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Database: UniProt
Entry: K2RYE2_MACPH
LinkDB: K2RYE2_MACPH
Original site: K2RYE2_MACPH 
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
//
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