ID   TR548_MIMIV             Reviewed;         137 AA.
AC   Q5UR29;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   29-SEP-2021, entry version 88.
DE   RecName: Full=Thioredoxin-like protein R548;
GN   OrderedLocusNames=MIMI_R548;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- FUNCTION: Participates in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide and
CC       catalyzes dithiol-disulfide exchange reactions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AY653733; AAV50812.1; -; Genomic_DNA.
DR   RefSeq; YP_003987063.1; NC_014649.1.
DR   SMR; Q5UR29; -.
DR   GeneID; 9925183; -.
DR   KEGG; vg:9925183; -.
DR   Proteomes; UP000001134; Genome.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..137
FT                   /note="Thioredoxin-like protein R548"
FT                   /id="PRO_0000244643"
FT   DOMAIN          2..137
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        61
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        64
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            55
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            62
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            63
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        61..64
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   137 AA;  15204 MW;  BFB8FB1A47CEE3FB CRC64;
     MSKDSVETNT IINTIDNTND NTTNITKKNS VEEIITLNDF STALGDESKG LVIIDFFTTW
     CGPCKRIAPD YIRMAEKYPT VSFYKINAEN ENLANIVAAC EIVSLPTFCF FKAGKYIGRF
     VNADPVGLEK SIVESSQ