ID A0A232F1P3_9HYME Unreviewed; 664 AA.
AC A0A232F1P3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Chorion peroxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=TSAR_006149 {ECO:0000313|EMBL:OXU24635.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU24635.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU24635.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU24635.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU24635.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
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:OXU24635.1}.
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DR EMBL; NNAY01001240; OXU24635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232F1P3; -.
DR STRING; 543379.A0A232F1P3; -.
DR Proteomes; UP000215335; 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:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000215335}.
FT BINDING 399
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 664 AA; 75634 MW; E7737F5AC5D91489 CRC64;
MPKNEKWRPE DLASVGELLL DISVNLARTY GLTTQQIEKY LPQIDTSKTL IRDVCPAFLS
TVECRPGKYR RFDGLCTNLE HPTWGASLSP FVRLLSPRFS DGMNAPRIAS SGNDLPLSRV
VSRTMHPDEG FHDHAGTVMV IAWGQFMDHD YTLTATPLDA MNRNDPEECC NRAPQDKNPY
CNEIQIPEDD YFFRLFNVRC MDFVRAFPGV RPGCRLGSRV PYNLLTGVLD GNTVYGISDE
FANKLRTGYA GLLRMNPVFE EYGLKDLLPL KLDIPDEGCT RPNRSMYCFE AGEIRVNEQL
VLTCMHTLMA REHNRVAKGL AQVNPHWDDE TLFQEARRIV IAEIQHITYN EFLPILLGKD
VMQKFGLLLE KDGYWDGFDP NVNPGVIDAF AAAAFRFGHS LLPTAVERWS KAHKFIASKR
LSDLIRRPFD LYRAGVFDEY FMGLMNQVAQ AMDDSITQEV TNHLFKKVGA KHGMDLVSFN
MQRGREFGIP GYMEFRKFCG LPGAETFEEL FGSMPNETVR RYLSIFEHPA DVDLWSGGVS
ERPLPESMLG PTFACIIATQ FSNSRRGDRF WYELPNQPSS FTPEQLQEVR KTKLARVICD
NTDLIDTIQI YPMVLPDHEI NPRVPCKSGI LPSIDFSKWA EFPQQAYAQD YANDYSGQYG
QFVK
//
