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Database: UniProt
Entry: K5XHN2_AGABU
LinkDB: K5XHN2_AGABU
Original site: K5XHN2_AGABU 
ID   K5XHN2_AGABU            Unreviewed;       611 AA.
AC   K5XHN2;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN   ORFNames=AGABI1DRAFT_53272 {ECO:0000313|EMBL:EKM82797.1};
OS   Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / FGSC
OS   10392) (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX   NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM82797.1, ECO:0000313|Proteomes:UP000008493};
RN   [1] {ECO:0000313|Proteomes:UP000008493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392
RC   {ECO:0000313|Proteomes:UP000008493};
RX   PubMed=23045686; DOI=10.1073/pnas.1206847109;
RA   Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., Nagy L.G.,
RA   Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M.,
RA   Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D.,
RA   Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V.,
RA   Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S.,
RA   Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B.,
RA   Burton K.S., Kerrigan R.W., Challen M.P., Grigoriev I.V., Martin F.;
RT   "Genome sequence of the button mushroom Agaricus bisporus reveals
RT   mechanisms governing adaptation to a humic-rich ecological niche.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012).
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   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007733}.
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DR   EMBL; JH971386; EKM82797.1; -; Genomic_DNA.
DR   RefSeq; XP_007326160.1; XM_007326098.1.
DR   AlphaFoldDB; K5XHN2; -.
DR   STRING; 597362.K5XHN2; -.
DR   GeneID; 18830036; -.
DR   KEGG; abp:AGABI1DRAFT53272; -.
DR   eggNOG; KOG1145; Eukaryota.
DR   HOGENOM; CLU_006301_5_2_1; -.
DR   InParanoid; K5XHN2; -.
DR   OMA; NRDNRTG; -.
DR   OrthoDB; 169393at2759; -.
DR   Proteomes; UP000008493; 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; 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   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; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 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   Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008493}.
FT   DOMAIN          84..259
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          378..399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  64765 MW;  3411C38184B6E389 CRC64;
     MDVYIPSTVT VGRLAKILNM KLNYLIRKMI EAGMGEEATH DHVLTSDYAV LLAEELGRNP
     IVDDEAAFDL YPPTLRPDSS CLSLRPPIVT IMGHVDHGKT TLLDTLRSSA VAKGEAGGIT
     QHIGAFSVPV NSSQGQHHIT FLDTPGHAAF SAMRERGAST TDIVVLVVAA DDGIMPQTKE
     VINLLKKDTG NVGLVVAINK IDKPDANAEA AKLALMAEGI QLESFGGDVP SVEVSGLTGK
     GLPELVETLA AMAEVQDLRA EKEGAVHGYV LESRVTKGLG PVATILVLRG SLKTGSHCLS
     GAHMAKVRLM TDSNGKSVKV ATPGMAVTVS GWKTLPKAGD EVLDGKESDV KKALANRVRM
     AGIAASLADV DAINATRKEE RERKKAEANK TDNHIDPVAE ADGPKELKLI IKADVSGSAE
     AIEGALQGIG NKEAMTKIVS AGVGDVTDSD VLMAKAVNAT IVAFSVSVPR SVQSAAAQNA
     VPITMSPIIY HLMEDVRKRV AALLPTITET TVTGEASVLQ LFDIHLKAKE VKKIAGCRVV
     NGLIEKAKFA RIVRDGSVIH DGSLDTMRVL KKDVTEVRKG SECGLSFVNF ADLREGDLIQ
     MYQTIEKPGV L
//
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