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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//