ID A0A1Q5UDV2_9EURO Unreviewed; 557 AA.
AC A0A1Q5UDV2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE SubName: Full=Coenzyme A disulfide reductase {ECO:0000313|EMBL:OKP10652.1};
GN ORFNames=PENSUB_3955 {ECO:0000313|EMBL:OKP10652.1};
OS Penicillium subrubescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1316194 {ECO:0000313|EMBL:OKP10652.1, ECO:0000313|Proteomes:UP000186955};
RN [1] {ECO:0000313|EMBL:OKP10652.1, ECO:0000313|Proteomes:UP000186955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 132785 {ECO:0000313|EMBL:OKP10652.1,
RC ECO:0000313|Proteomes:UP000186955};
RA De Vries R.P., Peng M., Dilokpimol A., Hilden K., Makela M.R.,
RA Grigoriev I., Riley R., Granchi Z.;
RT "Genome sequence of the ascomycete fungus Penicillium subrubescens.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OKP10652.1}.
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DR EMBL; MNBE01000313; OKP10652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5UDV2; -.
DR STRING; 1316194.A0A1Q5UDV2; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000186955; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase 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 InterPro; IPR001307; Thiosulphate_STrfase_CS.
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; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000186955}.
FT DOMAIN 464..551
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 557 AA; 60587 MW; DD85FBD71C14B047 CRC64;
MKIVIVGGAA GGMSAALRAR RLDEDAHITL IEQGDSLNYA NSGIPSSVGG VIETDTFLIH
QSAAGLKERF NIDMRENTEL VGISKENHSI LLKASNTNET YQLSYDKLIL AQGAHPMPLP
APGIEGEHVF RFQTMLDLHK IRDYVSGHFF KSAAIIGGGY VALKAVEALH NFGLRISIIH
FQNRICQDFD PDIANLIQSE LVKNGVHLHL NAKIQRIDIG TAEDSRVVTL VNGPSVPADL
VIIATDLAPC TEITKQSGLE CRDDGVLVNE FMQTNDPDIY AVGDMTKTTN FISSTPKTLP
LGGAASLQGR LAVDHIMKRA IPYRGHIGMY SCKVLTLTVA ILGLSVEKLK EVGYHPQFVT
VHVPDHTGYY PSSQQMTLRL AFQPASGRLL SAQILGRRGV DKRLDVLSVA LQSGMTVFDL
ENLQLSYAPE YGSAKDPVNV LGMVAANLLR GDLHTVTAAE LEARLDDWQI IDVQSPEIFA
QGHVPGALNV PIDTLRNRLA CIDKRKPVVV YSRVGYHGYL AYRTLAQLGY KVFNLDGGFK
LFSEGGSRLG IASGKVS
//
