ID   A0A091IZU0_EGRGA        Unreviewed;       842 AA.
AC   A0A091IZU0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE   Flags: Fragment;
GN   ORFNames=Z169_01623 {ECO:0000313|EMBL:KFP13073.1};
OS   Egretta garzetta (Little egret).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX   NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP13073.1, ECO:0000313|Proteomes:UP000053119};
RN   [1] {ECO:0000313|EMBL:KFP13073.1, ECO:0000313|Proteomes:UP000053119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP13073.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) 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|RuleBase:RU363067}.
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DR   EMBL; KK501152; KFP13073.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091IZU0; -.
DR   STRING; 188379.A0A091IZU0; -.
DR   Proteomes; UP000053119; Unassembled WGS sequence.
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; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
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:SF29; PHOSPHODIESTERASE; 1.
DR   Pfam; PF00233; PDEase_I; 1.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU363067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053119}.
FT   DOMAIN          362..799
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP13073.1"
FT   NON_TER         842
FT                   /evidence="ECO:0000313|EMBL:KFP13073.1"
SQ   SEQUENCE   842 AA;  94548 MW;  305A522C3E1F18EF CRC64;
     AQSRGAHHQH HRHPRLPSVE EKVPVIRPRR RSSCVSLGET SASYYGSCKM FRRPSLPCIS
     REQMILWDWD LKQWYKPYYQ NAGSGNGVDL PVLNEARSML TELLTDPSLP PQVISSLRSI
     SSLIGAFSGT CRPKASPFTP FPGFFPCPEI EDPAEKGDRK LLKGLNSRNS LPTPQLRRTS
     GVSGIPPIES TSRWERSNSK RSHQEYNTSS QGSHSNGSFG ANLLTIPKQR SSSMTLTHHI
     GPRRAGASPG LSPVGSPSHG SVSSGAFSSW SPVEFPDTAD FLTKPSINIH KPPGYTFSSP
     DIQQQARTPV GYMCSSCGRQ IPKPVPTAEP EFAEYKDRKS GEIGSASVSK ESFNHTEKKK
     DERKETIDQT QNNLLVEQSP TLETMFLDHD SLMEKMNNWN FQIFDLVQEM GDQSGRILSQ
     VTYTLFQDTG LFEIFKIPTQ EFINYFCALE NGYRDIPYHN RIHATDVLHA VWYLTTRPIP
     GFQQIHNEHI MESDMDEASG IAPVQVSYIS SKSCSIADDS NGCLASNIPP LELMALYVAA
     AMHDYDHPGR TNAFLVATNA PQAVLYNDRS VLENHHAAAA WNLFLSRPEY NFLSNLDHVE
     FKRFRFLVIE AILATDLKKH FDFLAEFNAK VNDINSHGIE WSNENDRLLA CQICIKLADI
     NGPAKVRELH LKWTEGIVNE FYEQGDEEAS LGLPISPFMD RSSPQLAKLQ ESFITHIVGP
     LCNSYNAAGL LPGQWVDEEE EDAESTEDDD GAQLESDDEE MEDDLILKAQ RKKGRRIFCQ
     LIHHLSENHK IWKKVIEEEE KNKGEGAKLL TEISSLPQAD EIQVIEEADE EDERQLGEDK
     TC
//