ID A0A094EIJ5_9PEZI Unreviewed; 966 AA.
AC A0A094EIJ5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=V499_08329 {ECO:0000313|EMBL:KFY71495.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY71495.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY71495.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY71495.1,
RC ECO:0000313|Proteomes:UP000029295};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:KFY71495.1}.
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DR EMBL; JPKB01001301; KFY71495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EIJ5; -.
DR HOGENOM; CLU_011078_0_0_1; -.
DR Proteomes; UP000029295; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0031179; P:peptide modification; IEA:InterPro.
DR CDD; cd04794; euk_LANCL; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 3.30.465.10; -; 2.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR007822; LANC-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF05147; LANC_like; 1.
DR PRINTS; PR01950; LANCSUPER.
DR SMART; SM01260; LANC_like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF158745; LanC-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 514..692
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 966 AA; 105474 MW; BF21B1FA1F21CFBB CRC64;
MEEILYISND IPTQALRSPP SELLQSCLEQ ILQTLPPKES YNEEQASGFF MGYTGLAFLF
FQISALRPGL EILGHDLIYW AKRYMEGKRT GIECFIVNKE QGCGLLNERL CFQALWACLS
KEHGDVLAFL SDMPAVLGPY PTDQGDPYET ELLYGRTGAL YLLRMLRHWV PASASSLEEP
IAKLAGKIMD TDSDGKGNWE WNGDRRYGPP HGDIGIITQL VLTLPSLAPK LSAKVEELLS
LQGPDGNWPS SRDTMETEKG WERVQYCHGA PGFVCALQTL RPFYPELHGR IDQAIARGRE
TTWSRGLLKK EPNLCHGILG NAFAFPIGPK REHFLALCTP DEIEKAKECD PKVFGAAAYG
MEVMVALQYL PSAAWTWAVC DMPIPPMLMF NDVFNLVGAG ALVLTLAPLP AIADFPAFPT
VLKVWCRSLP GDDSWPTVSQ WKNLNSSVGG RLIKTYPLGS VCHDPAYDAA KCASLQTAWT
DAQLHMESSS SVMAPFFANQ SCDPWTPTLR PCTLGNYVSY SVNATSADDI IEAVNFAQEH
NIRLVIRNTG HDYSGKSIGA GALAVWTHHL KSTQVLDWKD SYYDGKAIKM GAGVQGFEAM
AAAKAEGLVS IGGECPTVGV AGGYTQGGGH SALSTSFGLG ADQTLSFEVV TSKGHLVTAS
RTQNSDLYWA LSGGGGGTYG IVVSMTAKAY PDAIVGGATL IFQSSSTTAD NFYAGVEKFH
SLLPAMVDSG SMIVYFFDDT FFQIGPLTAY NKTSTEVKSV LSDFVEALDE LQIPYNVSYS
QSATYTDHYN TYFGPLPYGN IKVGIAQYGG RLIPRATIQN NNAAFMKMAR NITQDGVLFI
GVGTDVSAPA EMVSNSVLPA WRNTLIHATI TTPWNFTAPW AGMIALQDKM TDSIQPQIEA
VTPGSGAYMN EADFRQPDYK EAFFGSNYPK LLKIKDKWDG DYLFYAIKSV GSDHWNVAAD
GRMCRA
//