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Database: UniProt
Entry: A0A093KWJ9_FULGA
LinkDB: A0A093KWJ9_FULGA
Original site: A0A093KWJ9_FULGA 
ID   A0A093KWJ9_FULGA        Unreviewed;       498 AA.
AC   A0A093KWJ9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE   Flags: Fragment;
GN   ORFNames=N327_02113 {ECO:0000313|EMBL:KFW01751.1};
OS   Fulmarus glacialis (Northern fulmar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC   Fulmarus.
OX   NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW01751.1, ECO:0000313|Proteomes:UP000053806};
RN   [1] {ECO:0000313|EMBL:KFW01751.1, ECO:0000313|Proteomes:UP000053806}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW01751.1};
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   -!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
CC       3',5'-cyclic GMP: step 1/1. {ECO:0000256|ARBA:ARBA00037913}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       {ECO:0000256|RuleBase:RU363067}.
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DR   EMBL; KK593631; KFW01751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093KWJ9; -.
DR   Proteomes; UP000053806; 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; 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:SF230; HIGH AFFINITY CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 9A; 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   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|PIRSR:PIRSR623088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053806}.
FT   DOMAIN          156..477
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   ACT_SITE        232
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         232..236
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         272
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         273
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         273
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         382
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         433
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW01751.1"
FT   NON_TER         498
FT                   /evidence="ECO:0000313|EMBL:KFW01751.1"
SQ   SEQUENCE   498 AA;  58056 MW;  474044C6B48AA6CD CRC64;
     VWKVIFSKYC NSKDIMDLFC IATGLPRNTT ISLLTADNCM VSIDPTMPAN SERSPYKVIP
     VATGQLSEKE ELLQNLLGQI AEQFSRVFKI NELKTEVANH LAMLEKKVEL EGLKVVEIEK
     CKSDIKKMRE EMAARSSRTN CPCKYSFLDE NKRLTPRRDV PSYPKYMLSQ ETIEALRKPT
     FDVWLWEPNE MLSCLEHMYH DLGLVKDFNI NPITLKRWLL CIHDNYRNNP FHNFRHCFCV
     TQMMYSMISL CSLQEKFSQI DILILMTAAV CHDLDHPGYN NTYQINARTE LAVRYNDISP
     LENHHCAVAF QIISQPEYNI FSNVDQDQFK QIRQGIITLI LATDMARHAE ILDSFKEKME
     NFDYSNEEHM TCLKMVLIKC CDISNEVRPM EVAEPWVDCL LEEYFMQSDR EKSEGLPVAP
     FMDRDKVTKP TAQIGFLKFV LIPMFETVTK LFPEVEEVML QPLWESRDRY EELKQIDDAM
     KELQKKKSES LTTSSTEK
//
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