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Database: UniProt
Entry: A0A1J4RLL9_9ARCH
LinkDB: A0A1J4RLL9_9ARCH
Original site: A0A1J4RLL9_9ARCH 
ID   A0A1J4RLL9_9ARCH        Unreviewed;       187 AA.
AC   A0A1J4RLL9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:OIN87944.1};
GN   ORFNames=AUJ50_02070 {ECO:0000313|EMBL:OIN87944.1};
OS   Candidatus Aenigmarchaeota archaeon CG1_02_38_14.
OC   Archaea; Candidatus Aenigmarchaeota.
OX   NCBI_TaxID=1803500 {ECO:0000313|EMBL:OIN87944.1, ECO:0000313|Proteomes:UP000182362};
RN   [1] {ECO:0000313|EMBL:OIN87944.1, ECO:0000313|Proteomes:UP000182362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_38_14 {ECO:0000313|EMBL:OIN87944.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OIN87944.1}.
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DR   EMBL; MNUF01000028; OIN87944.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4RLL9; -.
DR   Proteomes; UP000182362; Unassembled WGS sequence.
DR   GO; GO:0102039; F:NADH-dependent peroxiredoxin activity; IEA:UniProtKB-EC.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF121; ALKYL HYDROPEROXIDE REDUCTASE C; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT   DOMAIN          2..157
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        47
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   187 AA;  21100 MW;  15DAE8D8720A9093 CRC64;
     MVKINEKAPD FREDAFIDGK MKKISLSGYK GKWVVLFFYP ADFTFVCPTE LGELADKYEK
     FKELGAEIIS VSTDTAYVHK AWHDNSETIK KIKFPMLSDP ARRVAASYGT LIENEGLSLR
     ATFLINPDGV IKAYEFHDND IGRSSHELIR KLEAAKFVSE HKGQVCPINW MPGEKTLKPG
     LDLVGKI
//
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