ID V2XUX2_MONRO Unreviewed; 1055 AA.
AC V2XUX2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE SubName: Full=Assimilatory sulfite reductase {ECO:0000313|EMBL:ESK97577.1};
GN ORFNames=Moror_17577 {ECO:0000313|EMBL:ESK97577.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK97577.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK97577.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK97577.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK97577.1}.
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DR EMBL; AWSO01000024; ESK97577.1; -; Genomic_DNA.
DR RefSeq; XP_007843150.1; XM_007844959.1.
DR AlphaFoldDB; V2XUX2; -.
DR STRING; 1381753.V2XUX2; -.
DR KEGG; mrr:Moror_17577; -.
DR HOGENOM; CLU_003662_0_0_1; -.
DR OrthoDB; 5488444at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06207; CyPoR_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT DOMAIN 670..901
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 1055 AA; 114841 MW; 71E37672D93924D2 CRC64;
MTREIPAIST ASSVTLASPI SPVTASFIEA TLEKLLHDPK IPASTIVEFL ASRSKNSSAV
YVYDLAEQVG FGTLTREWAK TQKGTAHTVD LQTRAGAGLS LVGRLSEGTS SDTATGAVLT
AYTSPHGLAK MAPALSHLPT ATASSRLVVQ VPTVTPVGEA FALSPSLASL TSTMSILPNN
IVVLLSSTAR EIIHFTQIAY KLTRSHVIHL FDHFSTGREI GHAVLPLSEQ QLQGGSIEEV
VKQAGYSFFD YTGDLNAHTA IILLNGPFAL AARAIARHTP GLGVVSVNVL RPWNEDALRC
VIPSTVKTIH VLDDVPNAAT QGPVYMDVIA AFLVSMNTLS IHSHRIIPAR TQELLLREDG
FFYYLSKIIS FLSKPPPPKY LRKLLFFNTP ESTLLPASGL VENALLTSQG VSAHLLTDHD
VFSKRGGITA SRILLHSKKD QHELPIPFVI PFDLGSSGDA DFLAVLDPSI MKTHAVLNYA
RPGALILIAT SWTPEEFFAS LPAPAASLLS ERDLRSFVID AESIASNFTE DVGFSRGDIA
SVVVYLAFLR LYLGAAATSD AVLAVARDTV GDAIEGVDLG KIHTRVWEAL EELDVLPPSG
DQSSSPLKRF EFNAIAVETY DGETVVNGAV LGSWHDAAKH IIFPSAFTPP VPESNEEFPQ
NPALRPEVPD RTYLVTCTVN RRLTPKEYDR NVFHLEFDTS GTGLKYAIGE ALGIHGWNDG
QEVLDFCEWY GADLNQLITI PVPNSEGRMH TRTVMQALQQ QIDLFGHPPK AFYTDLAAHA
TTSVDKHALL FIGSAEGSST YKKLSEKDTV TFADVLRMYP SAKPGIETLC ELVGDIKPRH
YSIASAQSVV GNRVDLLVVT VEWITPSGSP RYGQCTKYLA GLKIGQKVTV SIKPSVMKLP
PDDKQPLIMA GLGTGAAPFR AFLQHKAWLV SQGKEIGPVY YYFGSRHQSQ EYLYGEEIEA
FILDGVITRA GLAFSRDGPK KVYIQHRMLE DSKALIDMLH EQNGVFYLCG PTWPVPDVFE
ALCNAMETYK GIDAKAAGEY LEGLKEEERY VLEVY
//
