GenomeNet

Database: UniProt
Entry: H8X0L4_CANO9
LinkDB: H8X0L4_CANO9
Original site: H8X0L4_CANO9 
ID   H8X0L4_CANO9            Unreviewed;       266 AA.
AC   H8X0L4;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Glutaredoxin {ECO:0000313|EMBL:CCG21903.1};
GN   ORFNames=CORT_0B01850 {ECO:0000313|EMBL:CCG21903.1};
OS   Candida orthopsilosis (strain 90-125) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG21903.1, ECO:0000313|Proteomes:UP000005018};
RN   [1] {ECO:0000313|EMBL:CCG21903.1, ECO:0000313|Proteomes:UP000005018}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX   PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA   Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT   "Sequence and analysis of the genome of the pathogenic yeast Candida
RT   orthopsilosis.";
RL   PLoS ONE 7:e35750-e35750(2012).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE681720; CCG21903.1; -; Genomic_DNA.
DR   RefSeq; XP_003867341.1; XM_003867293.1.
DR   AlphaFoldDB; H8X0L4; -.
DR   GeneID; 14538636; -.
DR   KEGG; cot:CORT_0B01850; -.
DR   eggNOG; KOG1752; Eukaryota.
DR   HOGENOM; CLU_026126_0_1_1; -.
DR   OrthoDB; 1333222at2759; -.
DR   Proteomes; UP000005018; Chromosome 2.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR   CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR   PANTHER; PTHR45694:SF30; GLUTAREDOXIN 2; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..266
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003617080"
FT   DOMAIN          162..222
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   REGION          44..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   266 AA;  28929 MW;  44A4E8B5826710E1 CRC64;
     MAGVRHLRII GLTAFVLILI VVLHQTGRNA ASLVFAQASD QIPNKHRAKS NNGAQAQTPG
     GGVRVGTHGS SGSSNGKNPV VVSNNIVDSN NDEKTDDAIN QEISKDHSEE GVKKKPGEDV
     QNKENGVVEA NGGGSSDVTT NEQGEYDPQA ELIKIRSLSP MTIFSKSYCP YSKQLKKLLL
     EKYEIIPTPN IVELDVHNHG DELQQYLHEK SGRKTVPNVL VGPSFESRGG SDDFLEYHKK
     NQVIKLLTDW GQGRLQVSKK DTPSNA
//
DBGET integrated database retrieval system