ID B3RT43_TRIAD Unreviewed; 743 AA.
AC B3RT43;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=3',5'-cyclic-AMP phosphodiesterase {ECO:0000256|ARBA:ARBA00012276};
DE EC=3.1.4.53 {ECO:0000256|ARBA:ARBA00012276};
GN ORFNames=TRIADDRAFT_54830 {ECO:0000313|EMBL:EDV26628.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV26628.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV26628.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV26628.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004703}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE8 subfamily. {ECO:0000256|ARBA:ARBA00006437}.
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DR EMBL; DS985243; EDV26628.1; -; Genomic_DNA.
DR RefSeq; XP_002110624.1; XM_002110588.1.
DR AlphaFoldDB; B3RT43; -.
DR STRING; 10228.B3RT43; -.
DR EnsemblMetazoa; TriadT54830; TriadP54830; TriadG54830.
DR GeneID; 6751837; -.
DR KEGG; tad:TRIADDRAFT_54830; -.
DR CTD; 6751837; -.
DR eggNOG; KOG1229; Eukaryota.
DR HOGENOM; CLU_005940_4_2_1; -.
DR InParanoid; B3RT43; -.
DR OMA; RWCCGGS; -.
DR OrthoDB; 5479253at2759; -.
DR PhylomeDB; B3RT43; -.
DR UniPathway; UPA00762; UER00747.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00077; HDc; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF206; HIGH AFFINITY CAMP-SPECIFIC AND IBMX-INSENSITIVE 3',5'-CYCLIC PHOSPHODIESTERASE 8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50112; PAS; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT DOMAIN 143..188
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 358..704
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 445
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 445..449
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 486
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 486
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 610
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 610
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 662
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 743 AA; 84961 MW; EC0E7F9C3854663E CRC64;
MGERKQYRMI LAIFSENDKQ LNALKQAAEK GNYKLNVVHS ERSAIEYYQD YRPHIVFVDL
RSKDAFNGET ICKNVKDKSL SNQSTMIAVV NPSNSDKEEP SIAPLLAMGF NRRFVENFNV
GGCLNELIML EVNDLRQQVK IREADSLFAA IHNAYDSVEI TTDRSQFQYV NPAFERTTGY
WSSELIGKLD SVLPTSDKND PELFNTIKSY VSRGRTWEGS YVGKRKSGET YPQFVRVIPI
IGHEGFLTHH VTIKRDISEM ETKYKKYVEE SIKSYPNGKV VDPNHIKTVE ASTSMVINLI
KIAQENVSES PNNVTQSLDK VLQILKDAEI SFPQGADFDL INFTELGNNT ITSQGNLPRP
SLVVNAKSIL NDASAEIKIA LDGASDWDYD ILELERVTEK RPLVYLGMKI FERFRMGHYL
NASADVLCNW LKLIEANYRQ SNSYHNSTHA GDVLHASACF LDCDRVKNLL DPLDIMASLI
AAIVHDVDHP GVTSAFLCNS HNPLALLYND SAVLESHHAA LAFKLTTSND KVNIFKGLES
DEYRSIRSSI IDMVLATEMT KHFSYLSKFT DCLNASKNTV IADDGTELKV IESSSENRML
AKRILIKCAD ISNPARNWIL SKEWALRILD EYMCQYDEED KEGLPLTMHM FNREKCNVPQ
SQRSFYDYFV KDLFKSWHSF AHIPHVMKNI EENYDHWRNV EQKGIKIYNL KNEREIHNVV
YWRSLIFDLK IVEKSFAVTY VMN
//
