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Database: UniProt
Entry: A0A066XL59_COLSU
LinkDB: A0A066XL59_COLSU
Original site: A0A066XL59_COLSU 
ID   A0A066XL59_COLSU        Unreviewed;       260 AA.
AC   A0A066XL59;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Putative glutaredoxin {ECO:0000313|EMBL:KDN66720.1};
GN   ORFNames=CSUB01_01805 {ECO:0000313|EMBL:KDN66720.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN66720.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN66720.1}.
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DR   EMBL; JMSE01000907; KDN66720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066XL59; -.
DR   STRING; 1173701.A0A066XL59; -.
DR   eggNOG; KOG0911; Eukaryota.
DR   HOGENOM; CLU_026126_12_0_1; -.
DR   OMA; CEPCTAV; -.
DR   OrthoDB; 1038at2759; -.
DR   Proteomes; UP000027238; 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:UP000027238}.
FT   DOMAIN          9..102
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00085"
FT   DOMAIN          164..228
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   REGION          114..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   260 AA;  27914 MW;  F7BF202A1E56E92E CRC64;
     MSTITEIASV ADFEKHITST PPSTLHIISF HAPWAAPCAQ MATVLATLAS EYPVTSPPQT
     SWLSINAEEL SEISETYNVT AVPFLVLLRN GQVLETVSGS SAIKVRNAIE AHAKKPATAT
     TTNGNQGVEN GPSAAAPAEE AVDPAKAKEE LFKRLADLVK AAPVMLFMKG TPSSPQCGFS
     RQLVALLREH SVKYGFFNIL ADDEVRQGLK EYAEWPTYPQ LWVDGELVGG LDIVKEEIAN
     NPDFLAPYSV KSNAETAATS
//
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