ID A0A0D7AT09_9AGAR Unreviewed; 330 AA.
AC A0A0D7AT09;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative EFT2-translation elongation factor eEF2 {ECO:0000313|EMBL:KIY61503.1};
DE Flags: Fragment;
GN ORFNames=CYLTODRAFT_362805 {ECO:0000313|EMBL:KIY61503.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY61503.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY61503.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY61503.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
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; KN880929; KIY61503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7AT09; -.
DR STRING; 1314674.A0A0D7AT09; -.
DR OrthoDB; 166721at2759; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR CDD; cd04096; eEF2_snRNP_like_C; 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 InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR PANTHER; PTHR42908:SF10; ELONGATION FACTOR 2; 1.
DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 4: Predicted;
KW Elongation factor {ECO:0000313|EMBL:KIY61503.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW Protein biosynthesis {ECO:0000313|EMBL:KIY61503.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054007}.
FT DOMAIN 93..209
FT /note="Translation elongation factor EFG/EF2"
FT /evidence="ECO:0000259|SMART:SM00889"
FT DOMAIN 211..300
FT /note="Elongation factor EFG"
FT /evidence="ECO:0000259|SMART:SM00838"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KIY61503.1"
SQ SEQUENCE 330 AA; 36811 MW; 4CE482CC6B54802F CRC64;
KSDPCVQAWI AETGEHIVAG AGELHLEICL KDLQDDHAGV PLKISDPVVP YRETVKAESS
MVALSKSQNK HNRLYVKAMP LDDEVTKAIE DGKVNPRDDF KARARVLADE YGWDVTDARK
IWCFGPDTTG PNLLVDATKG VQYLNEIKDS CIAAFQWATK EGVLCEENMR GIRFNILDVT
LHTDAIHRGG GQLIPVCRRV CYAAALLAKP SLQEPVFQVE IQCPESAIGG IYSCLNKRRG
QVFSEEQRPG TPMFTVKAYL PVAESFGFNG ELRQHTGGQA FPQSVFDHWE LMNGDPLEKG
SKLEEIVQNI RTRKGLKREV PPLDTYYDKL
//
