ID A0A0U3G0D1_9MICC Unreviewed; 981 AA.
AC A0A0U3G0D1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=MB46_03755 {ECO:0000313|EMBL:ALV44759.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALV44759.1, ECO:0000313|Proteomes:UP000055883};
RN [1] {ECO:0000313|EMBL:ALV44759.1, ECO:0000313|Proteomes:UP000055883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A3 {ECO:0000313|EMBL:ALV44759.1,
RC ECO:0000313|Proteomes:UP000055883};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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 -!- 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; CP013745; ALV44759.1; -; Genomic_DNA.
DR RefSeq; WP_058945566.1; NZ_CP013745.1.
DR AlphaFoldDB; A0A0U3G0D1; -.
DR KEGG; arw:MB46_03755; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000055883; 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 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; 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}.
FT DOMAIN 474..645
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 53..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 483..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 533..537
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 587..590
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 981 AA; 101539 MW; 961B6DFD2997A312 CRC64;
MAKARVHELA KELGITSKEA VSKLQELGEF VRSASSTIEA PVVKKLRDAF PMSASAGESK
PAAPAPAAPK AAEPKAPVAT QESAPAAPSA VVPGPKAPAP AAKPGAKATP AAPAPAVATP
AVAEPAAAAA PAAPAAATPA ATPKAAPKAA APGAPRPGNN PFATSQGMPR SGNRPERNEG
RSEGRSDNRG DNRAPRPAGA GAGAGAPRPG NNPFAPSQGM PRPGSSRNAE AGAAGPRPGG
PRPPAGAPRP GAPRPAGAPG AGGPRPAAGA PRPGGARPTP GMMPNRTERP AAPGRGNDRP
GAPGRGRPGA PGATPGGAPG GAPAGGGFGK GGRGRGGTQG AFGKGGAGRG KQRKSKRAKR
QELEQMSAPS LGGVTVPRGN GITVIRLRRG ASISDFADKI EANPAALVTV LFHLGEMATA
TQSLDEDTFA LLGAELGYKV QVVSPEDEER ELLSSFDIDF EAELEAEGDE DLELRPPVVT
VMGHVDHGKT RLLDAIRKSD VVADEHGGIT QHIGAYQIVH EHEGTDRRIT FIDTPGHEAF
TAMRARGAKV TDIAVLVVAA DDGVMPQTIE ALNHAQAANV PIVVAVNKID KEGANPEKIR
GQLTEYGLVP EEYGGDTMFV DVSARNGINI EELLEAVLLT ADAALDMRAN PNKDARGIAI
EANLDKGRGS VATVLVQSGT LHVGDTIVAG TAHGRVRAMF DENGDVITEA GPSRPVQVLG
LSNVPRAGDT FFVTGDERTA RQIAEKREAA DRNAALAKRR KRISLEDFDQ AVADGKVDTL
NLILKGDVSG AVEALEDSLL KIDVGEGVQL RVIHRGVGAI TQNDVNLATV DNAIIIGFNV
KPAERVAELA DREGVDMRFY SVIYGAIDDI ELALKGMLKP EYEEAELGTA EIREVFRSSK
HGNIAGSIVR SGIIRRNTKA RVLRAGKIIG DNLTVDSLKR FKDDATEVRT DFECGIGLGS
FNDLQAEDII QTFEMREKPR V
//
