ID A0A0V1LMS2_9BILA Unreviewed; 902 AA.
AC A0A0V1LMS2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=pde-4 {ECO:0000313|EMBL:KRZ60794.1};
GN ORFNames=T02_10325 {ECO:0000313|EMBL:KRZ60794.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ60794.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ60794.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ60794.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|RuleBase:RU363067};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions, while site 2 has a preference for
CC magnesium and/or manganese ions. {ECO:0000256|RuleBase:RU363067};
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|ARBA:ARBA00007648, ECO:0000256|RuleBase:RU363067}.
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:KRZ60794.1}.
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DR EMBL; JYDW01000025; KRZ60794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1LMS2; -.
DR STRING; 6335.A0A0V1LMS2; -.
DR Proteomes; UP000054721; 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:0009966; P:regulation of signal transduction; IEA:UniProt.
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; IPR040844; PDE4_UCR.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR PANTHER; PTHR11347:SF219; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE, ISOFORM I; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF18100; PDE4_UCR; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW cAMP {ECO:0000256|ARBA:ARBA00023149};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721}.
FT DOMAIN 558..890
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 94..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 637
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 637..641
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 641
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 678
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 678
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 795
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 795
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 846
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 902 AA; 99598 MW; 8ACE97E2FFA62ECB CRC64;
MEVPDIVVTF KQGDEDSTSL DVVFEADSTS PTQTAGSLSV DDTARDGGDP LLVKPFLTAS
SGPALPLRRH SDVLPSSYGS FYLLNRRIKS LKVSNSDQGS SKPSLPSSHD QSSFDVNKKT
GVEAGTLPSG STHPHHRRGS FLYRIDSDAE LTHSTPRVSD SHGCCVCYRL VKWHRVEQEN
VNRRNSALAN VDSQEKAVCC AQPQAVTLVS SCSGRKPTAK QMQSASMHCQ QQLLSMSTVE
PADVDPRNYN SGIKDSGNSR QPDESFPLEQ DDQQQQLVVT VPLLVRRTLS TSALYKIDRC
RLKSLFWKKM HGEDLIVTPF AQVLASLRNV RSNLAKLTRS SSSRTSLAQI SGSVPGTTSQ
SSSASSANHI STAAAAAAAA ATGSDRATAN KQSSGVALPP PAPKSPGSMA TQLATSQEDN
FQLAADTLVE LDWCLEQLET IQTHRSVSEM ASSKFRKMLT KELSQFSDSK SGDQVSRFIF
TTFMGNEHEL DMANEKDKHA PILESDEERS TLVAGGKVGK GKQHVTSSMS QISGIRKLRL
PTATTVSSVD ESTGDLLPIC GLGKEASSEL TSHLNQIDRW GIDIFKVDEL SRNHSLTTIT
FTILKNRGLL KAFNIRPARL LTYLLHLEDH YRKNSYHNSL HAADVTQTVH VMLSTPSLES
VFTDLEKLAV IFAAAIHDVD HPGLTNQFLV NSGSELAIMY NDESVLEQHH LAVAFKLLQE
TDCDILTGFS KKHRQLFRRI VIDTVLATDM SKHMSLLADL KTMVETKKVS GPGVPSLEKY
SDRIQVLQNM IHIADLSNPA KPITLYQQWI DRLLEEYWKQ GDRERELGLE ISPMCDRRNV
SREKSQVGFI DYIVHPLMET WADLVYPEGQ AVLDQLEENR DWLFKKLSAT EREALPPSED
QE
//
