ID A0A1Q3EQQ7_LENED Unreviewed; 774 AA.
AC A0A1Q3EQQ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=LENED_011694 {ECO:0000313|EMBL:GAW09533.1};
OS Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX NCBI_TaxID=5353 {ECO:0000313|EMBL:GAW09533.1, ECO:0000313|Proteomes:UP000188533};
RN [1] {ECO:0000313|EMBL:GAW09533.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW09533.1,
RC ECO:0000313|Proteomes:UP000188533};
RG Lentinula edodes genome sequencing consortium;
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAW09533.1, ECO:0000313|Proteomes:UP000188533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 111202 {ECO:0000313|EMBL:GAW09533.1,
RC ECO:0000313|Proteomes:UP000188533};
RA Sakamoto Y., Nakade K., Sato S., Yoshida Y., Miyazaki K., Natsume S.,
RA Konno N.;
RT "A genome survey and senescence transcriptome analysis in Lentinula
RT edodes.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peroxidase family.
CC {ECO:0000256|RuleBase:RU004241}.
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:GAW09533.1}.
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DR EMBL; BDGU01001114; GAW09533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3EQQ7; -.
DR STRING; 5353.A0A1Q3EQQ7; -.
DR Proteomes; UP000188533; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.20.1280.290; -; 1.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR006603; PQ-loop_rpt.
DR PANTHER; PTHR14856; PQ-LOOP REPEAT-CONTAINING PROTEIN 1-LIKE PROTEIN; 1.
DR PANTHER; PTHR14856:SF9; SCRAMBLASE ANY1; 1.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF04193; PQ-loop; 1.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363051};
KW Peroxidase {ECO:0000256|RuleBase:RU363051};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 559..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 629..652
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 658..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..711
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..281
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
SQ SEQUENCE 774 AA; 85832 MW; A7850100CC6260C4 CRC64;
MKLNANYPKL SYMVYSFPLL YSRVNIILTL IGYAHSFSTF QWPNPQLRYA DNQLYEGSMG
ILVQDCPSRE NTTIPAQWLR IAYHDMSTHD IDDGSGGLDA SIQYELDRPQ NIGQGMIDSL
NDFKAFRIAT PFFGMADTIA LGAVFAVAGC GGPLIPFSAG RVDATEPGPE TVPEPQQDLA
SHTEAFRRQG FSPTEMIGLV ACGHTLGGVR QVDFPLIVTD TEDVVQSFDT TINFDNAVVS
EYLQNTTQNI LVVGPNVTTR SDFRIFASDG NVTMQSFLSS DTFAETCKDL IGRMINTVPN
GVTLTQPISE PFDYVVSEPL FSYRNGTLSM ATTLRVMTEN PSRTVTMLWV DRQGSSCPPI
GCTSPSISTQ QVVFSLIGNL QGLTGTRYSF NATINASTSI SKFWFEINEN DGSDPIVVDN
GGSGFVIEQD SMFIDNSRSE NVLLSSSFNE YRKVVVAVRG DTSSSVSITT FDPNSDASAP
PYLLTVITTN LQLDDSNPSE GGFTFFTVNI SETVNFVSIS GNIGGVSYVQ ENFDMTVAWQ
WDLHWFMPTK PIPLDSTGFS RDVCAILLIA NITRCFFWLG DRFELALLVQ SVLMILAQLA
LLYICIIYRP RIGPENLGNS NRLYSFWQWS SYTQYIEFLA GLILCQAILF LIFGRSRVFI
TLLGFFALGL ESTLPIPQLI SNYKQRSLYG FRMSTLIGWL GGDSFKTVYF FLQNSPLQFK
VCAIFQLSID FAILGQRRKS HDKFPRVYSE SSLSNEQSVS LPKVGGRGID LFPD
//
