ID A0A0N7JYZ0_9PSEU Unreviewed; 1009 AA.
AC A0A0N7JYZ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-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=AD017_05475 {ECO:0000313|EMBL:ALL80796.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL80796.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL80796.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL80796.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
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; CP012184; ALL80796.1; -; Genomic_DNA.
DR RefSeq; WP_060573286.1; NZ_CP012184.1.
DR AlphaFoldDB; A0A0N7JYZ0; -.
DR STRING; 1096856.AD017_05475; -.
DR KEGG; pecq:AD017_05475; -.
DR PATRIC; fig|1096856.3.peg.1149; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000066228; 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; PR01217; PRICHEXTENSN.
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:UP000066228}.
FT DOMAIN 504..675
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 28..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..126
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 513..520
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 563..567
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 617..620
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1009 AA; 103694 MW; 44381A3F4656FB61 CRC64;
MAGKARVHEL AKELGLSSKQ VLSKLQDLGE YVKSPSSTVE APVARKLRDA MAAGGGNGGG
NGQRRGSGAP GGGRPRAGGG GSGAPSPSRP SAPKPGPTPG AAPSRPGPAP KPGPRPGPPA
PAQGAPSPAQ PAAGQDAPKP GPATPAPTPH PQAPAADASA PAAPRPGPAA PKPGPKPGPA
APKPGPKPGE QGQGGGQGGG APRPGGDGQR GPKPGPRQPR VGNNPFGVGQ GSPKPAPRPG
PPAQQPGGQQ QGGGAAPQQP AARSGEAPPR PPRPGGGAGG PRPTPNSMPP RPNPGMMPAR
PAGGRPGPGG RGGPGGGRGG PGGGRGGPGG GRPGGGGGGG FRPGGGGPGG PPPAGGFRGR
PGGGGGRGRG GAAGAFGRPG GPARRGRKSK RQKRQEYDAM AAPSVGGVRL PKGNGETIRL
PRGASLTDFA EKINANPASL VQVLFHLGEM VTATASVSDE ILELLGQEMN YRVQVVSPEE
EDRALLESFD IEFGDLGDEE ALVARPPVVT VMGHVDHGKT RLLDTVRKAN VREGEAGGIT
QHIGAYQVPA ELEGEERLIT FIDTPGHEAF TAMRARGAKS TDIAVIVVAA DDGVMPQTVE
SINHAQAADL PIVVAVNKID VEGANPQKIR QQLTEYNLVA EEFGGDTMFV DISAKQGTNI
ESLLEAILLT ADAALDLRAN PDMDAQGVTI EGHLDRGRGP VATVLVQRGT LKVGDSVVAG
DASGRVRRMI DEHGADVTEA LPSRPVQVIG LTSVPGAGDT FLVVDEDRVA RQIADRRRAR
ERNAELASRR KRVSLEDLDA ALKETNTLNL IIKGDNSGTV EALEEALMKL DVGDDVDLRV
IHRGVGGITE GDINLAIADN VIVMGFNVRA EGKATELANR EGVEIRYYSV IYQAIEEIEQ
ALKGMLKPEY EEVELGRAEV REVFKSSKFG TIAGCLVMGG EIRRNARARL LRDSKVIHEN
LPVSSLRRYK DDVVEVREGF ECGLTLGSYS DIKVDDVIET FEMREKPRD
//
