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Database: UniProt
Entry: A0A0N8CRV2_9CRUS
LinkDB: A0A0N8CRV2_9CRUS
Original site: A0A0N8CRV2_9CRUS 
ID   A0A0N8CRV2_9CRUS        Unreviewed;       762 AA.
AC   A0A0N8CRV2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Chorion peroxidase {ECO:0000313|EMBL:JAL98683.1};
DE   SubName: Full=Lactoperoxidase {ECO:0000313|EMBL:KZS13197.1};
GN   ORFNames=APZ42_021642 {ECO:0000313|EMBL:KZS13197.1};
OS   Daphnia magna.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=35525 {ECO:0000313|EMBL:JAL98683.1};
RN   [1] {ECO:0000313|EMBL:JAL98683.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gilbert D., Podicheti R., Orsini L., Colbourne J., Pfrender M.;
RT   "Daphnia magna gene sets from two clonal populations assembled and
RT   annotated with EvidentialGene.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAL98683.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KZS13197.1, ECO:0000313|Proteomes:UP000076858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xinb3 {ECO:0000313|EMBL:KZS13197.1,
RC   ECO:0000313|Proteomes:UP000076858};
RC   TISSUE=Complete organism {ECO:0000313|EMBL:KZS13197.1};
RA   Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT   "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GDIP01105031; JAL98683.1; -; Transcribed_RNA.
DR   EMBL; GDIP01072895; JAM30820.1; -; Transcribed_RNA.
DR   EMBL; LRGB01001253; KZS13197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N8CRV2; -.
DR   STRING; 35525.A0A0N8CRV2; -.
DR   Proteomes; UP000076858; 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:SF115; GH11385P; 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:JAL98683.1};
KW   Peroxidase {ECO:0000313|EMBL:JAL98683.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076858};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..762
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013460451"
FT   BINDING         514
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   762 AA;  86536 MW;  CBF54437D6934783 CRC64;
     MVKRRPFLSC IPLFLISLID SIQSNSHRNN RQIHFDSEET IGRSLFRPFS QEVALLGNRT
     GFDIRFITNE QLDKEVSQAS DRMNDIIHFE EVLLENEIRI QPNTPSFSHL KIVQPSIGAQ
     QLAREALLVI EATLRLQKRF NLTPEETGLG LTIHSIRQTI TFPACRSRPP CMEHFGTGIV
     KYRTIDGSCN NLEQTSWGMT RSTFQRILPP AYSDGVFAPR VATDGSNLPS ARLVSLSIVS
     HHDAPRVDLS LLGMVFGQFV DHDLTFTPTF VLSDSSGIEC CTTDGGAMLP DGLRHPQCFS
     IDIPADDPFY RPFNQRCMNF VRTTPGLRPD CNFGYAEQLN ELTHWLDGSQ IYGSDAETLE
     KLREFRQGRL RSARINGQEI VPLDPKSNIT QPEDCNTSSC YMAGDIRLSE QPQLTVMHTL
     WLREHNRIAA ELSRFNPDWN DEIVFQETRR IVIAEYQFII YNEFLPIILG KRYMDMFNLT
     LSQPSYYNDA NKYDATIDPS IHNEFATAAY RMGHSLIQGL VKLFSQNGQV NEDRSFSLSS
     MLDTASPFGK EAAWMDEALR GLLEQPMQNF DSSFTPEVTN KLFRGGKSFG LDLVALNIQR
     GRDHGLPGYN SYREICGMKR ADHFRGFSPQ ISPDMISQLK HIYRSVDDVD LFVGGILETP
     VHDSLVGPTF LCIIGDQFAR LRKADRFFYD INHQLHSFNQ RQIDEIRKAS LARIICDHND
     GTIHMIQPQV FRTAGGINSK KRCDGPAIPR PDFSLWAGEP IF
//
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