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Database: UniProt
Entry: A0A1L7WFW2_9HELO
LinkDB: A0A1L7WFW2_9HELO
Original site: A0A1L7WFW2_9HELO 
ID   A0A1L7WFW2_9HELO        Unreviewed;       166 AA.
AC   A0A1L7WFW2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Probable peroxisomal membrane protein {ECO:0000313|EMBL:CZR51648.1};
GN   ORFNames=PAC_01525 {ECO:0000313|EMBL:CZR51648.1};
OS   Phialocephala subalpina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Mollisiaceae; Phialocephala;
OC   Phialocephala fortinii species complex.
OX   NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR51648.1, ECO:0000313|Proteomes:UP000184330};
RN   [1] {ECO:0000313|EMBL:CZR51648.1, ECO:0000313|Proteomes:UP000184330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR51648.1,
RC   ECO:0000313|Proteomes:UP000184330};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides. {ECO:0000256|RuleBase:RU366011}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010505, ECO:0000256|RuleBase:RU366011}.
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DR   EMBL; FJOG01000002; CZR51648.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7WFW2; -.
DR   STRING; 576137.A0A1L7WFW2; -.
DR   OrthoDB; 593245at2759; -.
DR   Proteomes; UP000184330; Unassembled WGS sequence.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   CDD; cd03013; PRX5_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR037944; PRX5-like.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR   PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Antioxidant {ECO:0000256|RuleBase:RU366011};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU366011};
KW   Peroxidase {ECO:0000256|RuleBase:RU366011};
KW   Redox-active center {ECO:0000256|RuleBase:RU366011};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184330}.
FT   DOMAIN          4..166
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        61
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ   SEQUENCE   166 AA;  17872 MW;  35C8696BD86F8532 CRC64;
     MADLKVGDSF PSGVTFSYVP YTPENGDITS CGIPINYDAS KEWVNKKVVL FSVPGAFTPG
     CSAKHLPGYI ENISALKGKG VDVVAVIAFN DAWVMSAWGK ANNIKNDDIL FLSDVGTEFS
     KKLGWTMGER TARYALIIDN GKITYAEKEP GREVSVSSAE AVLAKL
//
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