ID A0A443HQ18_BYSSP Unreviewed; 1523 AA.
AC A0A443HQ18;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Sulfite reductase [NADPH] subunit beta {ECO:0000313|EMBL:RWQ93879.1};
GN ORFNames=C8Q69DRAFT_471816 {ECO:0000313|EMBL:RWQ93879.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ93879.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWQ93879.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ93879.1,
RC ECO:0000313|Proteomes:UP000283841};
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
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:RWQ93879.1}.
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DR EMBL; RCNU01000008; RWQ93879.1; -; Genomic_DNA.
DR STRING; 264951.A0A443HQ18; -.
DR OrthoDB; 5474937at2759; -.
DR Proteomes; UP000283841; Unassembled WGS sequence.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.90.480.20; -; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
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; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
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 Pfam; PF01855; POR_N; 1.
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); 2.
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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000283841}.
FT DOMAIN 778..927
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT REGION 197..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1523 AA; 167184 MW; 2D554A0D84000DE2 CRC64;
MGSISTAGEA VARIAYLASD VVLSVQPSLR TDSQFSKSLN SLKAKGASGL ISKAAPEVRA
VRENADPLLS AFYPLQSGSI VSVTTSSNVL LSSIPHLFRL ANYPIVIHVA LDASPFPDYS
VISSIRQCGF AFLQSETLQE AQDIALTAHA LAIKSGKGVI HFFDPANSQA DNAIAEEDIE
VVKKVLDLEG DKATHVSGTG EQTLYTDSGR AATVEEKVEA APEAETEGAA ALPTPAKSPV
DSTDASSVGS SKRDSSVDSR APSSTATTVD VAAARPVNAA DVFEFTAQIW ETLSKATGRS
YHAVEYTGPH NAKSAIFIFG STGVFVDALE GAKDQPELQN VGIITARLYR PWVGSQISSS
IPASVEKIAV VEQARKTTRW GPAFLDLLSS LSPSQAPRLV AYRLGYVEPS TAVQALRGIL
QNLGSETPIQ NLEIGSHKAP LQKVPEQPEL ENAYTKILQQ LFNDRLYVAN QLASNNAGIS
ATIAASPEYG FGSLIARTEH RERLIREVEE AAKSGVFTTE TPKSWLSKWA LSARDAAKAN
SLAPDVISHL SVDGSKTAQD LLQSKQLFFK ESQWLIGSEA WAYDLGNSGV HHVLASGANV
NMLIIDSEPY SERAAADPTR RKKDIGLYAM NFGNAYVASV AVYGSYTQVL QAMAEADQFE
GPSVVVAYLP YNKEDDSPLT VLQETKKAVD LGYWPLYRWN PGQEENGEPK FSLDSERIRR
ELEDFLRRDN QLTQLMKRHP NFSSSLSESY GTEVRALQKR KAKDSYEKLL EGLFGAPLTI
LFASDNGNAQ NLAKRLGNRG RARGLKTTVF AMDDYPIEDL STEENVVFIT SVAGQGEFPQ
NGRSFWEVVK NSGDLDLSSI NYSVFGLGDS HYWPRKEDRI YYNKPAKDID ARVSFLGGRK
LTDIGLGDDQ DPDGYQTGYS EWEPRLWKAL GVDNVEGLPE EPAPLTNEDI KAQSNFLRGT
IVEGLNDEST GAISASDQQL TKFHGTYMQD DRDVRDERKA QGLEPAYSFM IRCRLPGGVA
TPSQYLQMDA ISSAHGNETM KLTTRQTFQF HGVVKGKLRA AMRAINKALM TTIAACGDVN
RNVMCSSLPE LSGYHREVHA VSKRISDHLI PATTAYHEIW LKDDNDKKIQ VAGDAVVDHE
PLYGPTYLPR KFKITIAIPP HNDTDVYAHD IGLIAIKGAD GHLEGFNVLV GGGMGTTHNN
KKTYPRTGSM LGFVPADQTH LVCEKIMLVQ RDHGDRKNRK HARLKYTIDD MGLDVFKSKV
EAILPEGVQF AEPRPFKFVS NIDTFGWQKD EKGLNHFTFF IENGRIEDTA DFPMRTGLRE
IAKLNKGEFR LTGNQHLILS NIEDADLPEI KALMAKYKLD NTSFSGLRLS SSACVAFPTC
GLAMAESERY LPVLISKLEA TLEENGLGKE SIVMRMTGCP NGCARPWLAE VAFVGKAYGA
YNMYLGGGYH GQRLNKLYRA SIKEDEILDI MKDLFKRYSL ERKTAPGQEP ERFGDWCIRA
GIIKETTEGK NFHEGVAEED EEE
//
