44618.1};
OS Stenotrophomonas panacihumi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=676599 {ECO:0000313|EMBL:KRG44618.1, ECO:0000313|Proteomes:UP000051802};
RN [1] {ECO:0000313|EMBL:KRG44618.1, ECO:0000313|Proteomes:UP000051802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16536 {ECO:0000313|EMBL:KRG44618.1,
RC ECO:0000313|Proteomes:UP000051802};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (OCT-2015) 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}.
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:KRG44618.1}.
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DR EMBL; LLXU01000067; KRG44618.1; -; Genomic_DNA.
DR RefSeq; WP_057646092.1; NZ_PZOY01000006.1.
DR AlphaFoldDB; A0A0R0ARL1; -.
DR STRING; 676599.ARC20_08095; -.
DR Proteomes; UP000051802; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 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:UP000051802}.
FT DOMAIN 420..589
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 175..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..571
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 177..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 429..436
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 475..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 529..532
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 921 AA; 97925 MW; CB5DB3D8F3E660B4 CRC64;
MSQQTTIRKL AELVNTPVEK LLEQLATAGM KFSGPDQVVT STEKMKLLGF LRRTHGKSEA
SAESVGEAPK KITLNRRKVE EVTVSAGRSK TTVNVEVRQK RTYVKAAEAE APEAPRAAPA
APAAPVAEAP VAPAAPVAPV AAPPRNPAPA APIDPERAEI LRKLEASRAR NLAEQQALAE
VDRKRAEENE RKRQEAQAER DRVEAERKAA EAAARSGGAT ADAGSAAPAR PARPAPAAPR
APVAARPAAP RADDRNNNAA RHKTRGSHAM VAGVEDDDAT KRFAGQLHLS AADRARRSNV
RGKPKPTGGR RGFEQQRGGG GGGSGPHGFE RPTAPVVREI AIGETITVAD LAQKLALKGG
DVVKALFKMG VMATITQSID HDTAVLITEE LGHKAVRADS NDFEDALLAH SEEVQGEARP
RPPVVTIMGH VDHGKTSLLD YIRRTKIASG EAGGITQHIG AYHVETPKGV ISFLDTPGHA
AFTSMRARGA KLTDIVVLVV AADDGVMPQT KEAVQHAKAA GVPLIVAVNK MDKSDADPLR
VKNELLSQDV VAEEFGGDTQ FVEVSAKTGL GIDTLLDAIS LQAEVLELKA VPDGRASGTV
IESSLDKGRG PVATVLVQQG QLKKGDYLVC GIQYGRVRAL FDETGKQPDF AGPSIPVQVL
GLSGVPDAGD DFVVVEDERL AKDVAQQREA KRRETRLVSS AGNRMEDILA QMGKGEGQQV
LNLVIKADVQ GSVQALSQAL VALSNDDIRI NVIHAGVGGI TESDANSAVA SKATVIGFNV
RADASARKII EANGVDLRYF SIIYDVIDQV KQVASGLLGV EIREEIIGIA EVRDVFRSSK
FGAVAGCMIV EGVVKRSKPI RVLRDSVVVF EGELESLRRF KENVEEVRNG TECGIGVKAY
NDVKVGDQIE CFERIEVPRT L
//
