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Database: UniProt
Entry: A0A3Q3FDB7_9LABR
LinkDB: A0A3Q3FDB7_9LABR
Original site: A0A3Q3FDB7_9LABR 
ID   A0A3Q3FDB7_9LABR        Unreviewed;       726 AA.
AC   A0A3Q3FDB7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Eosinophil peroxidase-like {ECO:0000313|Ensembl:ENSLBEP00000017514.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000017514.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000017514.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q3FDB7; -.
DR   Ensembl; ENSLBET00000018499.1; ENSLBEP00000017514.1; ENSLBEG00000013385.1.
DR   GeneTree; ENSGT00940000156009; -.
DR   Proteomes; UP000261660; Unplaced.
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   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:SF63; EOSINOPHIL PEROXIDASE; 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:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT   BINDING         461
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   726 AA;  82597 MW;  D68688ABEBE99C53 CRC64;
     RAIEKAVEEA KATVDSAYEY SRKQSIERVR TNAAKPSDVL RLLKQPVGPT RLAVRAADYM
     DNTIKLIKTS LVARQKRSIN ATDLISAEDL QLISDLTGCS AHQRPASCKT VSNLERFRTA
     SSICNNRKNS RRGSSNTPFT RWLPAEYQDE ISLPKGWDLK LKINKQLLPL VRQVSNHILS
     TKNSDVESDP LYTHLVTIFG QWTDHDLTFT PHSPVIRSFS NGIDCDKTCE RTEPCFPIAI
     PTNDIRFVEH SEKCIPFFRS TAACGSGQTG HMFGASTVRQ QMNTLTSFID SGQVYGSDDT
     KAQFLRDLTN DKGLLRVNTA YTDNGRELLP FTNMGANMCA TRARITNDIS LKEVPCFLAG
     DERSNENIGL SSLHTLFMRE HNRLARALAK LNPHWNGERL YQEARKIMGA YFQVITYRDY
     LFHIVGPDVI AKQLSTYPGY DEDVDPSISN VFATAAYRFA HLMVQPFMFR LNETYEEHPE
     YPSPLLHKAF FTPWRILFEG GLDPILRGLV GRRAKLNTQE HMMHDELRER LFEFSKELAL
     DLASLNMQRG RDHGLPGYNE WRKFCGLSQP KNERQLKRVL NNKELAKSLL KLYKTPSNID
     VWVGGVAEPF VKGGRVGPLF ACLVATQFQR IRQGDRLWWE NEGVFNEDQR ESLKQTSLSR
     IICDNTGITK VPDKFGQGSL AEVYHYPRWR VIWTTCRFES HSDCPENSGE CFKAKMESLG
     GTEPKL
//
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