ID A0A087QT67_APTFO Unreviewed; 836 AA.
AC A0A087QT67;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 03-MAY-2023, entry version 33.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=AS27_05678 {ECO:0000313|EMBL:KFM04421.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM04421.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM04421.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM04421.1};
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; KL225893; KFM04421.1; -; Genomic_DNA.
DR RefSeq; XP_009272918.1; XM_009274643.2.
DR AlphaFoldDB; A0A087QT67; -.
DR STRING; 9233.A0A087QT67; -.
DR GeneID; 103895128; -.
DR KEGG; afor:103895128; -.
DR CTD; 5158; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000053286; 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; 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:SF73; ROD CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT BETA; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000053286}.
FT DOMAIN 462..795
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT COILED 778..812
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 538
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 538..542
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 542
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 579
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 699
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 699
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 752
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 836 AA; 96559 MW; C6E8E4F73DCFC125 CRC64;
MSISEDDVEK FLDGNPAFAK QYFEKKLKTE SWDSNETEMF FELIKEMQES VNMEKVVFKT
LRTIRSFIHA DRCSLFMYRQ RNGTPELATR LFNIQEGSTL EECLVSPDCE IVYPLDMGIV
GYVAQTKKTV NIKDVSECAQ FSPFVDELTN YTTKSILATP ILNGKDLVAV ILAINKLNGP
YFTSSDETLF LKYLNFASLN LKIYHLSYLH SCETRRGQVL LWSANKVFEE LTDIERQFHK
AFYTVRAYLN CDRYSVGLLD MTKQKEFFDL WPVLLGEVPP YSGPRTPDGR EIVFYKVIDY
ILHGKEDIKV IPNPTPDHWA LVTGLPTYVA ESGFICNIMN AAADEMFKFQ EGPLDESGWT
IKNVLSMPIV NKKEEIVGVV TFYNRKDGKP FDEQDETLME SLTQFLGWSV LNTDTYDKMN
KLENRKDIAQ DMVLYHVKCD KDEIQEILPT REKLGKEPSE CEEEELASIL KEELPGPTKF
EIYEFRFSDF DCTELELVKC GIQMYYELGV VKKFQIPQEV LVRFVYSVSK GYRKITYHNW
RHGFNVAQTM FTLLMTGKLK RYYTDLEALA MVTAALCHDI DHRGTNNLYQ MKSQNPLAKL
HGSSILERHH LEFGKFLLSE ESLNICQNLN RRQHEHVIHL MEIAIIATDL ALYFKKRTMF
QKIVDESKTY DSVTAWTEYL SLETTKKEVV MAMMMTACDL SAITKPWEVQ SKVALLVAAE
FWEQGDLEIS VLQQQPIPMM DRRKAAELPK LQVGFIDFVC TFVYKEFSRF HEEIQPMLDG
LLNNRNEWKT RADEYDAKMK ALEEEKKKDA EKMAAKKDGI TCNGGTAPAS KTCSIL
//
