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Database: UniProt
Entry: A0A0F9WNI8_9MICR
LinkDB: A0A0F9WNI8_9MICR
Original site: A0A0F9WNI8_9MICR 
ID   A0A0F9WNI8_9MICR        Unreviewed;       377 AA.
AC   A0A0F9WNI8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Sulfite reductase subunit alpha {ECO:0000313|EMBL:KKO74573.1};
GN   ORFNames=AAJ76_5900016370 {ECO:0000313|EMBL:KKO74573.1};
OS   Vairimorpha ceranae.
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Nosematidae;
OC   Vairimorpha.
OX   NCBI_TaxID=40302 {ECO:0000313|EMBL:KKO74573.1, ECO:0000313|Proteomes:UP000034350};
RN   [1] {ECO:0000313|EMBL:KKO74573.1, ECO:0000313|Proteomes:UP000034350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA08 1199 {ECO:0000313|EMBL:KKO74573.1,
RC   ECO:0000313|Proteomes:UP000034350};
RX   PubMed=25914091;
RA   Pelin A., Selman M., Aris-Brosou S., Farinelli L., Corradi N.;
RT   "Genome analyses suggest the presence of polyploidy and recent human-driven
RT   expansions in eight global populations of the honeybee pathogen Nosema
RT   ceranae.";
RL   Environ. Microbiol. 0:0-0(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KKO74573.1}.
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DR   EMBL; JPQZ01000059; KKO74573.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F9WNI8; -.
DR   VEuPathDB; MicrosporidiaDB:AAJ76_5900016370; -.
DR   VEuPathDB; MicrosporidiaDB:G9O61_00g013710; -.
DR   VEuPathDB; MicrosporidiaDB:NCER_101456; -.
DR   OrthoDB; 9164at2759; -.
DR   Proteomes; UP000034350; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034350}.
FT   DOMAIN          71..225
FT                   /note="Sulfite reductase [NADPH] flavoprotein alpha-
FT                   component-like FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00667"
FT   DOMAIN          264..353
FT                   /note="Oxidoreductase FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00175"
SQ   SEQUENCE   377 AA;  44324 MW;  FB8D2A541375C2D9 CRC64;
     MKFNKLEYNL NVDFVPLNIR NFNKLIIKKT NYTGSYKIKT NENINLIDTN ILNIENLFCT
     WKKVYKVQLN YTLDFVPGDS IGLLCSNNDL LVNEMLSLLE MSGDTLLYIE QVGKTGFQFE
     GSLRDFFKYI FDFTSLPKKA WLMDISKTSK NKHDIEYLCS KEGVKDYLSI IKNWNNVLDI
     IYTFQCKPSL EDLIMNCQTI KPRYYSLTNH VNEKCEILVA IIKKGDRYGH VSNFIDMQNY
     NNLKICHRPS KLFRLNFCKK VLGICTGTGI APFFSFLKNK EDDQYIKLIY GFRNQEDDLI
     KDAKYKNTEI IKILSCNKIY VTDYLLQNLN KIKTYIKDGC LVYVCGRPDM QKTIYSIFNE
     NFSEIVKEKR LFFDSWI
//
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