ID S7ZLA3_PENO1 Unreviewed; 280 AA.
AC S7ZLA3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 03-MAY-2023, entry version 35.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EPS31400.1};
GN ORFNames=PDE_06355 {ECO:0000313|EMBL:EPS31400.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS31400.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS31400.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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DR EMBL; KB644413; EPS31400.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZLA3; -.
DR STRING; 933388.S7ZLA3; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_0_1; -.
DR OrthoDB; 1038at2759; -.
DR PhylomeDB; S7ZLA3; -.
DR Proteomes; UP000019376; Unassembled WGS sequence.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03028; GRX_PICOT_like; 1.
DR CDD; cd02984; TRX_PICOT; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR033658; GRX_PICOT-like.
DR InterPro; IPR004480; Monothiol_GRX-rel.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR PANTHER; PTHR10293:SF73; GLUTAREDOXIN-3; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000019376}.
FT DOMAIN 7..102
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF00085"
FT DOMAIN 190..254
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT REGION 129..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 280 AA; 29922 MW; DD0EBE4A637F6E72 CRC64;
MSALTEITSE AEFTSHLASL SPSALLVLYF HTPWAAPCTQ MRAVLEAIAG QYPAASPPVI
SFVSINAEEL PDISEELDVT AVPFVVLMRG GQRLEDISGS DAVKVRNAIE RHAGGSVPVD
GAKASLPAPL AATPRENGPE IATQPPAASA RAPEPAANAI DVSAAPALTP EQSKEALWAR
LDQLVKAAPV MLFMKGTPSS PQCGFSRQLV GILRERSVKY GFFNILADED VRQGLKEYAD
WPTFPQLWVG GELVGGLDIV RDEIENDPGF FDQYSVNKQA
//
