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Database: UniProt
Entry: A0A2T7P9G8_POMCA
LinkDB: A0A2T7P9G8_POMCA
Original site: A0A2T7P9G8_POMCA 
ID   A0A2T7P9G8_POMCA        Unreviewed;       817 AA.
AC   A0A2T7P9G8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Peroxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C0Q70_09323 {ECO:0000313|EMBL:PVD30062.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD30062.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD30062.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD30062.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD30062.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:PVD30062.1}.
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DR   EMBL; PZQS01000005; PVD30062.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7P9G8; -.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg5.
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   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR11475:SF4; LD42267P; 1.
DR   PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00090; TSP_1; 3.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SMART; SM00209; TSP1; 3.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 2.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   PROSITE; PS50092; TSP1; 3.
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:UP000245119}.
FT   REGION          730..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         425
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   817 AA;  91751 MW;  DEA7B66698231DF8 CRC64;
     MSLTAASVEQ LMQQVIVYNK QGDAQPLGPL YQSGFPSVFT TVSPITTTPA PNSPESNLRC
     QSSVELKCDP ELKFRTPDGT CNNLVHNLWG SALSPLRRIL QPQYGDGEWL ELIGTRVSSV
     MLSALSVSAP RTTSTHSRNP LPSARAISVL IHPSGPGNLM TSLTHMVMQW GQYLDHDITS
     TPIQTGELKS NITYYTHDYT SKTILYWFIF LFHRTACFPI PIPSYDPYFK GRSCFSFTRS
     LQVTNSNCKQ VPVEQLNQLT AYVDASQVYG SSAEEQKNLR TFKGGQMTTS GNDLLPKDKA
     ESCVLNNPNR DYCFKAGDLR VNEQMGLASM HTVWMREHNR LVQKMAAVNP HWNDERLFQE
     TRKIVGALYQ KITYGDWLPI VLDRNRFAAN NLQLLPSGQQ SNIYNPSVDA GVKNVFASAA
     FRFGHSLIRS TMSQYAKYVF IYFYLNETFQ MSTSTVIVTL VVTKKVDRFF TEEIKNHLFQ
     DKRGNSLDLV AFNIQRGRDH GLPPYNEWRK YCKLPVMTSF SNMPDHDELT GQAFSQIYEH
     PDDIDLFSGA ISERPEGNGL VGPTFACILS EQFRNLKFGD RFWFETRDPV TGFSLEQLEE
     IRRHSLARVI CANTGGGHIQ GNPFVQPSDS NPMVNCNDLP DMTMEPWREV QGRARVGTWT
     EWGEWSACDQ GMQLRQRACS QYGECAGNYQ DSQPCASPGW TSQWSQWSPW STCFQGLQAR
     SRACSGQPAT GFGSPCPGGP QETRPCSSGT VGWAQWGPWG TVCSQGRQWR ERTCTRSPNQ
     VGVCSGPSSQ SKPCTPPWNY PWNNNGNPQT GPYNTYG
//
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