ID C7P162_HALMD Unreviewed; 234 AA.
AC C7P162;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=DsbA-like thioredoxin domain-containing protein {ECO:0000313|EMBL:ACV49077.1};
GN OrderedLocusNames=Hmuk_2972 {ECO:0000313|EMBL:ACV49077.1};
OS Halomicrobium mukohataei (strain ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB
OS 13541) (Haloarcula mukohataei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=485914 {ECO:0000313|EMBL:ACV49077.1, ECO:0000313|Proteomes:UP000001746};
RN [1] {ECO:0000313|EMBL:ACV49077.1, ECO:0000313|Proteomes:UP000001746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700874 / DSM 12286 / JCM 9738 / NCIMB 13541
RC {ECO:0000313|Proteomes:UP000001746};
RX PubMed=21304667; DOI=10.4056/sigs.42644;
RA Tindall B.J., Schneider S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Pitluck S., Mikhailova N., Pati A., Ivanova N., Mavrommatis K.,
RA Chen A., Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Han C., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.,
RA Detter J.C.;
RT "Complete genome sequence of Halomicrobium mukohataei type strain (arg-
RT 2).";
RL Stand. Genomic Sci. 1:270-277(2009).
CC -!- SIMILARITY: Belongs to the glutaredoxin family.
CC {ECO:0000256|ARBA:ARBA00007787}.
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DR EMBL; CP001688; ACV49077.1; -; Genomic_DNA.
DR RefSeq; WP_015763919.1; NC_013202.1.
DR AlphaFoldDB; C7P162; -.
DR STRING; 485914.Hmuk_2972; -.
DR GeneID; 8412525; -.
DR KEGG; hmu:Hmuk_2972; -.
DR eggNOG; arCOG02868; Archaea.
DR HOGENOM; CLU_000288_47_1_2; -.
DR OrthoDB; 15256at2157; -.
DR Proteomes; UP000001746; Chromosome.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR13887:SF14; CLPXP ADAPTER PROTEIN SPXH; 1.
DR PANTHER; PTHR13887; GLUTATHIONE S-TRANSFERASE KAPPA; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Reference proteome {ECO:0000313|Proteomes:UP000001746};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 42..190
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 25..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 234 AA; 24954 MW; C6853F198A93C6E1 CRC64;
MDDLTRRRLL GGTAGLVAGT AGCVGGDANT DADATPTDRE LMTSGSSDVD FDHPSATGIN
DQPTLGDRGR QGVIVAFEDP SCPTCRRFHR NTFPQIESEL LAPGDVAYVF RGYPVVYEWG
GPATRALEAT FARDPAAVWD LKAHYFDQQG QFSTDNVLDR TRSYLDDATN VDGSAVVTAV
SEDAAAQAVQ TDYDAGQAAG ASGTPTFYLF RDGEYQTTVS GAQDFTVFEN VLLG
//
