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Database: UniProt
Entry: A0A286UKD9_9AGAM
LinkDB: A0A286UKD9_9AGAM
Original site: A0A286UKD9_9AGAM 
ID   A0A286UKD9_9AGAM        Unreviewed;      1481 AA.
AC   A0A286UKD9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Sulfite reductase subunit beta {ECO:0000313|EMBL:PAV20086.1};
GN   ORFNames=PNOK_0502000 {ECO:0000313|EMBL:PAV20086.1};
OS   Pyrrhoderma noxium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Hymenochaetaceae; Pyrrhoderma.
OX   NCBI_TaxID=2282107 {ECO:0000313|EMBL:PAV20086.1, ECO:0000313|Proteomes:UP000217199};
RN   [1] {ECO:0000313|Proteomes:UP000217199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FFPRI411160 {ECO:0000313|Proteomes:UP000217199};
RA   Chung C.-L., Lee J.T., Akiba M., Lee H.-H., Kuo T.-H., Liu D., Ke H.-M.,
RA   Yokoi T., Roa M.B., Lu M.J., Chang Y.-Y., Ann P.-J., Tsai J.-N.,
RA   Chen C.-Y., Tzean S.-S., Ota Y., Hattori T., Sahashi N., Liou R.-F.,
RA   Kikuchi T., Tsai I.J.;
RT   "The Genomic Landscape Of Tree Rot In Phellinus noxius And Its
RT   Hymenochaetales Members.";
RL   bioRxiv 0:0-0(2017).
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:PAV20086.1}.
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DR   EMBL; NBII01000004; PAV20086.1; -; Genomic_DNA.
DR   STRING; 2282107.A0A286UKD9; -.
DR   InParanoid; A0A286UKD9; -.
DR   OrthoDB; 276396at2759; -.
DR   Proteomes; UP000217199; Chromosome 4.
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   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000217199}.
FT   DOMAIN          737..891
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50902"
FT   REGION          197..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1481 AA;  162080 MW;  09F1B61CA0552240 CRC64;
     MSIGLRGTLA DKVADSNLEG LDSPAITCFG GVACSLVHLG TLSRKMALSA VSAVARVAFF
     TSDVVVDLKQ SSEYSIFSDE YKTLARKATH TPRIIPVSYA ADPGAYASYH KSASLLAFTA
     QSSPRVLSQL LPHLSELSSS PIVLHFAVNG DLADVLRLRS AVPYFIHSST LRQAHDNALI
     ASRIARTEQQ IRTYVSHEKV AAPTNGKVNG ASSNGHTNGH SNGHTNGHAN GHTNGHANGH
     TNGYTNGYTN GHVNDLSDSS SSGVTTPSTP SSSFKSLDDP TILSLYGAYE TASLSLSTLL
     LKLIELLGSI PSDVKQIVVL EQIGSWNVKW TPLYLELMSA LQFLDKSFPE IRSGLLGDPA
     TVTDIDVLKF LQQSNESSQR LRLGKASGSV EADKTIVSIP KVPKHEASYT KILETLFAER
     LEVANKPEYV AAHGNLATTP EFALGRVQRQ LEDRDRLIKA VQTVVESSSA ASDLHSLLSK
     WLLARDDHAK SSSLGSEIIS QLESNPSVHP LVPTILSLRT HFPAVSRWII GSDAWSYDLG
     ASGLHHLIAS GLNVNTLILD TVPYSYRNVD EDPLRRRKRD VGLYAMNHGD VYVASVAVYS
     SYTQVLQALT EADRFPGPSV VLAYLPYLNE DVPALDVLKE TKLAVDTGYW PLYRWNPSKE
     NVTGAEPFSL DSDVIKQELQ TFLDRQNHLS QLSRAQPTLA AELVSSLGEK VLVARQERAK
     KAYEDLLSGV GGGAGPLLVL YASDGGAAEK KARRLAARAR ARGLTTNIAV MDSTSLEELS
     KNEEDFVAFI TSVAGQGEAP QNGRALFKAL NAAAARGERP LASLKYSVFG MGDSHYWPRP
     EDAHFYNKAG KDLDARLESL GATRFADLGL GDDQDADGSE TGYKLWEPLI WKALGVDNVE
     IIEAEPDPIT NEHMKIASNY LRGTIVEGLE DTSTGALAPS DTQLTKFHGI YQQDDRDIRD
     ERTAQGAEPA YSFMIRVRMP GGVCSPEQWL AMDQISDEHG NGTFKITTRQ TYQFHGVIKR
     HLKQTIRDIN RALLDTLAAC GDVNRNVITS AIPEKSRLHA EVYEFATAIS ERLLPRTTAY
     HEIWLDKKLV AGDAVRDFEP LYGEFYLPRK FKVAVAVPPT NDVDVFANDV GFIAIIGKDG
     NLEGFNVTAG GGMGVTHGNK KTYPRLGSVL GFCTPEQGCD VAEKIMLVQR DNGNRADRKN
     ARLKYTIDRM GLDVFKGEVE KLLGWKLGPA RSYTFERNID DFGWSTGENG KHNFMMYIEN
     GRVQDEAGKE FKAGLREIAK IHKGTFRMTT NQHLLLADVP TEELPRIKKL LQYYKLDNLN
     FSGLRLSSSA CVAFPTCGLA MAESERYLPL LINKVEAICE ENGLRNDSIV MRMTGCPNGC
     ARPYVAEVAF VGKAPGTYLM LLGGGYYGQR LNKIYRESVT EPEILAILRP MIKHYALERL
     EGEHFGDFVI RAGYISATTE GKAWYEGMGG LGAHREISSV A
//
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