ID M2QSJ0_CERS8 Unreviewed; 1074 AA.
AC M2QSJ0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 08-NOV-2023, entry version 41.
DE RecName: Full=Tr-type G domain-containing protein {ECO:0000259|PROSITE:PS51722};
GN ORFNames=CERSUDRAFT_63510 {ECO:0000313|EMBL:EMD39993.1};
OS Ceriporiopsis subvermispora (strain B) (White-rot fungus) (Gelatoporia
OS subvermispora).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Gelatoporiaceae; Gelatoporia.
OX NCBI_TaxID=914234 {ECO:0000313|EMBL:EMD39993.1, ECO:0000313|Proteomes:UP000016930};
RN [1] {ECO:0000313|EMBL:EMD39993.1, ECO:0000313|Proteomes:UP000016930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B {ECO:0000313|EMBL:EMD39993.1,
RC ECO:0000313|Proteomes:UP000016930};
RX PubMed=22434909; DOI=10.1073/pnas.1119912109;
RA Fernandez-Fueyo E., Ruiz-Duenas F.J., Ferreira P., Floudas D.,
RA Hibbett D.S., Canessa P., Larrondo L.F., James T.Y., Seelenfreund D.,
RA Lobos S., Polanco R., Tello M., Honda Y., Watanabe T., Watanabe T.,
RA Ryu J.S., Kubicek C.P., Schmoll M., Gaskell J., Hammel K.E., St John F.J.,
RA Vanden Wymelenberg A., Sabat G., Splinter BonDurant S., Syed K.,
RA Yadav J.S., Doddapaneni H., Subramanian V., Lavin J.L., Oguiza J.A.,
RA Perez G., Pisabarro A.G., Ramirez L., Santoyo F., Master E., Coutinho P.M.,
RA Henrissat B., Lombard V., Magnuson J.K., Kuees U., Hori C., Igarashi K.,
RA Samejima M., Held B.W., Barry K.W., LaButti K.M., Lapidus A.,
RA Lindquist E.A., Lucas S.M., Riley R., Salamov A.A., Hoffmeister D.,
RA Schwenk D., Hadar Y., Yarden O., de Vries R.P., Wiebenga A., Stenlid J.,
RA Eastwood D., Grigoriev I.V., Berka R.M., Blanchette R.A., Kersten P.,
RA Martinez A.T., Vicuna R., Cullen D.;
RT "Comparative genomics of Ceriporiopsis subvermispora and Phanerochaete
RT chrysosporium provide insight into selective ligninolysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5458-5463(2012).
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DR EMBL; KB445793; EMD39993.1; -; Genomic_DNA.
DR AlphaFoldDB; M2QSJ0; -.
DR STRING; 914234.M2QSJ0; -.
DR HOGENOM; CLU_002794_3_1_1; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000016930; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 1.
DR CDD; cd01885; EF2; 1.
DR CDD; cd16268; EF2_II; 1.
DR CDD; cd16261; EF2_snRNP_III; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.240; -; 1.
DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 3.90.1430.10; Yeast translation eEF2 (G' domain); 1.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR42908:SF3; ELONGATION FACTOR-LIKE GTPASE 1; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000016930}.
FT DOMAIN 8..269
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 1074 AA; 120469 MW; 3DB1431446507564 CRC64;
MAATAEAIHV RNVTTIGHVD HGKTTMMDAL LAANNIISSR MAGKIRYLDS REDEQERGIT
MESSAVSLRF KVMERDTDGG SSPKTYVVNM IDTPGHVDFS SEVSIASRLC DGALVLVDVV
EGVCTQTITV LRQAWQDRLR PVLVINKFDR LITELKLSPL EAYHHLSQLI EQVNAVMGSF
FASERMEDDL RWREERERRL AEKKEAHATE VDAIVNEDDE FQEKDDEDIY FAPERGNVVF
ASAIDGWGFR IGKFAHLYAV KLGMKEANLR TVLWGDFYLD PKTKKVISYK HLKGRALKPL
FVHFVLDNIW AIYDAVVLNP NPDKVQKIVT TLNLKIPPRE LKTKDYRHLL SLVFSQWLPL
STCVIQTVVD IVPPPSDAQR TRIPKMLYPD LYEPIIEPKN KLEENLYACD ANPNASVVAL
VSKMFAVPAK DLPSNKKKPL TADEMRSRVK AAREARERAQ AENTASEPVI TTPLETALEK
LEIKDESPEP NSEEQDEVGE TLLGFARIYS GVIRVGTKIC CVLPKYNTSL GPKHPRNAQH
VVTTQVEALY TMMGRELVAV DSVQAGNVFA IQGLEGKVWR NATLCAPNMN GVGDINDLSE
VNDWLVNLGG AYRNAAPILR IALEPEIPAE LPKLIRGLKL LSQSDPCVQT YQQPTGEYVI
LTAGELHYER CHKDLTERFA KIQINASKPI VPFRETAVKA ADMSLPKTPG ARRGTMHGSV
TNNAVKFTIR ATPLPDVIKE FLRDNLALLR RMELEQKTDK LGSGDEEAAD LEEEFDKLGE
LLKKPTVKPE EFWTTLAAKF KETGGEWTDV VNQIWAFGPQ RAGTCILVDS RADGALNSLR
QRLERNKSGE TSREADTLSR DFDNHLEAGF QLATFQGPLC AEPVDGLAYF VESLEIDRAL
IEQERDLNRM PQVIGAFISA VKDACRNGLL DWSPRLMLAM YSCDIQASTD VLGKVYGVVA
RRRGKIVAEE MKEGTELFTV SAVIPVVESF GFAMEMRRRT SGAASPQLIF NGYEMLDQDP
FWVPTTEEEL EDLGEKADRI NIAKSYMDAV RERKGMFVDR KLVEFAEKQR TLKR
//