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
//