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Database: UniProt
Entry: A0A133VH62_9EURY
LinkDB: A0A133VH62_9EURY
Original site: A0A133VH62_9EURY 
ID   A0A133VH62_9EURY        Unreviewed;        67 AA.
AC   A0A133VH62;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Thioredoxin-like fold domain-containing protein {ECO:0000259|Pfam:PF13192};
GN   ORFNames=AKJ52_03050 {ECO:0000313|EMBL:KXB05783.1};
OS   candidate division MSBL1 archaeon SCGC-AAA382C18.
OC   Archaea; Euryarchaeota; candidate division MSBL1.
OX   NCBI_TaxID=1698281 {ECO:0000313|EMBL:KXB05783.1, ECO:0000313|Proteomes:UP000070404};
RN   [1] {ECO:0000313|EMBL:KXB05783.1, ECO:0000313|Proteomes:UP000070404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC-AAA382C18 {ECO:0000313|EMBL:KXB05783.1};
RX   PubMed=26758088; DOI=10.1038/srep19181;
RA   Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA   Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT   "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT   pools of the Red Sea.";
RL   Sci. Rep. 6:19181-19181(2016).
CC   -!- SIMILARITY: Belongs to the glutaredoxin family.
CC       {ECO:0000256|ARBA:ARBA00007787}.
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:KXB05783.1}.
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DR   EMBL; LHYF01000074; KXB05783.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133VH62; -.
DR   Proteomes; UP000070404; Unassembled WGS sequence.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR005243; THIRX-like_proc.
DR   NCBIfam; TIGR00412; redox_disulf_2; 1.
DR   PANTHER; PTHR36450; THIOREDOXIN; 1.
DR   PANTHER; PTHR36450:SF1; THIOREDOXIN; 1.
DR   Pfam; PF13192; Thioredoxin_3; 1.
DR   PIRSF; PIRSF037031; Redox_disulphide_2; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR037031-51};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Redox-active center {ECO:0000256|PIRSR:PIRSR037031-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070404};
KW   Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   DOMAIN          1..66
FT                   /note="Thioredoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF13192"
FT   ACT_SITE        10
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT   ACT_SITE        13
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037031-50"
FT   DISULFID        10..13
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037031-51"
SQ   SEQUENCE   67 AA;  7182 MW;  8D29FC1F4892162E CRC64;
     MKIEILGPGC PNCEKLEEET KKAIEDLELK DIEVTKVDDP AEIAGKGVMN TPALAIDGEV
     KFSGRGP
//
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