ID K2RYE2_MACPH Unreviewed; 543 AA.
AC K2RYE2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 22-FEB-2023, entry version 29.
DE RecName: Full=Rhodanese domain-containing protein {ECO:0000259|PROSITE:PS50206};
GN ORFNames=MPH_13504 {ECO:0000313|EMBL:EKG09455.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG09455.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG09455.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG09455.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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:EKG09455.1}.
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DR EMBL; AHHD01000660; EKG09455.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RYE2; -.
DR STRING; 1126212.K2RYE2; -.
DR VEuPathDB; FungiDB:MPH_13504; -.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_1_2_1; -.
DR InParanoid; K2RYE2; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000007129; 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; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007129}.
FT DOMAIN 460..540
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 543 AA; 59334 MW; B019B25C9EAB541C CRC64;
MNIVIVGGVA GGMSAATRAR RLDETAHITV FEKGPYVSYA NCGIPYALGK VIEDDGSLIL
QTPKSFRDRF NIDVRLNTEA ITIDREKRLV HVRTTDTEEQ HHAPYDKLIL AQGAEPFRPP
IEGIGLPNVF TLQTIMDLQS IRCFMSEHRV KKTTIIGGGF IGLEAAENLR NLGLEVSLLE
YAPHVFPPVD RDMAGPIHAE LRRNDVRVIL NARVQQIQLG CVVQASGEEI PTDLVLLAVG
IRARAALARQ AGLKVGKAGV SVNEFMQTSD PDIYAVGDMV ETEHRIAARP LSLALAGPAN
RQGRLAADHI FGKAIRYRGN VGTAVCKVFD LTVAATGLSV SSLRQAGYDP LWVTVHPPDH
AGYYPGANSI MLKVAFERQT GRLLGAQAVG KTNVDKRIDV LSTTLQAGMT IFDLEHLELA
YAPPFGSAKD PVNMAGFVGS NVLRGDTEIV HTEDLANTRD LDQMQLVDVR SQKEFARGHI
PFARNLPVNS LRDGLSGLDK SRRVVVYCQV GYRGYLAYRI LKQNGFDAVN LDGGYRSVVE
GYF
//