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Database: UniProt
Entry: V4MII0_EUTSA
LinkDB: V4MII0_EUTSA
Original site: V4MII0_EUTSA 
ID   V4MII0_EUTSA            Unreviewed;       464 AA.
AC   V4MII0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=EUTSA_v10025134mg {ECO:0000313|EMBL:ESQ55152.1};
OS   Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX   NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ55152.1, ECO:0000313|Proteomes:UP000030689};
RN   [1] {ECO:0000313|EMBL:ESQ55152.1, ECO:0000313|Proteomes:UP000030689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA   Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA   Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA   Mitchell-Olds T., Schumaker K.S., Wang X.;
RT   "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL   Front. Plant Sci. 4:46-46(2013).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; KI517384; ESQ55152.1; -; Genomic_DNA.
DR   RefSeq; XP_006413699.1; XM_006413636.1.
DR   AlphaFoldDB; V4MII0; -.
DR   STRING; 72664.V4MII0; -.
DR   EnsemblPlants; ESQ55152; ESQ55152; EUTSA_v10025134mg.
DR   GeneID; 18028625; -.
DR   Gramene; ESQ55152; ESQ55152; EUTSA_v10025134mg.
DR   KEGG; eus:EUTSA_v10025134mg; -.
DR   eggNOG; KOG0189; Eukaryota.
DR   eggNOG; KOG0191; Eukaryota.
DR   OMA; VELANNM; -.
DR   OrthoDB; 457540at2759; -.
DR   Proteomes; UP000030689; Unassembled WGS sequence.
DR   GO; GO:0009973; F:adenylyl-sulfate reductase activity; IEA:EnsemblPlants.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:InterPro.
DR   GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:InterPro.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   CDD; cd02993; PDI_a_APS_reductase; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00063; CysH; 1.
DR   InterPro; IPR004511; PAPS/APS_Rdtase.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004508; Thioredoxin-indep_APS_Rdtase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR00424; APS_reduc; 1.
DR   PANTHER; PTHR46482:SF9; 5'-ADENYLYLSULFATE REDUCTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR46482; 5'-ADENYLYLSULFATE REDUCTASE 3, CHLOROPLASTIC; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030689}.
FT   DOMAIN          343..464
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   464 AA;  51461 MW;  AE5A9360A289967F CRC64;
     MALAINVSLS SSGISSSSFP SSELKVSQIG SLRLSDRINV SAASLSFSGK RSSVKPLNVQ
     SITKESMVSQ AASMVASEVT EKLDVVEVED FEELAKRLEN ASPLEIMDKA LEKFGNDIAI
     AFSGAEDVAL IEYAHLTGRP YRVFSLDTGR LNPETYRLFD TVEKHYGIRI EYMFPDAVEV
     QALVRNKGLF SFYEDGHQEC CRIRKVRPLR RALKGLRAWI TGQRKDQSPG TRSEIPVVQI
     DPVFEGLDGG AGSLVKWNPV ANVEGNDVWN FLRTMDVPVN TLHAAGYVSI GCEPCTRAVL
     PGQHEREGRW WWEDAKAKEC GLHKGNIKEN NNGNATANVN GTSTVADIFK SENVVNLSRQ
     GIENLMKLEN RKEAWIVVLY APWCPFCQAM EASFDELADK LAGNGVKVAK FRADGDQKEF
     AKRDLQLGSF PTILVFSKNS SRPIKYPSEK RDVDSLTSFL NLVR
//
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