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}.
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; 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
//