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Database: UniProt
Entry: A0A2J6QHH9_9HELO
LinkDB: A0A2J6QHH9_9HELO
Original site: A0A2J6QHH9_9HELO 
ID   A0A2J6QHH9_9HELO        Unreviewed;       492 AA.
AC   A0A2J6QHH9;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PMD25721.1};
GN   ORFNames=NA56DRAFT_676874 {ECO:0000313|EMBL:PMD25721.1};
OS   Hyaloscypha hepaticicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX   NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD25721.1, ECO:0000313|Proteomes:UP000235672};
RN   [1] {ECO:0000313|EMBL:PMD25721.1, ECO:0000313|Proteomes:UP000235672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD25721.1,
RC   ECO:0000313|Proteomes:UP000235672};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC       {ECO:0000256|RuleBase:RU362121}.
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DR   EMBL; KZ613469; PMD25721.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6QHH9; -.
DR   STRING; 1745343.A0A2J6QHH9; -.
DR   OrthoDB; 1887365at2759; -.
DR   Proteomes; UP000235672; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02922; FCB2_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
DR   InterPro; IPR037458; L-MDH/L-LDH_FMN-bd.
DR   PANTHER; PTHR10578:SF149; L-LACTATE DEHYDROGENASE (CYTOCHROME); 1.
DR   PANTHER; PTHR10578; S -2-HYDROXY-ACID OXIDASE-RELATED; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU362121};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU362121};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362121};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT   DOMAIN          1..77
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50255"
FT   DOMAIN          103..463
FT                   /note="FMN hydroxy acid dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51349"
FT   REGION          273..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   492 AA;  55049 MW;  46EBC5E412EB819F CRC64;
     MALTGEEIAK HNSRESCWVI VHGKAYDVTE FLPEHPGGPK IILKYAGKDA TEEFEPIHPP
     DTLDKYLDQS KHLGEVDMST IEKEAKEESP EEKERQDRIA RMPILEQCYN LMDFEAVARN
     VMKKSAWAYY SSGADDEITM RENHSAFHKI WFRPRILVDV EKVDFTTTML GTKCDIPFYV
     TATALGKLGH PEGEVVFTRA AKKHNVIQMI PTLASCSFDE IMDAAEGDQV QWMQLYVNKD
     REITKKIVQH AEKRGCKGLF ITVDAPQLGR REKDMRSKFT DSGSNVQAGS KTDNSQGAAR
     AISSFIDPAL SWKDIPWFKS ITKMPIILKG VQRVEDVIRA IETGVQGVVL SNHGGRQLDF
     ARSGIEVLAE VMPVLRERGW ENRIEIYIDG GVRRATDIIK ALCLGAKGVG IGRPFLFAMS
     AYGQPGVDRA MQLLKDEMEM NMRLIGCSSV DQLNPTLVDT RGLSMHTTSV PVDTLGLTTY
     DPLISPKEKA KL
//
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