ID   A0A091K8M0_COLST        Unreviewed;       772 AA.
AC   A0A091K8M0;
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=N325_04644 {ECO:0000313|EMBL:KFP33375.1};
OS   Colius striatus (Speckled mousebird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX   NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP33375.1, ECO:0000313|Proteomes:UP000053615};
RN   [1] {ECO:0000313|EMBL:KFP33375.1, ECO:0000313|Proteomes:UP000053615}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP33375.1};
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; KK549595; KFP33375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091K8M0; -.
DR   Proteomes; UP000053615; 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:UP000053615}.
FT   DOMAIN          292..729
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          99..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFP33375.1"
FT   NON_TER         772
FT                   /evidence="ECO:0000313|EMBL:KFP33375.1"
SQ   SEQUENCE   772 AA;  86573 MW;  DE158F7C4AFE185B CRC64;
     QMILWDWDLK QWYKPYYQNV GSGNGVDLSV LNEARSILTD LLTDPSLSPQ VISSLQSVNS
     LIGAFSGMCR PKASPFTPFP GFFPCPEVED LKKEIESCSS RNSLPTPQLR RTSGVSGIPP
     IESTSRWERS NSKRPHQEYN TSSQGSHSNG SFAANLLTIP KQRSSSVSST HHIGPRRAGA
     SPGLSPVGSP SHASVSSGAF SSWSPVEFPD TADFLTKPSI NIHKPPGHTF SSPDFLQQVK
     TPLDYTCSSC GRQILKPVPT SEPEYKDRKS GEIGSACVTK ESSHHTEKKK DERREMINQT
     QSNLLVEQSP TLEAMLIDHE SLMDKMNNWN FQIFDLVQEM GDQSGRILSQ VTYTLFQDTG
     LFEIFKIPTK EFMNYFRALE NGYRDIPYHN RIHATDVLHA VWYLTTRPIP GFQQIHNEHI
     MESDMDEASG IAPVQVSYIS SKSCSIADNS YGCLASNIPA LELMALYVAA AMHDYDHPGR
     TNAFLVATNA PQAVLYNDRS VLENHHAASA WNLFLSRPEY NFLSNLDHVE FKRFRFLVIE
     AILATDLKKH FDFLAEFNAK VNDINSHGIE WSNENDRLLA CQICIKLADI NGPAKGRELH
     LKWTEGIVNE FYEQGDEEAS LGLPISPFMD RSSPQLAKLQ ESFITHIVGP LCNSYNAAGL
     LPGQWVDEEE EDAESTEDDD GAQLESDDDE MEDDVILKAQ RKKGRRIFCQ LIHHLSENHK
     IWKKAIEEEE KSKAEGAKLL TEISSLPQAD EIQVIEEADE EDERQLGEDK TC
//