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Database: UniProt
Entry: V2XYV1_MONRO
LinkDB: V2XYV1_MONRO
Original site: V2XYV1_MONRO 
ID   V2XYV1_MONRO            Unreviewed;      1457 AA.
AC   V2XYV1;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Sulfite reductase beta subunit {ECO:0000313|EMBL:ESK97670.1};
GN   ORFNames=Moror_17452 {ECO:0000313|EMBL:ESK97670.1};
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:ESK97670.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK97670.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK97670.1,
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000256|ARBA:ARBA00001929};
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000256|ARBA:ARBA00010429}.
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:ESK97670.1}.
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DR   EMBL; AWSO01000021; ESK97670.1; -; Genomic_DNA.
DR   RefSeq; XP_007843025.1; XM_007844834.1.
DR   STRING; 1381753.V2XYV1; -.
DR   KEGG; mrr:Moror_17452; -.
DR   HOGENOM; CLU_001975_0_1_1; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
DR   GO; GO:0009337; C:sulfite reductase complex (NADPH); IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:InterPro.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR   HAMAP; MF_01540; CysI; 1.
DR   InterPro; IPR011786; CysI.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR02041; CysI; 1.
DR   PANTHER; PTHR11493:SF47; SULFITE REDUCTASE [NADPH] SUBUNIT BETA; 1.
DR   PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 2.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559}.
FT   DOMAIN          720..872
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
SQ   SEQUENCE   1457 AA;  161449 MW;  44E5B3A24A8F2A58 CRC64;
     MRCFRRQVSI SLAHQLLWSD EVFEVFIMTA IDAVARIAFI ASDTLVHSLP SATPVISRVS
     ELSKQRTPLV VPVPNGGDPA ASILRRSSSG GLIAYLASLG SQSISRLVLA CSELSSLPLV
     LHIAVGNDLS DALLLRAVAP YFILSANAQQ ASDNALLASR IARAEKKAVV HVFYGQSEEG
     KVTELEEDEI LQLLFKEEEN KLNGVNGHAN GHVNGDVLRH QDDPDILALF KAYERASLHT
     LSFVHRPIRS FTTRGSSEPH TLIFLLGRDN LDVDVDGVSF VSVSLLSPLL PSRILNEIPL
     TISCVVVLEQ VTNWSMKWTP LYLEVVSALQ QREATERPTV HTGVLGNLDD VSEIDVQKLL
     QRAAESPLSR LSLGSIPSPN QASIHIEPHV PKHELSYTKI LSHLFNDRLE VSNSPSFVRS
     QGEIATTPEY ALGRVRGQLE RRDELIAAVR ELLQSPGLDA KLHSLLSKWV LAKDHAEKSR
     MLGQEIVQHL EASPVKSSAA DTVLSLRTYL PSASRWIIGS DAWSYDLGAS GLHHAIASKL
     NVNILLIDTV PYSSRNSSDQ GRRKHDVGLY AMNHGDVYVG SVAVYSSYAQ VLQALLEADA
     YSGPSVVLAY LPYASEDVMA LDILKETKLA VDAGYWPLYR WDPSKERDGK EPFSLDSDAI
     KIDLQQFLDR QNHLSQLVRS KPEMASELVS SLGETVKEAR KKKAQQSYNE LVTALDVPPI
     TILYASDGGA AEKVAKRVRN RAQVRGLTVT LATMDSVPLD TLVGEEYVVF VTSTAGQGEP
     PQNGRQFFKA INAAVSKGDK LFTKLKYAIF GMGDSHYWPR PEDAQYYNKP GKDLDVRLEK
     LGGERVIDLA LGDDQDADGY QTGYKAWEPK LWKLFGVDNI EVTEKEPDPI TNEHIKAASN
     YLRGTIAEGL EDTSTGALAA SDTQLTKFHG IYQQDDRDIR EERQAQGVEP AYAFMIRVRM
     PGGVCKPDQW LQMDQIANEH GNGTFKITTR QTFQFHGVIK RHLKPAIQDI NRALLDTLAA
     CGDVNRNVIC SSIPTMSKLH AQVHQFCVTV SEHLVPRTTA YHEIWLDKKL VAGEALKDVE
     PLYGEFYLPR KFKIAVAVPP TNDVDVFAND VGFIAIVDDQ GELAGFNVTV GGGMGVTFGN
     KKTYPRTADV VGFCKPDQGK YMAEKIMLVQ RDNGNRVDRK NARLKYTIDR MGLDVFKAEV
     EKLLGYELEP SRPYAFDRNI DDFGWATGED GKHHFTMFIE NGRIQDEPGK DFKTGLREIA
     KVHKGTFRLT ANQHLLISDI ADDDLPRIKE ILAQFRMDNL NYTGLRLSSS ACVAFPTCGL
     ANAESERYLP LLIDKVEKLC EENGLRNDSI VMRMTGCPNG CARPYVAEVA FVGKAPGTYL
     MLLGGGYYGQ RVNKIYRETV TEPEILAILG PMIKRYALER NEGEHFGDWT VRAGYIAQTT
     SGKEYYDRAG GEEQFQV
//
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