ID A0A0J8S3P8_COCIT Unreviewed; 269 AA.
AC A0A0J8S3P8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Monothiol glutaredoxin-4 {ECO:0000313|EMBL:KMU92085.1};
GN ORFNames=CIHG_09923 {ECO:0000313|EMBL:KMU92085.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU92085.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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DR EMBL; DS017053; KMU92085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8S3P8; -.
DR STRING; 396776.A0A0J8S3P8; -.
DR VEuPathDB; FungiDB:CIHG_09923; -.
DR eggNOG; KOG0911; Eukaryota.
DR Proteomes; UP000054563; 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 NCBIfam; TIGR00365; Grx4 family monothiol glutaredoxin; 1.
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.
DR PROSITE; PS51352; THIOREDOXIN_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:UP000054563}.
FT DOMAIN 1..114
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 133..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 269 AA; 29206 MW; AD1A6B7AA46474A2 CRC64;
MSTLHEITSE ADFTTQLSSL PSTSLAVLSF HTPWAAPCTQ MRNVLSTLAS TYPATTPPSI
HFLSINAEDL PDISEQYDVS AVPYLVLLRD NKIVETVSGS DPVRVREAIE KHVGQDGQTD
RPSIPPPLVA VPRATAAQDT SDDATASDAQ LEPPVPTKEE LFARLSELVK AAPVMLFMKG
TPSAPQCGFS RQIVSILREN GVKYGFFNIL ADEDVRQGLK EFADWPTFPQ LWVKGELVGG
LDIVKEEISA NPDFFCDYSV SKPTSAPSA
//
