ID K1XUD6_MARBU Unreviewed; 283 AA.
AC K1XUD6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Monothiol glutaredoxin-4 {ECO:0000313|EMBL:EKD16294.1};
GN ORFNames=MBM_05588 {ECO:0000313|EMBL:EKD16294.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16294.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD16294.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16294.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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DR EMBL; JH921439; EKD16294.1; -; Genomic_DNA.
DR RefSeq; XP_007293477.1; XM_007293415.1.
DR AlphaFoldDB; K1XUD6; -.
DR STRING; 1072389.K1XUD6; -.
DR GeneID; 18761523; -.
DR KEGG; mbe:MBM_05588; -.
DR eggNOG; KOG0911; Eukaryota.
DR HOGENOM; CLU_026126_12_0_1; -.
DR InParanoid; K1XUD6; -.
DR OMA; NGPRCGF; -.
DR OrthoDB; 1038at2759; -.
DR Proteomes; UP000006753; 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:UP000006753}.
FT DOMAIN 9..106
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|Pfam:PF00085"
FT DOMAIN 180..244
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT REGION 111..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 283 AA; 30473 MW; C61F9DDFC7E40F91 CRC64;
MSTLLELKTE EEWNQYAASV PSNTLQVLYF KAEWAAPCKQ MTTVLQTLAS SYPVTEPLST
SWVSLDAEDV PDVSDSFDVT AVPFLVLQRN GQVLETVSGS DAMKVRAAIE KHSNSTTVPT
TANGAAHTPS NNGTSAKNVS SSAPTTQDSA TAPEIPSAEI KEDKEALHNR LSSLVKAAPV
MLFMKGTPSA PQCGFSRQLV ALLRENSVKY GFFNILADDE VRQGLKEFAD WPTFPQLWVD
GELVGGLDIV KEEMGNDPDF LKPYSVVKST PAAPSQETAT ATA
//