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Database: UniProt
Entry: A0A0V0XYL9_TRIPS
LinkDB: A0A0V0XYL9_TRIPS
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ID   A0A0V0XYL9_TRIPS        Unreviewed;       494 AA.
AC   A0A0V0XYL9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A {ECO:0000313|EMBL:KRX92880.1};
DE   Flags: Fragment;
GN   Name=PDE7A {ECO:0000313|EMBL:KRX92880.1};
GN   ORFNames=T4E_85 {ECO:0000313|EMBL:KRX92880.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX92880.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX92880.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX92880.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KRX92880.1}.
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DR   EMBL; JYDU01000100; KRX92880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0XYL9; -.
DR   Proteomes; UP000054815; Unassembled WGS sequence.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   PANTHER; PTHR11347:SF198; CAMP-SPECIFIC 3',5'-CAMP PHOSPHODIESTERASE 4; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR623088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..494
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006872833"
FT   DOMAIN          115..445
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   ACT_SITE        190
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         190..194
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         231
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         349
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         400
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX92880.1"
SQ   SEQUENCE   494 AA;  56402 MW;  7FE19B8C74689FB7 CRC64;
     LISCCAILFS LLIKAVLKSS NKSSFVVMFP FAATPSLHIA ITQPSCCNKQ FSVDVAQVLD
     QHQRSRSSSN VQDQIKDTSL FIHSIKLVKS STSAMSLVFH PSSADRSPAR SVHYVEMNPT
     SSLECLLRRC AHWNFDVFLL NRLSDGHPIM ALGCKLFKWY DFASVFHFDW MAVFKCLRLI
     ESGYYNNPYH TAVHAADVAQ ALHCFIQTFD LSHAYSHLDL FIALIAAFGH DVYHPGVNSQ
     FLENSNHYLY QIYQNCSVLE NFHWRCLLAI LHECGLALFF TSSEWNYICE TLGALILSTD
     IRRQNEYLTD LKVNFFNSNF LSGDDNGELL LQKRESRIAC LQMLLKCADV SNCGRELRHS
     RLWALRVSAE LYSQGEKEKQ LGIKVSEHCD SSITSVPLIQ IKFADHVVLP LYNELKKFSN
     CSLTARILKH IHSNRHYWLR TLNGDTDTLT DTAKRFCLLA IKKQRLRSHL VYLDENCLLY
     PPDGKSVLRN LALQ
//
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