ID A0A0N1H2L5_9EURO Unreviewed; 836 AA.
AC A0A0N1H2L5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN ORFNames=AB675_4706 {ECO:0000313|EMBL:KPI38935.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI38935.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI38935.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI38935.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI38935.1}.
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DR EMBL; LFJN01000016; KPI38935.1; -; Genomic_DNA.
DR RefSeq; XP_017998898.1; XM_018144865.1.
DR AlphaFoldDB; A0A0N1H2L5; -.
DR STRING; 1664694.A0A0N1H2L5; -.
DR GeneID; 28736744; -.
DR OrthoDB; 1478506at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR PANTHER; PTHR31356:SF53; PEROXIDASE; 1.
DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00141; peroxidase; 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|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|RuleBase:RU363051};
KW Peroxidase {ECO:0000256|RuleBase:RU363051};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW Signal {ECO:0000256|RuleBase:RU363051};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU363051"
FT CHAIN 22..836
FT /note="Peroxidase"
FT /evidence="ECO:0000256|RuleBase:RU363051"
FT /id="PRO_5005873016"
FT TRANSMEM 813..835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 130..397
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 23..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..54
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..88
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..673
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 85823 MW; E15F7D9E80A82927 CRC64;
MVWSNLLVVA AAALQLGSVV AEPPVPSLPA GPGPVAPSAS AGPPPVPPPP PKDTPPKDDS
PKDVPPTDAP APGPESEKPP PTSAPSINPT FPQPWDKLED IMYLNMGYNA EELSQPFTPC
STETNGFNPA AGLLRVAFHD TAQYDAAARV GGLDASIAFE LTGDLGRSNG GPFVVNSLTY
LSRYYSDQVS MSDLIAASVY SAVRGCGGPI VPVRAGRIDA TQAGAPGVPN VLDSLASMTA
GFKRMGFDTQ EMIKLTACGH TMGGVHPQLF GIANPENKSV FHFDATPGGY DNAVVVDIVQ
NKSVDHLFTT GLANSDKKIF TSDNGTTLAS LFKAEVYHHE CQVLLQRMIE LVPGNVQLSE
PIAPYEVKPG VVQLSLSTDG KVLEFSGEVR IRTTTLSLDS IMSVEVIYYD DDGKEVDSIA
TELVGTASGH DDTFAFFGWA AEIDAKAGVS AYTVVITSKD GKALTYDNNG HKYDVEDAIF
IDRPSSHIGK GDAQGNVKVE IVVVTRGEAS SPTLTLTAQS KRDNDDNPLP VLSSTSYPLK
KSSTNGAFTI YVVTFTLKKY QLIAGTFTIT ATVDGKEVKL PYNKFIGFKG HHHPGGHPGH
GNGPGGSGPG GNGTIPGGDG PGSDGPGNDG PGGDGPGSDG PWTDNPGGDG WGGEGPGDGP
DGRPPPPPPK ACTTEAAPCD AQPWATDTTW VVPTPSVHTK PYGGWPTDTP NSPGKPGSGG
SGSGKPGSGH DGHGSGSPGS SGSDGNSEPW TDNGDDSCEE GGEYTSPAKS TWIEWSPAPA
PATNTPYAPT APKPTSTTGG PKPTGVAVYT GGAGANAVVA CSGVFVAAVL GLAALL
//
