ID I3JPK5_ORENI Unreviewed; 913 AA.
AC I3JPK5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=pde11a {ECO:0000313|Ensembl:ENSONIP00000010799.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000010799.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000010799.2}
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; I3JPK5; -.
DR STRING; 8128.ENSONIP00000030946; -.
DR Ensembl; ENSONIT00000010808.2; ENSONIP00000010799.2; ENSONIG00000008590.2.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000164264; -.
DR HOGENOM; CLU_006980_0_1_1; -.
DR TreeFam; TF316499; -.
DR Proteomes; UP000005207; 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:SF139; PHOSPHODIESTERASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
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:UP000005207}.
FT DOMAIN 547..871
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 43..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 623
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 623..627
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 627
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 663
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 664
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 775
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 775
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 828
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 913 AA; 103742 MW; 70DF630A2EEE3173 CRC64;
MAVSKMLFSD VESFLDSHPE LFEDYLNRKG NYGMVEKWLK NHQASKSPTA SAPAETREEK
SNPCKDSWAS KCDGLQRRAS QKELRKTFAR SKAINVNRTY DEHVNSRAQE PLTSMRRRAL
LRKASSLPPT TAHILSALLE SRVNIPQYPS TAVDFKYYLK EHNEREFFLE LVKDISNDLD
LTSLSYKILV FVCIMVDADR CSLFLVEGTG NKQTLVSKFF DVHAGTTVLP SMNSDEVQVP
WGKGIIGYVA EHGETVNIPD AYQDRRFSDE IDKLTGYKTK SLLCMPIRNS DGEIIGVAQA
INKNSSGELF TEDDEKVLQM YLPFCGIAIS NAQLFAASRK EYDRSRALLE VVNDLFEEQT
DLEKIVRKIM HRAQTLLKCE RCSVQLLEDI ESPVVKFTKS FELLSPKCSA DTESSFKDSL
EKSSYSDWLI NNSIAELVAS TGLPVNISDA YQDPRFDAEA DQFSDFHIRS VLCVPIWNSN
HQIIGVAQVL NRLDGKPFDD ADQRLFEAFV IFCGLGINNT IMYDQVKKSW AKQSVALDVL
SYHATCSKTE VDKFKAANIP LVCELGIDKL SFDDFSLDVD AMITAALRMF MELGMVQKFK
IDYETLCRWL LTVRKNYRMV LYHNWRHAFN VCQCMFAMLT TAGFQETLTD VEILALIVGC
VCHDLDHRGT NNAFQAKTGS ALALLYGTSA TLEHHHFNHA VMILQSEGHN IFSNLSSTEY
SDLMQLLKQS ILATDLTLYF ENRNMFFELV SNGEYNWNVK AHRDMCRSMM MTACDLGAVT
KPWEISRKVA ELVTSEFFEQ GDRERLELKL TPSAIFDRNR KDELPGLQLE WIDGICSPLY
ETLVKLNPKL QPMVDMIKAN RAKWEELNRK RQRGQSVSAP ASPSIVGHFK SCPFLLIANQ
FERKILTTLV VIC
//
