ID A0A423X0X2_9PEZI Unreviewed; 1548 AA.
AC A0A423X0X2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Flavodoxin-like domain-containing protein {ECO:0000259|PROSITE:PS50902};
GN ORFNames=VMCG_02360 {ECO:0000313|EMBL:ROW09495.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROW09495.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROW09495.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROW09495.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) 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:ROW09495.1}.
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DR EMBL; LKEA01000004; ROW09495.1; -; Genomic_DNA.
DR STRING; 356882.A0A423X0X2; -.
DR Proteomes; UP000283895; 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:UP000283895}.
FT DOMAIN 809..958
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT REGION 266..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1548 AA; 171374 MW; 4069E19328586473 CRC64;
MSFLFKHLPT LDITNKQEMA STTGTTGIRT PAEAVARIAY QASDVIVSVQ PSLAVDSVFS
SHLKTYHGRK DESLVAKNKV PELLSVRYNA DPLLSVFEPA RNGQLVSVTT TSRILLPSVG
HLYKLANYPV VIHVALHPEQ FPDYSAITSI RNSGWTFLQS ESIQEAQDMA LTAHALAIRS
GKGVIHFFSS AACKDDEPVA FETQQVVKDV LNQDQVRRVQ DSKIEGAGIY ADDGRVAREE
LPESSQVATS AQSPVVNGLT VPEVEGKVSS HASEKSSEQS ATSSPPSVSS ATTIEAQPPV
VTSEHIYNYI TAIWAQLKEL VGREYHVFEY SGSQTAETCL FIFGSDAGLF ADTIDRAPSS
EGFANCAIIT PRLYRPWLGI KLLDILPKSV KKVAVLEQVS RKTTKWGPIL IDALTSLKSG
MGGVETIVGY QLGYINQETV QQALRGIYQN LVSDKPIQNL EVGSQQGPEE SPDYTLKAPK
LETAYSKILD QLFGSRVFLA NSIKSENAGV STTVAASPEY GFGSLLARKE KRQNFVADVK
EAVVSGTDLA EAPKQSLAQW SANAEDASKV EQYAEDVVSA LEADNSSLSQ KFLTNKAFFR
KESLWLVGSD AWSYDLGNSG VHHVLASGEN VNMLIIDSTP YSERAAADAT RRKKDIGLYA
MNFGNAYVAS TAVYSSYTQV LQAMDEADKF DGPSIVMAYL PYNGENDSPL TVLQETKQAV
DIGYWPLYRW NPKNELKGEP NFSLDSERVK KELKQFLDRD NHLTQLMAKE PKFAPVLSED
FGTEIRAQQK RNAKDAYNKL LEGLQGAPLT VLFASDNGNA ESVAKRLGNR GKARGLKTTV
MAMEDYPIED LPTEDNIVFI TSTAGQGEFP QNGLSFWHTV KDSTDLDLAT VNYSVFGLGD
SHYWPRKEDK VYYNKPGKDL DRKLADFGGK RLAEVGLGDD QDPDGYSTGY NDWEPKIWQA
LGVDNVEGLP DEPPPITNED IKLESNYLRG TILEGLKDTS TGAISAADQQ LTKFHGTYMQ
DDRDVRDERK AQGLEPAYSF MIRCRLPSGV STPKQWIQMD DIANTLGNET MKLTTRQTFQ
FHGIVKGKLK PAMQAINRAL MTTIAACGDV NRNVMCSSLP TQSKFHKEVH ACSQLISDHL
LPSTHAYHEI WLTDDDDKKT QVAGDAVQDF EPLYGPTYLP RKFKITIAVP PHNDTDVYAH
DVGLIAIKGE DGNLAGFNLL VGGGMGTTHN NKKTYPQTGR MLGYVAKEDV HIACEKVMLV
QRDHGDRKNR KHARLKYTVD DMTVEGYKAK VEEYWGKQFE APRPFKFESN VDTFGWLKDE
TGMNHFTFFI ENGRIEDTAD FQMKTGLREI AKAHKGEFRL TGNQHLILSN VADEDLDDMK
ALMKKYKLDN IKFSGLRLSS SACVAFPTCG LAMAESERYL PVLISKLEDC LEENGLRQDS
IVMRMTGCPN GCARPWLAEV AFVGKAYGAY NMYLGGGYHG QRLNKLFRSS IKEEEILGIM
KPLLKQYSLE REEGERFGDF CIRKGVIKAT TDGTNFHADV AEEESDEE
//
