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Database: UniProt
Entry: A0A0Q8RLU1_9SPHN
LinkDB: A0A0Q8RLU1_9SPHN
Original site: A0A0Q8RLU1_9SPHN 
ID   A0A0Q8RLU1_9SPHN        Unreviewed;       240 AA.
AC   A0A0Q8RLU1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:KRB94857.1};
GN   ORFNames=ASE22_02730 {ECO:0000313|EMBL:KRB94857.1};
OS   Sphingomonas sp. Root720.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB94857.1, ECO:0000313|Proteomes:UP000051570};
RN   [1] {ECO:0000313|Proteomes:UP000051570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB94857.1, ECO:0000313|Proteomes:UP000051570}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root720 {ECO:0000313|EMBL:KRB94857.1,
RC   ECO:0000313|Proteomes:UP000051570};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRB94857.1}.
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DR   EMBL; LMID01000001; KRB94857.1; -; Genomic_DNA.
DR   RefSeq; WP_056354606.1; NZ_LMID01000001.1.
DR   AlphaFoldDB; A0A0Q8RLU1; -.
DR   STRING; 1736595.ASE22_02730; -.
DR   Proteomes; UP000051570; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd03178; GST_C_Ure2p_like; 1.
DR   CDD; cd03048; GST_N_Ure2p_like; 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; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051:SF19; DISULFIDE-BOND OXIDOREDUCTASE YFCG; 1.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01151; Main.2:_Nu-like; 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   Reference proteome {ECO:0000313|Proteomes:UP000051570};
KW   Transferase {ECO:0000313|EMBL:KRB94857.1}.
FT   DOMAIN          1..87
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          91..219
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          204..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   240 AA;  27305 MW;  296BCEE2024C98E5 CRC64;
     MIDLHYWPTN NGIKVAILLE ELGIPYRIVP VNLGRGDQFA DDFLAISPNN RMPAIVDTEP
     KGGGAPLSVF ESGAILFYLA EKEGRFWPQD DARVRYEVVQ WVVWQAANQG PKFGERGHFA
     QVPESAGDQS YARRRFDDEV HRLYGVLNNR LHDRRHVAGD DYTIADIAAY PYTMGWRQQG
     IDLDEFRYVK RWFDEVSARP AVQRGLALTA GPPEDPAKLS PEEAERRRGI LFNQRARPAP
//
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