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Database: UniProt
Entry: A0A165DSM1_9BASI
LinkDB: A0A165DSM1_9BASI
Original site: A0A165DSM1_9BASI 
ID   A0A165DSM1_9BASI        Unreviewed;       220 AA.
AC   A0A165DSM1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 22.
DE   SubName: Full=Putative translation elongation factor eEF-1B gamma subunit {ECO:0000313|EMBL:KZT53460.1};
GN   ORFNames=CALCODRAFT_440066 {ECO:0000313|EMBL:KZT53460.1};
OS   Calocera cornea HHB12733.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Calocera.
OX   NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT53460.1, ECO:0000313|Proteomes:UP000076842};
RN   [1] {ECO:0000313|EMBL:KZT53460.1, ECO:0000313|Proteomes:UP000076842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12733 {ECO:0000313|EMBL:KZT53460.1,
RC   ECO:0000313|Proteomes:UP000076842};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; KV424037; KZT53460.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165DSM1; -.
DR   STRING; 1353952.A0A165DSM1; -.
DR   InParanoid; A0A165DSM1; -.
DR   OrthoDB; 159792at2759; -.
DR   Proteomes; UP000076842; Unassembled WGS sequence.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR   CDD; cd03044; GST_N_EF1Bgamma; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1.
DR   PANTHER; PTHR43986:SF1; ELONGATION FACTOR 1-GAMMA; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   3: Inferred from homology;
KW   Elongation factor {ECO:0000313|EMBL:KZT53460.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:KZT53460.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076842}.
FT   DOMAIN          2..83
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          88..215
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
SQ   SEQUENCE   220 AA;  24058 MW;  37A4DE898C79305F CRC64;
     MSVGTLYTFS GLPFGKRVRA VAAAAGLKVD EPLTQAGKSN KTAIFVAKFP NAKFPAFEAP
     DGFKLFESSA IARYLASLAP DAKLLGTTAQ ETALVDQWIS FADNEVRVPM INALMILRGT
     AGAYSQEIEH HWRQRVIPHL EILDAHLKDN TFLVGNNLTI ADLTLATIVQ QAFTTLVDRS
     ARAKLPSLVE WYDSIVNLPT VKDVYGETAY IDVALQYQSA
//
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