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Database: UniProt
Entry: U2SCF8_9BACL
LinkDB: U2SCF8_9BACL
Original site: U2SCF8_9BACL 
ID   U2SCF8_9BACL            Unreviewed;       166 AA.
AC   U2SCF8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Redoxin family protein {ECO:0000313|EMBL:ERK60412.1};
GN   ORFNames=HMPREF1983_00159 {ECO:0000313|EMBL:ERK60412.1};
OS   Gemella bergeri ATCC 700627.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Gemellaceae; Gemella.
OX   NCBI_TaxID=1321820 {ECO:0000313|EMBL:ERK60412.1, ECO:0000313|Proteomes:UP000016637};
RN   [1] {ECO:0000313|EMBL:ERK60412.1, ECO:0000313|Proteomes:UP000016637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700627 {ECO:0000313|EMBL:ERK60412.1,
RC   ECO:0000313|Proteomes:UP000016637};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:ERK60412.1}.
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DR   EMBL; AWVP01000009; ERK60412.1; -; Genomic_DNA.
DR   RefSeq; WP_021752238.1; NZ_KI271790.1.
DR   AlphaFoldDB; U2SCF8; -.
DR   PATRIC; fig|1321820.3.peg.157; -.
DR   eggNOG; COG2077; Bacteria.
DR   HOGENOM; CLU_042529_12_0_9; -.
DR   Proteomes; UP000016637; Unassembled WGS sequence.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR   CDD; cd03014; PRX_Atyp2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR002065; TPX.
DR   InterPro; IPR018219; Tpx_CS.
DR   PANTHER; PTHR43110; THIOL PEROXIDASE; 1.
DR   PANTHER; PTHR43110:SF1; THIOL PEROXIDASE; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   PROSITE; PS01265; TPX; 1.
PE   4: Predicted;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022559};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT   DOMAIN          18..166
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   166 AA;  18522 MW;  E9FBCD2E0CFFFAE6 CRC64;
     MKKTISFKGK PVTVEDIVKV GDVFPTFKAV TKELADFNLE DYKGKVVVIN AFPSVDTGIC
     ALQTIRFNKE VKNYNDLVVI TISKDLPFAL GRFCADKGIE NAITVSDYKY RDFENNAGGL
     IEELGLLARL VYVVDREGVV RHKELCEEVG SEPNYEAALE VVKKLL
//
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