ID A0A2V3IE98_9FLOR Unreviewed; 564 AA.
AC A0A2V3IE98;
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=Peroxinectin A {ECO:0000313|EMBL:PXF40415.1};
GN ORFNames=BWQ96_09875 {ECO:0000313|EMBL:PXF40415.1};
OS Gracilariopsis chorda.
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC Gracilariaceae; Gracilariopsis.
OX NCBI_TaxID=448386 {ECO:0000313|EMBL:PXF40415.1, ECO:0000313|Proteomes:UP000247409};
RN [1] {ECO:0000313|EMBL:PXF40415.1, ECO:0000313|Proteomes:UP000247409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKKU-2015 {ECO:0000313|EMBL:PXF40415.1,
RC ECO:0000313|Proteomes:UP000247409};
RC TISSUE=Whole body {ECO:0000313|EMBL:PXF40415.1};
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:PXF40415.1}.
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DR EMBL; NBIV01000298; PXF40415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3IE98; -.
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: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: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 Reference proteome {ECO:0000313|Proteomes:UP000247409};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..564
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016025814"
FT BINDING 341
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 564 AA; 64333 MW; C1912A3117307300 CRC64;
MTSPPLFFHF CVFFFLVSGV YAQAPRPNGR DNTALTPLSE DDADLPVQQL AQCNQTHFRT
YDGSCNNLRN PLWAAAGTAQ FTYHPSHTST TALGSRLPSA RLLSNILSSQ SSDLLNNRFV
SEFTVFFGQF LDHTIVATPV NQSESMPIPI PHADPIFSNF SKGTLPFHRS VRAALPDAPH
LERPINSLSS LIDLSSVYGA DDLRTNVLRS FSKGEIRTSP KGMLQLNTQR LRNAPSNQPH
FFLAGDHRAN EHPMLTALHI LFVREHNRIC RELKAQYPRW DDERLFQNAR HINIAQFQKV
VYEEFIPAMT GRYVGRYYGY LPNVNPTVSL IFSTAAYRVG HTMVGNSIHR LGKGLRNMPS
FQFTSMFFRP STVMNEGIEP FLRGSLYHRA QEVDLSVHDA LRNFLFTGIP QESGVDLVAL
NIQRGRDHAL PTYNKVRQLM GRRPARTFAD ISRDPAVQSK LATAYGTVNK VELWPGLVAE
DHVHRASMGP TMLRIWHTEF ARLRDGDRFY YRRWQAFPLH MWWRVPSLRR FVYSRRSTMR
EILIQNTGIA SWEVPRNPFF SGGL
//
