ID A0A2V3INY7_9FLOR Unreviewed; 541 AA.
AC A0A2V3INY7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=Lactoperoxidase {ECO:0000313|EMBL:PXF43773.1};
GN ORFNames=BWQ96_06466 {ECO:0000313|EMBL:PXF43773.1};
OS Gracilariopsis chorda.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Gracilariopsis.
OX NCBI_TaxID=448386 {ECO:0000313|EMBL:PXF43773.1, ECO:0000313|Proteomes:UP000247409};
RN [1] {ECO:0000313|EMBL:PXF43773.1, ECO:0000313|Proteomes:UP000247409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKKU-2015 {ECO:0000313|EMBL:PXF43773.1,
RC ECO:0000313|Proteomes:UP000247409};
RC TISSUE=Whole body {ECO:0000313|EMBL:PXF43773.1};
RX PubMed=29688518; DOI=10.1093/molbev/msy081;
RA Lee J., Yang E.C., Graf L., Yang J.H., Qiu H., Zel Zion U., Chan C.X.,
RA Stephens T.G., Weber A.P.M., Boo G.H., Boo S.M., Kim K.M., Shin Y.,
RA Jung M., Lee S.J., Yim H.S., Lee J.H., Bhattacharya D., Yoon H.S.;
RT "Analysis of the draft genome of the red seaweed Gracilariopsis chorda
RT provides insights into genome size evolution in Rhodophyta.";
RL Mol. Biol. Evol. 0:0-0(2018).
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:PXF43773.1}.
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DR EMBL; NBIV01000111; PXF43773.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3INY7; -.
DR Proteomes; UP000247409; 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 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:SF4; LD42267P; 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:PXF43773.1};
KW Peroxidase {ECO:0000313|EMBL:PXF43773.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247409};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..541
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015971485"
FT BINDING 318
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 541 AA; 61111 MW; 425A5117C5C24692 CRC64;
MIKLIAILLI TAFATTALAQ APRRIGIGSS SLSSRGPRRR AARIAVSPEC VGITTRTITG
FCTNDADPTL GESRRAQASY FNVSTQQPAD QNLPSPRLVS NIVSAQEGPT ENSHGLNEMF
TFFVPTGDPE LSVASLEFIR SERERVDQTS PVERPITVLT SALDLSTVYG SEEDRNRVLR
VPNSCLLKTS RDAVSGAELL PRNTKGFVNV PTITDEFFIA GDARANETPM LTAMHTIWVR
EHNRLCRVLD ERFPNADSVQ QYETARAINI AQYQKIIYKE WLPAILGPLN LRPYPGYLRS
VDPTVSIEFT TAGFRLGHTL VSGNVRRMNG RGMVLPPIPA EEMFFVKSDE VPSRLISQLL
RAASVFRAQE FDEKVVDTLR NFLFENVEEE EGFDLVALNL QRSRDHNVPK YNDLREFFRG
TRASSFRDIS RNRETMDKLR RAYGTVDNVE AWIGLVSESK ALGAGVGRTL GQLLRREFER
LRNGDQFFYE RRNTIRPEVF QQLSTLETEL FHDDFLFNRI LLRNTPISVQ TLDRRSNAFL
V
//
