ID A0A2T9YP40_9FUNG Unreviewed; 1521 AA.
AC A0A2T9YP40;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN ORFNames=BB561_002827 {ECO:0000313|EMBL:PVU94061.1};
OS Smittium simulii.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133385 {ECO:0000313|EMBL:PVU94061.1, ECO:0000313|Proteomes:UP000245383};
RN [1] {ECO:0000313|EMBL:PVU94061.1, ECO:0000313|Proteomes:UP000245383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWE-8-4 {ECO:0000313|EMBL:PVU94061.1,
RC ECO:0000313|Proteomes:UP000245383};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(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:PVU94061.1}.
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DR EMBL; MBFR01000103; PVU94061.1; -; Genomic_DNA.
DR STRING; 133385.A0A2T9YP40; -.
DR Proteomes; UP000245383; 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 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 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; 1.
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); 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 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:UP000245383}.
FT DOMAIN 794..942
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 1521 AA; 169725 MW; 9FD9338B1EA21A9A CRC64;
MIYQNLKLNA FSSAALSAYY SSDIILIEDG ELSASAIGIL DSLVSKNSSF PTKNSIRPPS
IIKISPFGDF PKILQSALEP TETPTSVSVI ATSHILLSLL PTVYSYSKLF SDKNKHIPSL
TITIGISGPK NNQSDASDVM AYMDSKCSIF ASHTIQQVFD FSLISSIISK NSQIPAISYF
DSNILDNFKL ENIIFRDFSS TVELYKTIVN KKSDEASTLS EKSNIDLESV NTQNLSKESN
DNVLDGKDKI LEQINIDQII SSSLDLFKST PYLPAKYDGS TDASVVFVSI TDFGFSKDVD
FVESSCGYLT LYQVRPLPKQ LILEKLPASV KKIVILEHIE ENSKIWGPLV FDFIELIQSS
AFKDRNSINP LIIDIQSPYS FSKQLSIAGS LKNLLSIINS TNCSKLFKMS KIALDSPNEQ
TQNNNESSEN QDTFKALDLH QYSEVEIANQ IPYQKLFETV FQDRFKIINS ENPSMIWSNL
NSLKSNPEYG FGILASQEQK QRQLHKIVTD ILQDTENDLG TEINTLLYKW VETVSKANSD
LVQLVKNINS AIKNYQNVDS PYIKSLKEYS ANFLTYSNWL VGSDEWAVDF GNSGIHQVLS
SGFNINMLIL DSANYSDSRS DENNQLAALL KNKKDIGLYA LNYGNAYVAS ISAYASYTQA
LTALIEASTF PGPSVVLAHI PSQSEKVINT SHSPIESMKL AKIAVDNGKW PLYRWTPKIE
SNNDGNFILD SQKLRNEIKQ FLDKKNTLCL ISNTVPTYNS KINNSVEQTQ ADAIAKSAKS
DLEKLMAGLQ GPSITILYAS DGSNAHAVAK KIHFGAKARK MSSEIFIMND FDFSEIEFKS
LVIFVVSTAG QGEFPTNGKG FWKSLKDASV NLSNLKYSVF ALGDSHYWPS EEDSIFYNKP
GKDLDKRLFE LSAIRLCSIG LGDDSNDNGW EAGFSAWEPE LWKSLGYDSL VDLSNVYEDE
PPKISDEDNK IQSNYLRGNI VAELNDSSKG DVDEFTGKLL KFHGTYGQDD RDIRDQRIEN
GLSPAYSFMI RVRLPAGKAT CKQWIAMDDL ATKYGNETIK ITTRQTFQLH GVLKSNLRNT
INSINKALMD TIAACGDVNR NVVSSANPLQ PQLREEVAKL AKDISESLLP KTTAYHEIWV
SDKIVAGQAL QDFEPMYGQS YLPRKFKIAI AIPPENDVDV FAYDLGLIAI LNESEDIIGY
NVAVGGGMGM THNNKKTYPR LASILGYINK NDVIEVSKAI VTTQRDFGDR KNRKHARMKY
TIDDYGIDWF RSQVEERSNV KFEQEKKYNF VRNGDRYGWV DSIPGYKNYT MFVQNGRVAD
LPGYQLKSAL RNIASVHKGY IQLTCNSHVI IADVANKDVA NMDDLLKKLG VHNKNHSQLR
LHSMACTSFP TCGLAMAESE RYLPSLVTLL DETINEAGLR NDAIVIRMTG CPNGCARPYV
AEIGLVGKAP GTYNLYLGGA HNGSRLNKVY KESVQEEEIL EILKPLIKNY ALEKLDDEKF
GDYVIRSGVI RETFQGLDFH N
//
