ID A0A1S1QTX4_9ACTN Unreviewed; 1076 AA.
AC A0A1S1QTX4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=BCD49_14360 {ECO:0000313|EMBL:OHV38143.1};
OS Pseudofrankia sp. EUN1h.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Pseudofrankia.
OX NCBI_TaxID=1834515 {ECO:0000313|EMBL:OHV38143.1, ECO:0000313|Proteomes:UP000179465};
RN [1] {ECO:0000313|Proteomes:UP000179465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EUN1h {ECO:0000313|Proteomes:UP000179465};
RA Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA Nouioui I., Abebe-Akele F., Thomas K., Gtari M., Tisa L.S.;
RT "Sequence Frankia sp. strain EUN1h.";
RL Submitted (JUL-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 -!- 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:OHV38143.1}.
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; MBLN01000045; OHV38143.1; -; Genomic_DNA.
DR RefSeq; WP_035931083.1; NZ_MBLN01000045.1.
DR AlphaFoldDB; A0A1S1QTX4; -.
DR Proteomes; UP000179465; 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; 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; 1.
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|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 569..741
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 46..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 578..585
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 628..632
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 682..685
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1076 AA; 107820 MW; 05E75BF396AD58FB CRC64;
MVGKARVHEL AKELGVDSKT VLGTLKEMGE FVKSASSTVE APVVRKLKER LGGEGEAPAA
RPAGRPAPGP TGNGARPGAG PRPFPGPTPG RPGPGPRPGP GGARPGPAAR PVSPGAGAPG
AGAPLPPSAG SPAAVGGPSA GGPSVGGSPA GGAEAPVAPA RPDTAPRPEV ARPAGAAASA
APQSPSQAGP RPGPRPAPSG PSGPSGGRPP RSGGPAAPGG SAGGPGAPGA AQAAAGGPSA
APTRPGGGPR PGPRPGPRPA GPGNNPYTTP GSAAGPRPGP PSAPGGPRSG APGRPGGAPG
AARQGGPGGP RPSPGGMPPR PGGSGGPRPG PGGGMPPRPG GSGGPRPGPG MFAPRPAGGA
PGRPAGPGAR PGGGGGGPRP GGGGGFAGRS GAPGRPGGAP GGGGAGRPGG PGGGGGGAGG
GRPAAGGRGR GGTTAGAFGP GGRGRPGRQR KSKRAKRQEW ESGLEAPRMG AMVPRGNGQA
IRLPRGASLA DFADKIDANP GAMVQVVFTQ LGEMVTATQS CTDETLQLLG VQLGYDVQIV
SPEDEDKELL ESFDLEFGGE YGDDVVLTTR PPVVTVMGHV DHGKTKLLDA IRSTDVVGGE
AGGITQHIGA YQVRSVVDGE ERPITFIDTP GHETFTAMRA RGAQVTDIVV LVVAADDGVK
PQTIEALNHA QAAGVPIVVA VNKIDKEGAD PAKVRGQLTE YGLVAEEYGG DTMFVDVSAR
NRTNIEGVLE AIVLTADASL DLQAAFDVEA QGVAIEGRLD RGRGPVATVL VQRGTLKIGD
SIVAGEAFGR VRAMLDENGA NVSEAGPARP VQVLGFTSVP DAGDNFLVVP EDRVARQIAE
RRQARERNAE LAMSRGRPTL ETILERMKEG EKTQLNLILK GDVSGSVEAL EDALLKIDLG
DEVGLRIIDR GVGAITETNV MLASASDALI IGFNVRPQGK ATELADREGV EVRYYSVIYQ
AIEDIENALK GMLKPVYEEA QLGTAEVREV FRVPRIGNVA GCIVRSGLIR RNSKARLIRD
GVVVADNLTV ESLKRFKDDV TEVRDGYECG IGLGSFNDIK IEDVIETFEQ REIPRA
//
