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Database: UniProt
Entry: A0A143YTS0_9LACT
LinkDB: A0A143YTS0_9LACT
Original site: A0A143YTS0_9LACT 
ID   A0A143YTS0_9LACT        Unreviewed;       835 AA.
AC   A0A143YTS0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Pyridine nucleotide disulphide reductase class-i signature {ECO:0000313|EMBL:CZQ95645.1};
GN   ORFNames=TR210_1323 {ECO:0000313|EMBL:CZQ95645.1};
OS   Trichococcus ilyis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Trichococcus.
OX   NCBI_TaxID=640938 {ECO:0000313|EMBL:CZQ95645.1, ECO:0000313|Proteomes:UP000076878};
RN   [1] {ECO:0000313|EMBL:CZQ95645.1, ECO:0000313|Proteomes:UP000076878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Trichococcus_R210 {ECO:0000313|EMBL:CZQ95645.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the sulfur carrier protein TusA family.
CC       {ECO:0000256|ARBA:ARBA00008984}.
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DR   EMBL; FJNB01000008; CZQ95645.1; -; Genomic_DNA.
DR   RefSeq; WP_068622737.1; NZ_FNYT01000007.1.
DR   AlphaFoldDB; A0A143YTS0; -.
DR   STRING; 640938.TR210_1323; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000076878; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd01524; RHOD_Pyr_redox; 1.
DR   Gene3D; 3.40.1260.10; DsrEFH-like; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   Gene3D; 3.30.110.40; TusA-like domain; 1.
DR   InterPro; IPR032836; DsrE2-like.
DR   InterPro; IPR027396; DsrEFH-like.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR001455; TusA-like.
DR   InterPro; IPR036868; TusA-like_sf.
DR   PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 1.
DR   Pfam; PF13686; DrsE_2; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF01206; TusA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF75169; DsrEFH-like; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   SUPFAM; SSF64307; SirA-like; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS01148; UPF0033; 1.
PE   3: Inferred from homology;
FT   DOMAIN          464..551
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   835 AA;  89836 MW;  8DB043CDDDD6D3FE CRC64;
     MKRKIVIIGG VAGGATAAAR LRRLNEEDEI VIFEKGEYIS FANCGLPYHI GGTIQERDNL
     LLETVGGMAK KFNIGIKNFS EVVKINRAEK TITVKHVLTG ATTEESYDKL IISTGARPIK
     PAIAGIEEAE NVFTLRNIPD MDKIKAYINE HQVKRATVIG GGFIGLEMME NLWELGIQVS
     LVEMSDQVMA PIDFEMAQSV HAHIDMHNVN LILNDGVKAF EDKGSKVRLN SGKVLNTDMT
     ILSIGVTPEN ELATAAGLKT GVRGAIVVND QLQTSDPDIF AVGDVIEVTD FVNGKPTVVP
     LAWPANRQGR LVADHLNGMD VRYKGTMGTS VAKVFELTVA AAGNNEKTLN GSGTDYKVVH
     IHPNSHAGYY PGASPLDIKL LFGLDGKILG VQAVGMEGVE KRVDVIATAM KLGATVYDLP
     DLELAYAPPY SSAKDPANIA GYVASNILEG KIDTFQWHEV DGLIAKGAFL LDVREEFELA
     TGALGNAYTI PLAQIRERMS ELPKDKTIHV FCQVGHRGYN AARILMQNGF SVKNLDGGYK
     TYKQAKTTLT YEEDVPEAAV HVEPVHAKPA AQPASNTIQV DACGLQCPGP ILKVKENIDK
     MVDGQELIIE ASDFGFLADI AAWTKNTGNT LLSKEIDGKI VRAHVAKGKA GAVKSATPAG
     FNEAALAAQA AQAPILQETK DGATMVVFSG DLDKALASFI IANGAAAYGK QVTMFFTFWG
     LNVIKRPEKV SVAKRGMERM FDIMLPSHAG KLPISKMNMS GVGSKMIQAV MKQKNVDSLP
     AMIAQAQKMG VKMVACTMSM DIMGIKEEEI IEGVDFGGVA AYIGDTMDAN LNLFI
//
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