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Database: UniProt
Entry: R9LCL4_9FIRM
LinkDB: R9LCL4_9FIRM
Original site: R9LCL4_9FIRM 
ID   R9LCL4_9FIRM            Unreviewed;       705 AA.
AC   R9LCL4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
DE   Flags: Fragment;
GN   ORFNames=C814_02762 {ECO:0000313|EMBL:EOS56455.1};
OS   Anaerotruncus sp. G3(2012).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=1235835 {ECO:0000313|EMBL:EOS56455.1, ECO:0000313|Proteomes:UP000014129};
RN   [1] {ECO:0000313|EMBL:EOS56455.1, ECO:0000313|Proteomes:UP000014129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G3(2012) {ECO:0000313|Proteomes:UP000014129};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anaerotruncus bacterium G3.";
RL   Submitted (APR-2013) 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,
CC       ECO:0000256|RuleBase:RU000644}.
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|RuleBase:RU000644}.
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:EOS56455.1}.
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DR   EMBL; ASTA01000081; EOS56455.1; -; Genomic_DNA.
DR   AlphaFoldDB; R9LCL4; -.
DR   STRING; 1235835.C814_02762; -.
DR   PATRIC; fig|1235835.3.peg.2908; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_406858_0_0_9; -.
DR   Proteomes; UP000014129; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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   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   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000256|RuleBase:RU000644};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW   ECO:0000256|RuleBase:RU000644};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014129}.
FT   DOMAIN          207..374
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EOS56455.1"
SQ   SEQUENCE   705 AA;  77561 MW;  B4FC82CE39A77C16 CRC64;
     QQQGGQRQQG GQQNRGNQQR QDNRQGGQQQ NQQAPQQQKP RQRPQGGMTV DTRAGSTQVE
     MEKYNEKYDN LAQSKLGNRD TAAQKQKLTQ RSAQRRAGKP VMSRKEKEDA KMRRLELERQ
     RRKNLSITIP EEITVGELAA RLHVTSAEII KRLMGLGVMA TVNETLDFDT ASMVSIEIGA
     KVEKEVVVTI EDRLFEVEED DDDKMVERPP IVVVMGHVDH GKTSLLDAIR NANVTAGEAG
     GITQHIGAYQ VLVNDRPVTF LDTPGHAAFT SMRARGAQVT DIAVIVVAAD DGIMPQTVEA
     INHAKAAGVS IIVAVNKMDK PHANPDKVMQ ELTEYELVPE EWGGDVPCIK VSAKTSEGIP
     DLLEMIQLVA DTSELKANPD KMAKGTVIEA KLDKGRGPVA TILVQSGTLH TGDVVIAGTA
     IGRVRVMMND RGEKVAEATP SMPVEITGLG DVPEAGDVFN AVEDERLAKE LVDQRKFENK
     QQQFSSYEKV TLDNLFSHIS QGDMKELPII VKADVQGSVE AVKQSLEKLS NDEVRVKVIH
     GAVGAVSESD VMLADASNAI IVGFNVRPDP MAKDNAERDG VELRLYRIIY DAINDVETAM
     KGMLAPKTRE VELGRAEIRQ VYKITNVGTV AGCYVLEGKI TRNAEIRVVR DGIIIADDHL
     SSLKRFKDDV KEVAKGYECG MGLNKFNDLK EGDIFEAYEI EEYRE
//
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