ID R7CHC2_9ACTN Unreviewed; 581 AA.
AC R7CHC2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN ORFNames=BN613_00157 {ECO:0000313|EMBL:CDD77142.1};
OS Cryptobacterium sp. CAG:338.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Cryptobacterium.
OX NCBI_TaxID=1262868 {ECO:0000313|EMBL:CDD77142.1, ECO:0000313|Proteomes:UP000018369};
RN [1] {ECO:0000313|EMBL:CDD77142.1, ECO:0000313|Proteomes:UP000018369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:338 {ECO:0000313|Proteomes:UP000018369};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:CDD77142.1}.
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DR EMBL; CBHR010000160; CDD77142.1; -; Genomic_DNA.
DR AlphaFoldDB; R7CHC2; -.
DR STRING; 1262868.BN613_00157; -.
DR Proteomes; UP000018369; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF1; PHAGE SHOCK PROTEIN E-RELATED PROTEIN; 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; 2.
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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018369}.
FT DOMAIN 478..569
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 581 AA; 62440 MW; 0D9A0CB2EAFA05E5 CRC64;
MKVVIVGGVA GGATCAARLR RLDEQAEIII IERTHYVSYA NCGLPYYIGG TITDRAKLTL
QTPKSFRSRF NIDVRVDQEV TQINREAHEV EIRNLVTGNT YTETYDKLVL SPGAHPIMPN
LSGIESSRVF TLRTVEDTFA IADFIEQTHT TSATVVGGGF IGLEMAENLV DRGMDVAVLQ
RPTHLMHSLD DDIASLLHNR MREAGITLKL GADVAGFTET GDSISGGITT SFKDKGDDIG
ATAQTITSDL VILAIGVAPE SNLAKAAGLD LGIKGSIKVN KHLLTSDPDI YAIGDAIETT
QVVTGKSAHI ALAGPANKQG RIVADHICSI DRSFTGSLGS SIMKAFDLTV ATTGLSTKTA
TASGLNFDSI IITPASHATY YPGSHAMTMK VLFERPTGRI LGAQIIGVDG VDKRIDVLAV
AIKAGMTAFD LTEIDLAYAP PYASAKDPVN MAGDVIENIL EGTVNQIHWD EALDRAVTDE
NVVILDTRTD AEFSRGHIEN TLNPVLHIPV DSLREQMDEI PRDKQLLVHC ATGIRSYIAC
RILKQNDFDC TNIAGGYNFY QALKLDRNAD AKNVGDCGLK A
//
