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Database: UniProt
Entry: W3AQA7_9FIRM
LinkDB: W3AQA7_9FIRM
Original site: W3AQA7_9FIRM 
ID   W3AQA7_9FIRM            Unreviewed;       921 AA.
AC   W3AQA7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
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=UYO_0868 {ECO:0000313|EMBL:ETP73185.1};
OS   Lachnospiraceae bacterium JC7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1165092 {ECO:0000313|EMBL:ETP73185.1, ECO:0000313|Proteomes:UP000018967};
RN   [1] {ECO:0000313|EMBL:ETP73185.1, ECO:0000313|Proteomes:UP000018967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC7 {ECO:0000313|EMBL:ETP73185.1,
RC   ECO:0000313|Proteomes:UP000018967};
RA   Rosewarne C.P., Cheung J.L., Evans P.N., Tomkins N.W., Denman S.E.,
RA   O Cuiv P., Morrison M.;
RT   "Isolation and genomic characterisation of Lachnospiraceae sp. JC7, a newly
RT   identified member of the bovine rumen core microbiota.";
RL   Submitted (JUL-2012) 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|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:ETP73185.1}.
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DR   EMBL; ALYD01000006; ETP73185.1; -; Genomic_DNA.
DR   AlphaFoldDB; W3AQA7; -.
DR   PATRIC; fig|1165092.3.peg.869; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000018967; 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; 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.
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          416..589
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..314
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         425..432
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;  101144 MW;  9E2E4EB31583FAE2 CRC64;
     MSDENQKENG LNSKDEKKGE APKKKKLAVV FHSQNSANHK NHPLGGKLST AKEQGARKTQ
     QASEQKAQSE KPKKTSPNGR PLPPGTARVT PLRELNELQK RQAEEEAKRE AERKAQEEEA
     RRKAAEEAKR EAERKAQEEE ARRKAAEAAK SAPSVSERSS DRPQRTADRP RFDRSGDRND
     RNGDHQSRPA FGQRNDRNGD RPQGGFRKDG ARPAAGTGRP ADRNGQQRPG QRPAGFGGQR
     RPQEASTVAV DISSKPTAGR NAHKPGDKNF GNKNFDNEKA EAAKRNRNNR KQNKYTAEQS
     YERDDEMAAR KKKTGKGAFI KPEVVKPVEE EIKSITIPEV ITIKELADKM KIKPADIIKK
     LFMKGQMVTL NTELSYEEAE NIAVDYDILC EQEEKIDVIA ELVKDDIEDT DADMVSRPPV
     VCVMGHVDHG KTSILDAIRN TNVTAKEAGG ITQSIGAYQV SVKVNDEDRV ITFLDTPGHE
     AFTAMRMRGA QSTDIAVLVV AADDGVMPQT VEAINHAKAA NTPIIVAINK IDKEGANPDR
     VKQELMKYDL VPEDYGGDTI CVPVSAKKNI GIEDLLENVV LEADVMELKA NQNRSAYGVV
     IEAELDKGRG SVARLLIQKG TLHQGDVVAV GSAYGKVRAM TDDKGRRIKK AGPSQPCEIL
     GLNAVPNAGE IFQVKDSEKE AKAYAAAFVT ESKQKKVEES KKKVSLDALF DQIKAGEIKE
     LPIVIKADVQ GSVEAVKDSL EKIKNDEVAV KVIHAGVGAI SESDVVLASA SNAIVIGFDV
     KPDATAKEIA ERENVDVRLY NIIYKAIEDI EDAMKGMLAP VYEEKVIGHA EIRQIFKASG
     VGNIAGCMVK DGLVQRGAKA RIMRGPKQDQ IFEGEIASVK RFKDDVKEVK AGYECGLVFD
     GFNEIEIDDY VEVYVMEEVK R
//
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