ID A0A1V6R0P0_9EURO Unreviewed; 668 AA.
AC A0A1V6R0P0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=GST N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENSOL_c023G04378 {ECO:0000313|EMBL:OQD94941.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD94941.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD94941.1}.
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DR EMBL; MDYO01000023; OQD94941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6R0P0; -.
DR STRING; 60172.A0A1V6R0P0; -.
DR OrthoDB; 767442at2759; -.
DR Proteomes; UP000191612; Unassembled WGS sequence.
DR CDD; cd00299; GST_C_family; 1.
DR CDD; cd00570; GST_N_family; 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; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43968; -; 1.
DR PANTHER; PTHR43968:SF6; GLUTATHIONE S-TRANSFERASE OMEGA; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF13417; GST_N_3; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000191612}.
FT DOMAIN 437..515
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 520..656
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 74765 MW; 38AC056D2352793C CRC64;
MDSELRMSSP RLGPSMPIND QSNLQLGQFD PESQPFGSFR PPTEAESQLQ NATHAFIRPP
RSGEPANNFI TASPSTQHQS HQGHPGNGVA SHLQPQGQSS NGLHQSQDYN NGVAHAANMS
GALHGAGTGQ MGPPASLSPN ELAMGNNAHQ AQNNNLTTLQ SSSQPFQSDF IELDSGSVDP
VSFTGPGELQ GFKVVPNPPH LDYWRDRLFN VDEMITLSEE EFQTYFPHVD NVYSHRSTQR
YKRKPFVSHY WDCRLKGRPP GTPKSDDPEK KKRKRTARER DLCHVKIKVV EYFPVSEISN
TTHAVEPLPT NILPGMYTFS LNDDPAIRNA QTFGMLTPNP GLPPNHPGSN GGRYFTIQRV
NGNGANGKND GVSGGHQHTL EESDRVKKSS VQRYVLKEKK DKRTRTDRVM SRTGQKSYHT
KATGLAAETA IKHSADVNLK LFGSCFCPFV QRVWIALELK GIPYQYIEVD PYEKPQSLLE
VNPRGLVPAL RHDDWGCYES NVLLEYLEDL GVGAAMLPGD PKLRAHCRLW ADHVNRHIVP
SFYRILQEQD QQKQIEKTQE LRDAMEKLLE VAHPKGPFFM GPQMSLVDVQ AAPWIIRLRR
VLKPYRGWPD AEEGSRLAIW MDAIETNQHV QATTSTDELY HDSYERYAQN RPNTSQVANA
INAGRGLP
//