ID G4UJD1_NEUT9 Unreviewed; 1538 AA.
AC G4UJD1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Sulfite reductase beta subunit {ECO:0000313|EMBL:EGZ74100.1};
GN ORFNames=NEUTE2DRAFT_87991 {ECO:0000313|EMBL:EGZ74100.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ74100.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ74100.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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}.
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DR EMBL; GL891217; EGZ74100.1; -; Genomic_DNA.
DR STRING; 510952.G4UJD1; -.
DR eggNOG; KOG0560; Eukaryota.
DR HOGENOM; CLU_001975_1_0_1; -.
DR OMA; YGSYTQV; -.
DR Proteomes; UP000008513; 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 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 Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 1.
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; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
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 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 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:UP000008513}.
FT DOMAIN 799..948
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT REGION 248..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1538 AA; 169016 MW; 91771821EF017950 CRC64;
MASTQQIKTP QEAVARIAYL ASDVVVSVQP SLAAESDFSA TLKSLASSRT QSLVSKAADA
VAEIIPVRHN NDPLLSVFTP IRSGRLVSVT TTSEVLLPSI AHLYKLAQLP VVLHVALGPK
SLPDYTAITS IRNSGWTFLQ SNSLQEAQDL ALTAHALAVQ SGKGVIHFFD PSSSASEQPI
AAEDISLVQE ILNLDNVRRF QSASISGSSI YANDGRVAVV SEQSEPVASQ TILDARQVEA
ATATATDSLA PAQDGSDESA QTSQEQSEAS EASATPSASV ATTIDEQAPV VTSEHIYKYV
TAIWAKLNDL AGRQYSAFEY SGPSNAENAL FVFGSGSPLF AQAIAQAQSD DSFAKAGVLT
ARLYRPWLGA KLLEAIPKSV KRVAVLEQVS RKTTKWGPLL IDVLTSVKSG PGGVETIVGH
QLGYISQETV VQALRGIFQN LTSEKPVQNL EVGEREAPKE ASEYGLEKPK LETAYTKILD
QLFGERAYIA NSIEKDNAGV SNTISATPEY GFGALLARKE RKQKFVSEVK EAASNGQFSS
DAPKQALAKW VANAEDSKKV EEVASEAVSK LSEDGSDLSK SLLEYKQFFR KQSLWLVGSD
AWSYDLGNSG VHHVLASGEN VNLLIIDSTP YSERAAADAN RRKKDIGLYA MNFGNAYVAS
TAVYSSYTQV LQAMDEADKF NGPSVVLAYL PYFGEHDSAL TVLQETKKAV DIGYWPLYRW
NPENEKKGEP SFSLDSERIK KELKEFLDRD NHLTQLMKKE PSFGAVLSED FGTEIRAQQK
RKAKDAYNQL LEGLFGAPLT ILYASDNGNA ISLSKRLGNR GRARGLKTTV MSMEDYPVED
LATEENIVFI TSTAGQGEFP QNGLSFWHAV KDNTSLDLAN VRYSVFGLGD SHYWPRKEDK
IYYNKPAKDL DRVLANFGAK PLAPIGLGDD QDPDGFQTGY SEWEPKLWEA LGVANVDGLP
EEPAPRTNED IKIESNYLRG TIVQGLNDTS TLAISADDSQ LTKFHGTYMQ DDRDIRDERK
AQGLEPAYSF MIRCRLPGGV STAKQWVQMD DIANELGNET MKLTTRQTFQ FHGVVKSKLK
PAMQAINRAL MTTIAACGDV NRNVMCSPLP AHSKYHRAVH ACAKRISDHL LPNTTAYHEI
WLTDDDGAKT QVGGNAVQDF EPLYGPTYLP RKFKVSIAIP PHNDVDVYAH DIGLIAIKNE
DGSLAGFNLL AGGGMGATHN NKKTYPQTGR MLGFVTAADV HLACEKVMLV QRDNGDRKNR
KHARLKYTID DMGVDVFKAK VEEYWGQKFE EARPFHFDSN VDTFGWTKDE TGLNHFTMFI
ENGRIEDTAE FQMKTGLREI AKVHKGEFRL TPNQHLILSN VADEDKPELE KLLAQYKLDN
LHHSGLRLSS SACVAFPTCG LAMAESERYL PVLITKLEGV LEEVGLKQDS IVMRMTGCPN
GCARPWLAEV AFVGKAYGAY NMYLGGGYHG QRLNKLYRSS IKEDEILTIM KGLLRRYAKE
REEGERFGDW TIRAGIIKAT TDGRNFHEGV AEEEGDEE
//
