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Database: UniProt/TrEMBL
Entry: A5E437_LODEL
LinkDB: A5E437_LODEL
Original site: A5E437_LODEL 
ID   A5E437_LODEL            Unreviewed;       222 AA.
AC   A5E437;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   30-AUG-2017, entry version 64.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDK46195.1};
GN   ORFNames=LELG_04376 {ECO:0000313|EMBL:EDK46195.1};
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 /
OS   NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Lodderomyces.
OX   NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK46195.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK46195.1, ECO:0000313|Proteomes:UP000001996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239
RC   {ECO:0000313|Proteomes:UP000001996};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
RA   Agrafioti I., Arnaud M.B., Bates S., Brown A.J., Brunke S.,
RA   Costanzo M.C., Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L.,
RA   Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R.,
RA   Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C.,
RA   Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.,
RA   Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.,
RA   Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M.,
RA   Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000213|PDB:4IVF}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RG   Enzyme Function Initiative (EFI);
RA   Vetting M.W., Toro R., Bhosle R., Al Obaidi N.F., Morisco L.L.,
RA   Wasserman S.R., Sojitra S., Washington E., Scott Glenn A.,
RA   Chowdhury S., Evans B., Hammonds J., Hillerich B., Love J.,
RA   Seidel R.D., Imker H.J., Armstrong R.N., Gerlt J.A., Almo S.C.;
RT   "Crystal structure of glutathione transferase homolog from
RT   Lodderomyces elongisporus, target EFI-501753, with two GSH per
RT   subunit.";
RL   Submitted (JAN-2013) to the PDB data bank.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
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DR   EMBL; CH981529; EDK46195.1; -; Genomic_DNA.
DR   RefSeq; XP_001524404.1; XM_001524354.1.
DR   PDB; 4IVF; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-222.
DR   PDBsum; 4IVF; -.
DR   ProteinModelPortal; A5E437; -.
DR   SMR; A5E437; -.
DR   STRING; 379508.XP_001524404.1; -.
DR   EnsemblFungi; EDK46195; EDK46195; LELG_04376.
DR   GeneID; 5231402; -.
DR   KEGG; lel:LELG_04376; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   eggNOG; COG0625; LUCA.
DR   InParanoid; A5E437; -.
DR   KO; K00799; -.
DR   OMA; DIAVWPW; -.
DR   OrthoDB; EOG092C499E; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:4IVF};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001996};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT   DOMAIN        3     91       GST N-terminal. {ECO:0000259|PROSITE:
FT                                PS50404}.
FT   DOMAIN       98    222       GST C-terminal. {ECO:0000259|PROSITE:
FT                                PS50405}.
FT   REGION       13     15       Glutathione 1 binding. {ECO:0000213|PDB:
FT                                4IVF}.
FT   REGION       55     56       Glutathione 1 binding. {ECO:0000213|PDB:
FT                                4IVF}.
FT   REGION       75     76       Glutathione 1 binding. {ECO:0000213|PDB:
FT                                4IVF}.
FT   REGION      115    118       Glutathione 2 binding. {ECO:0000213|PDB:
FT                                4IVF}.
FT   BINDING      15     15       Glutathione 2. {ECO:0000213|PDB:4IVF}.
FT   BINDING      55     55       Glutathione 2. {ECO:0000213|PDB:4IVF}.
FT   BINDING     115    115       Glutathione 1. {ECO:0000213|PDB:4IVF}.
FT   BINDING     115    115       Glutathione 3. {ECO:0000213|PDB:4IVF}.
FT   BINDING     140    140       Glutathione 1. {ECO:0000213|PDB:4IVF}.
FT   BINDING     140    140       Glutathione 2. {ECO:0000213|PDB:4IVF}.
FT   BINDING     140    140       Glutathione 4. {ECO:0000213|PDB:4IVF}.
SQ   SEQUENCE   222 AA;  25363 MW;  CD739EBD9A298767 CRC64;
     MALKPIKLYT APTPNGYKIS IFLEVLGLDY EVQKFDLSKN ETKEDWFVKL NPNGRIPTIN
     DPNFKGVDGG LVLSQTGAIL QYLADTYDKE HKFSYPAGTA EYYKTLEYLI FQVAENGPIQ
     GQANHFVFAA KEKVPYGINR YITDTKRIYG VFEDILSRNK ANDSKYLVGD RYTVADFALL
     GWAYRLSRLE IDINQWPLLG KWYDSLLKLP AVQKGFEVPP KN
//
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