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Database: UniProt
Entry: A0A0A2EMR1_PORCN
LinkDB: A0A0A2EMR1_PORCN
Original site: A0A0A2EMR1_PORCN 
ID   A0A0A2EMR1_PORCN        Unreviewed;       366 AA.
AC   A0A0A2EMR1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=HQ35_08750 {ECO:0000313|EMBL:KGN78947.1};
OS   Porphyromonas cangingivalis.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=36874 {ECO:0000313|EMBL:KGN78947.1, ECO:0000313|Proteomes:UP000030125};
RN   [1] {ECO:0000313|EMBL:KGN78947.1, ECO:0000313|Proteomes:UP000030125}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-109 OH1386 {ECO:0000313|Proteomes:UP000030125};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA   Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT   "Porphyromonas cangingivalis strain:COT-109_OH1386 Genome sequencing.";
RL   Submitted (AUG-2014) 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:KGN78947.1}.
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DR   EMBL; JQJD01000056; KGN78947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2EMR1; -.
DR   STRING; 36874.HQ34_03285; -.
DR   eggNOG; COG0526; Bacteria.
DR   OrthoDB; 9794348at2; -.
DR   Proteomes; UP000030125; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR025380; DUF4369.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF14289; DUF4369; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Cytochrome c-type biogenesis {ECO:0000256|ARBA:ARBA00022748};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030125};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..366
FT                   /note="Thioredoxin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001986275"
FT   DOMAIN          227..365
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   366 AA;  41080 MW;  7235F202B04F7617 CRC64;
     MNRLLMTILS LLTASTYCYA QHTVEIKGKI DGVKSGQLVL LRHRSENKID TLGTTPFSTP
     DFALSASLSE PSVVRLVVAG YAGGFEFIAE PGAQYLALLK DGDGAYIKGG DLQDKWLHFQ
     SWMKASQDSI DIVKKRYDAL LAQNKYRSAS RTNDTLIYLQ KRQLEEQENF LKGNDNIISA
     YMAQSTAVAK GLSLEDSERL YVTLGPSARS SISGRIMKER IDRLKKTSTG QKAPDFTMSA
     PDGKQYTISK VPGKIKIVDF WASWCGPCRL NNRTLKELYA TYHTQGLEII GVSMDDNRDK
     WIDAIEKDQL PWINISDLKA WKSEVSKLYD ITGIPALFIL DENNNIIGRN IKGEALKTFI
     NKQFNR
//
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