ID A0A3M6VJL1_9STRA Unreviewed; 1499 AA.
AC A0A3M6VJL1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN ORFNames=DD238_004746 {ECO:0000313|EMBL:RMX65706.1};
OS Peronospora effusa.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Peronospora.
OX NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX65706.1, ECO:0000313|Proteomes:UP000282087};
RN [1] {ECO:0000313|EMBL:RMX65706.1, ECO:0000313|Proteomes:UP000282087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R14 {ECO:0000313|EMBL:RMX65706.1,
RC ECO:0000313|Proteomes:UP000282087};
RA Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA Reyes Chin-Wo S., Mou B., Michelmore R.;
RT "Comparative genomics of downy mildews reveals potential adaptations to
RT biotrophy.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RMX65706.1}.
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DR EMBL; QLLG01000233; RMX65706.1; -; Genomic_DNA.
DR STRING; 542832.A0A3M6VJL1; -.
DR VEuPathDB; FungiDB:DD237_005095; -.
DR Proteomes; UP000282087; 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; 3.30.413.10; 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:UP000282087}.
FT DOMAIN 758..911
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
SQ SEQUENCE 1499 AA; 167062 MW; 14C7E6A7CE9909D8 CRC64;
MPQFIAAVEE AISHVAYAFS DYSYLVQPVP FGSALEKYII NARRNVFDQV GKVEENVVGQ
ELIERAYAAA TCGQFVTLFV SSPSTLLQMV PVMYKLSRAQ LPAVIHVVAR EHSDLMAVRQ
TGFVILYSLN SIETEDMALL THVASLRANV PFLHVYDGEM TRNDLEQQVA ASSHKLNTLV
NYEYLANLIG LKNASEAPAF RQLVLSKSSV ATNADDAELY FQVSPECIAK YNAVPEIIED
VIQQVFTKRN YQLFEYFGHP EAKQVLVVMG TASSVVKDAV EALYTNWKAE IGVISVRLFR
PWSTKSFLNV VPATAVKFAV LDRMDDATNV GEPLFMDVLG SFQSEEWQKK PVPLVIGGKY
AYNVSESVFD VVTARTLVED LTANKLQNGF VVASPAAVEN YNAKTTTTAQ RVNSYVSSKD
GFEGPYVKML LQLFEKRAVI ANLVRSETIW KAQDQSIGDN AVLENGEFGF GVHLGILAKR
QELKDKVKTV VTDDNAKGIV SQRLLECLVH WFEKQPKHDE LASEITILLE NEQQQSDVLA
EISALKQYFA PLSQWIIGSE EFSRDVGTSG VHQVLASGEN VNLLILDTEP MNAVSKNNRK
RDLGLYAMQY GNAYVASVAL YDSYSQVLRA LNEADAFDGP SIVLAYAPSS SNMEQETKEA
VASGYWPLYR YNPTLEDVEG EKAFSLESPN IKKELLTFLQ RNNQLSLFAK QALTAPTVAS
ATEKYKQIGQ HALKTSFEAL LNGIGGQHQE PWQINTKLWL LVGSDNGHAD EFASKLAEDA
LNFGLKNVEK MDMNEMTIDQ LLDEANDENT YVVFVCSTAG QGEFPSNGKK FWGELSDFSS
TLPLQFAVFG MGDSLYWPRE DEKHYFCKAP ADLDAKLSEL GAKRIVDLAK GDDQDEDGPM
TVFEAWKPQL WEQIGIPVDV VSLHQGTKKK QRTNEEIKKE SNYLRGTLVE GLEDRTTKAL
PADDTQLTKF HGIYQQDDRD LREQMRLEKV EKAFSFMIRV RVPGGVSTAA QYLMVDQLAD
SHANGNIKLS TRQAYQLQGI LKWNLKPVVQ GINQVLMDSL AACGDVNRNV MVTVNPSCSV
ETHQEILNVA RDISAHLSPK TSAYHEIWLD KKMVAGGEVK DFEPFYGEAY LPRKFKIAIA
IPPSNDVDVF ANCLGFIAIL KKDKLVGFNV SVGGGMGMTH NNNKTFPRVG DVMAFCTVDQ
AKDVAEKTMV LQRDFGDRVN RKHARFKYTV EDHGLEWIRT EIEKRLGYKL MDPHKHNLVS
NGDRYGWIKN SNGKYHYGLF VEGGRIKDSK VTSIRTGLRE LAKALPHVEF HLTGNQNLSL
GNIAEEEIPQ IKAFMETYKF GNDNYSGMRL NSIACAALPM CGLAFAEAER YLPSLVTKIE
DILETNGLRD DAIVIRMTGC PNGCARPYLG EIGFVGRSPG IYNMYLGAGF AGDRLNKLYK
EALDEAQILE ELEPIIKDYA ENRNEGEKFG DFVIRADYVK ACLAAPLVEN RAAGETFHA
//
