ID A0A226E559_FOLCA Unreviewed; 707 AA.
AC A0A226E559;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Chorion peroxidase {ECO:0000313|EMBL:OXA52569.1};
GN ORFNames=Fcan01_11990 {ECO:0000313|EMBL:OXA52569.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA52569.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA52569.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA52569.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA52569.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:OXA52569.1}.
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DR EMBL; LNIX01000006; OXA52569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226E559; -.
DR OMA; RYFFTHN; -.
DR OrthoDB; 2959589at2759; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09823; peroxinectin_like; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR PANTHER; PTHR11475:SF106; CURLY SU; 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000313|EMBL:OXA52569.1};
KW Peroxidase {ECO:0000313|EMBL:OXA52569.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287}.
FT BINDING 464
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 707 AA; 78930 MW; 7A5AB5BD1332DBD0 CRC64;
MFNAFLDTCL VCFKMSSSVV TVVCLVLGTL CLVRADFSIQ VEPQPEPDVG TPFIDFNNLA
KKNETADPFG QISLNYQSLW KRAADIYEEH VVQQFQNGST SRPCRAAKCN EFSNEYDKNS
NIFEIYATIV KDKHNITKRQ AVGGNTPGMC TNPSTSHCPN FVNSRFRTVD GTCNNVNNPA
WGASNRQFNR LLQPAYEDGF DAPRGGFNSR LQNPRVISTT VHPDNPSIVN RRITNMVPQF
GQFLDHDLTL TMEAGSQCCA NPNSNPANCW PIFVGNDAFF SRFTQCLDFT RSTPCQSNGQ
RQQMSGNTAF IDAGQIYGSN PTRSNQLRTF SGGMLRANTN LRGFLPTSNS LGIQVQGDFV
AGDDRINEMP ALAVMHNVWL MEHNRIATQF QRISTWNDER IYQETRRIVI AEFQQVVYSE
YLPIVLGAAT NEYNLGVSTW STYGANIDPT IINEFATAAY RYGHSMVIGL VQMLNSQDQL
VDSYQVANEY FQSRQITRDN GQGYDMILRG LMRQNSPEMD RFVTTGVTQF LFKPQNQNFG
SDLVARNIQR GRDHGVRSYN DYRMGCGGSD LSTATWSVVP AGINPDGWTQ CSRVYQRPID
IDLFVGGLIE TPYNGALTGQ TFTCLMGTQF TRTKHGDRYF FTHNLPTGFT GAQLTELTRR
RLSDIICENS QQPNSPANVF LVEGTGNPVI ACGAGSGRPV LNLNLYL
//
