ID A0A841DQM5_9ACTN Unreviewed; 1163 AA.
AC A0A841DQM5;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 02-APR-2025, entry version 16.
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=HDA44_002331 {ECO:0000313|EMBL:MBB5978990.1};
OS Kribbella solani.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=236067 {ECO:0000313|EMBL:MBB5978990.1, ECO:0000313|Proteomes:UP000558997};
RN [1] {ECO:0000313|EMBL:MBB5978990.1, ECO:0000313|Proteomes:UP000558997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17294 {ECO:0000313|EMBL:MBB5978990.1,
RC ECO:0000313|Proteomes:UP000558997};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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|ARBA:ARBA00004496,
CC 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}.
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:MBB5978990.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JACHNF010000001; MBB5978990.1; -; Genomic_DNA.
DR RefSeq; WP_184833671.1; NZ_BAAAVN010000001.1.
DR AlphaFoldDB; A0A841DQM5; -.
DR Proteomes; UP000558997; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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 FunFam; 1.10.10.2480:FF:000003; Translation initiation factor IF-2; 1.
DR FunFam; 2.40.30.10:FF:000007; Translation initiation factor IF-2; 1.
DR FunFam; 2.40.30.10:FF:000008; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.10050:FF:000001; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.300:FF:000019; Translation initiation factor IF-2; 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; IPR053905; EF-G-like_DII.
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.
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; PF22042; EF-G_D2; 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 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.
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:UP000558997}.
FT DOMAIN 656..827
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..134
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..212
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..259
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..331
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..348
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..359
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..403
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..531
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..544
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 665..672
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 715..719
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 769..772
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1163 AA; 116215 MW; A7FB4E507718D178 CRC64;
MAKVRVYELA KELGVTSKVV LTRLNDMGEF VRSASSTIEA PVVRRLAEEF EKNPPKKRAA
KKAAASTSAA PQATAPVPGA PAQSAPAAPA DRAAAQPGAA TQSGSDAAAQ SGAPVSSGSG
ASGRPAPSGA TPGARPGPRP GPKPGPRQEA APADSIAAAT GTTDAPATAP GSGSAAAAGS
AAGSGSAVPG GSAPAAGGSA APVGTGSAAP GTPGAGSAGS VAPGTPGAGS ATPGAGSSAG
SAGSGIGSAT PGAGSATSGD VAREGAASSA TPSFEAPAAK AAPAPGPRRT GGDAARGDGS
ARPGPRPGGQ GSGPRPSGQA GAPRPGGSAP RPGAPGAGAR PGAPRPGGSQ QGGEGGGAPR
PGAPRPGGAP RPGAPRPGNN PFSSTQGMQR GGRPGPGGQG GGDRQAPSPA GMAPRPPQNR
QDGGRGGNDR PRPSGGVPGA PRPNPAMMPK SSAGTFTGRP GGGSGGPGGP GGNRGGRPGG
GPGGGPRGGG GGGGGFRPGG GPSGPPGGGG GRPGPGNRGR GGTQGAFGRP GGPARRGRKS
KRAKRQEFDN MQAPAVGGVR VKHGDGEVVK LPRGASLTDF AEKVGVDPAS LVQVLFHLGE
MVTATQSVNE ETLELLGTEL NYDVQIVSPE DEDRELLQSF DIDFGNDEGD EGDLAARPPV
VTVMGHVDHG KTKLLDAIRM ANVQAKEAGG ITQHIGAYQV TTEVDGQERA ITFVDTPGHE
AFTAMRARGA QATDIVILVV AADDGVMPQT IEALNHARAA GVPIVVAVNK IDVPAADPTK
VRGQLTEYGL VPEEYGGDTM FVDVSAKSRI NIEGLLEGVV LTADAALDLR ANPKMHAEGI
AIEANLDKGR GPVATVLVQR GTLRVGDSMV VGPAYGRVRA MLDEHGDPVE EATPSRPVLV
LGLTAVPGAG DKFLVVDDDR MARQIAEKRE ARARAAANAK RRARRTLEDF MASMEKGEAQ
ELLLILKGDV SGSVEALEDA LVRIEVGDEV NLRIIDRGVG AINENDVNLA IASNAVIIGF
NVRPAGKAGD LAEREGVDVR YYSVIYSAID DIEAALKGML KPIYEEATLG QAEIREIFRS
SKVGNIAGCW VTSGLIRRNA KVRLIRDGAV VVDNTELSSL KRFKDDASEV REGFECGLTI
NNFNDIKVGD VVEAFELREK PRS
//
