ID A0A1F5CUW6_9ARCH Unreviewed; 557 AA.
AC A0A1F5CUW6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN ORFNames=A3K70_03870 {ECO:0000313|EMBL:OGD46650.1};
OS Candidatus Bathyarchaeota archaeon RBG_16_48_13.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1797381 {ECO:0000313|EMBL:OGD46650.1, ECO:0000313|Proteomes:UP000176610};
RN [1] {ECO:0000313|EMBL:OGD46650.1, ECO:0000313|Proteomes:UP000176610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:OGD46650.1}.
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DR EMBL; MEZH01000004; OGD46650.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5CUW6; -.
DR STRING; 1797381.A3K70_03870; -.
DR Proteomes; UP000176610; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
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 PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 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 PROSITE; PS50206; RHODANESE_3; 1.
PE 3: Inferred from homology;
FT DOMAIN 469..555
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 557 AA; 61445 MW; F3B5894C166D5D2A CRC64;
MESEFVIIGG NASGMKAAAR ARRCNPNLQI TVFEKGDYVS FAGCGLPYYI SGLIEDSDEL
IVRSPDWFKE FLDLDVKVNH RVEGINRKAR KLVVRDLSTD CILHVTYRKL LIATGANPIK
LPIEGASSRG VFTIKSMEDG SNLRDFISER KPRKAVIVGA GLIGLEMAES LLISGLDVSI
VEKLEQILPI LDDDMAFLVE KYLKNKSIKF FLGESVRAFD EDAKGSISYV ETDKRKIAAG
LAIISIGVKP EVTLAREAGL EIGETGAIRV NSKMYTCDPN ILAAGDCVET VDFVTGRPIW
APLGSTANKQ GRVAGENAAG GEVEFGGVAP VQIARLFDLS VAKAGLSEIE ARKLDFDIEV
TFTNSWDHPQ YYPGARIITM KTMVNRPDHR LLGCQIVGER GVDKRIDVMA TALYKKMTCD
DLSKLDLAYA PPYSPALDSI ITAGNVALNK LKGAYVSING KDLLQRMMRG EDLQLVDVLQ
PKLYKECHIP KSTNIPLNEL WKRSNELDRE KEVITICKYG ITSYHAARFL KERMSFKDVK
SLEGGIIVWQ GPTEKSI
//
