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Database: UniProt
Entry: A0A1W5D1L4_9LECA
LinkDB: A0A1W5D1L4_9LECA
Original site: A0A1W5D1L4_9LECA 
ID   A0A1W5D1L4_9LECA        Unreviewed;       187 AA.
AC   A0A1W5D1L4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=TSA family {ECO:0000313|EMBL:KAA6411498.1, ECO:0000313|EMBL:SLM37018.1};
GN   ORFNames=FRX48_04778 {ECO:0000313|EMBL:KAA6411498.1};
OS   Lasallia pustulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC   Lasallia.
OX   NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM37018.1, ECO:0000313|Proteomes:UP000192927};
RN   [1] {ECO:0000313|EMBL:SLM37018.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000192927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sharma R., Thines M.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KAA6411498.1, ECO:0000313|Proteomes:UP000324767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1-1 {ECO:0000313|EMBL:KAA6411498.1};
RA   Greshake Tzovaras B., Segers F., Bicker A., Dal Grande F., Otte J.,
RA   Hankeln T., Schmitt I., Ebersberger I.;
RT   "The hologenome of the rock-dwelling lichen Lasallia pustulata.";
RL   Submitted (SEP-2019) 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; VXIT01000007; KAA6411498.1; -; Genomic_DNA.
DR   EMBL; FWEW01001418; SLM37018.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W5D1L4; -.
DR   OrthoDB; 593245at2759; -.
DR   Proteomes; UP000192927; Unassembled WGS sequence.
DR   Proteomes; UP000324767; 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   PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR   PANTHER; PTHR10430:SF39; PEROXIREDOXIN AHP1; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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}.
FT   DOMAIN          35..186
FT                   /note="Redoxin"
FT                   /evidence="ECO:0000259|Pfam:PF08534"
FT   ACT_SITE        78
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ   SEQUENCE   187 AA;  19624 MW;  206D5D2909F8BBC9 CRC64;
     MFPARSLFRA TPRAAAAVRP RPYSPFHTSA PFAVKAGDAI PDLDCLVENS PGNKVNLAKE
     LTGRGLIIGV PAAFSPSCSE SHIPGYLNSK ALKGAGQVFV VSVNDPFVMK AWGSTLDPSG
     TSGVRFLGDP SAKFTTALDL HFDGAAIFGG DRSKRYALVV EDGKVKEAHV EPDNTGLNVS
     AADKVLL
//
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