ID A0A3Q1GUB7_9TELE Unreviewed; 940 AA.
AC A0A3Q1GUB7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000030977.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000030977.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU363067}.
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DR AlphaFoldDB; A0A3Q1GUB7; -.
DR STRING; 80966.ENSAPOP00000030977; -.
DR Ensembl; ENSAPOT00000023549.1; ENSAPOP00000030977.1; ENSAPOG00000017983.1.
DR GeneTree; ENSGT00940000165630; -.
DR InParanoid; A0A3Q1GUB7; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
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; 3.30.450.40; -; 2.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
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; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF191; PHOSPHODIESTERASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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 cGMP {ECO:0000256|ARBA:ARBA00022535};
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:UP000257200}.
FT DOMAIN 538..862
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 41..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 614
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 614..618
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 618
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 654
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 655
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 766
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 766
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 819
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 940 AA; 106941 MW; F3EF0B1A8D1B20CF CRC64;
MTAFDFSDIE AFLDCHPDLF EEYLVRKAKC DQVSRWLKEH QPSKVSAAEE KRGASTDPLW
PTNADGLRRR SSHMELRRNF ARSKATTAHR TYDEHVSLSE HESQSSMRRR ALLRKASSLP
PTTAHILSAL LESRVNVPQY ASSAIDYKYR LKETNEREFF LELVKDISND LDLTNLSYKI
LINVCILVDA DRCSLFLVEG PAHKRTLVSK FFDVHSGTTV RPSSSTLNSN EVQVPWGKGI
IGYVAEHGET VNISNAYEDH RFSDEIDKLT GYKTQSILCM AICNSDGEVI GVVQAINKNP
IGTPFTEDDE KVLQMYLPFC GISISNAKLF SESRKEYERS RALLEVVNDL FEEQTDLEKI
VRKIMQRALT LLQCERCSVL LLEDIDSPVV KFSKTFELMS PLCNIDRDIS MEKLSCSDWL
INNSIAELVA STGLPVNISD VCQDPRFDAE ADQASGFHIR SVLCVPIWNR THQIIGVAQI
LNRLDRKTFN DADQRLFEAF VIFCGLGINN TMMYNQVKKT WAKQSVALDM LSYHATCSKV
EVDRLKAAKI PLSSELGIDE FHFNDFSLDN DAMITASLRM FLELGVVQKF KIDYEVLCRW
LLTVRKNYRT VAYHNWRHAF NVSQCMFVMI TTASFQDVLS EAEILALMVG CLCHDLDHRG
TNNAFQAKTG SALALLYGTS ATLEHHHFNH AVMILQSEGH NIFANLCSKE YSNMMQLLKQ
AILSTDLTLH FERRTKFFEC VLSGDFSWTD EGHREVLRSM LMTACDLGAV TRPWKISKQV
AELVTSEFFE QGDRERSELK LTPAAIFDRN RKDELPALQR EWIDGICKPL YQTLLKLNRK
LQPMVDGIDA NRQKWQDLCS SYQQTRRASV SNPSAEPGQN IEFSEDTETS ERPKTAATVK
LDENKKLKSK CRQDLKWRLN QQPCDDEEAS AGIVTPAGNK
//
