ID A0A0A0AKY6_CHAVO Unreviewed; 739 AA.
AC A0A0A0AKY6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE Flags: Fragment;
GN ORFNames=N301_09125 {ECO:0000313|EMBL:KGL94213.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL94213.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL94213.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL94213.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-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 AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004703}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE8 subfamily. {ECO:0000256|ARBA:ARBA00006437}.
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DR EMBL; KL871964; KGL94213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0AKY6; -.
DR STRING; 50402.A0A0A0AKY6; -.
DR UniPathway; UPA00762; UER00747.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF85; HIGH AFFINITY CAMP-SPECIFIC AND IBMX-INSENSITIVE 3',5'-CYCLIC PHOSPHODIESTERASE 8A; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW cAMP {ECO:0000256|ARBA:ARBA00023149};
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:UP000053858}.
FT DOMAIN 134..204
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 391..730
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 258..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 467
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 467..471
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 507
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 508
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 636
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 636
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 688
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:KGL94213.1"
FT NON_TER 739
FT /evidence="ECO:0000313|EMBL:KGL94213.1"
SQ SEQUENCE 739 AA; 83806 MW; 180F3EB3BC7F0E62 CRC64;
QVLLVFAKED NQSNGFCWAC EKAGFRCNIA RTPESALECF LDKHHDIIII DHRHSRYFDA
EALCRSIRTT KPSENTVIIG VVRRHADREE SSILPLISAG FTRRYVENSN IMACYNELIQ
LEFGEVRAQF KLRACNSLFT ALEKSQEAIE ITSEDHVIQY VNPAFETVMG YQIGELIGKE
LTEVPINEKK ADFLDTINSC IKIGKEWQGM YYAKKKNGDS IQQNVKILPV VGQGGKIRHY
VSISRLCNDN NKVSENNIQT CRHKDRRKGS LDVRSTTSRG SDGSSQRRHS SMARIHSMTI
EAPITKVINI INAAQESSPM PVAEALDRVL EILRTTELYS PQLGTKDEDP HTSDLVGGLM
TDGLRRLSGN EYILSAKQTH QVAGSLISPI SLNDIPPRIT QAMENEEHWD FDIFELEAAT
HKRPLVYLGL KIFARFGICE FLNCSESTLR SWLQVIEANY HSSNSYHNST HSADVLHATA
YFLSKERVKQ TLDPIDEVAA LIAATVHDVD HPGRTNSFLC NAGSELAILY NDTAVLESHH
AALAFQLTTR DDKCNIFKNM ERNEYRTLRQ AIIDMVLATE MTKHFEHVNK FVNSINKPLA
ALEENGNNGD GESIKTVLTS PENRILIKRM LIKCADISNP CRPIEQCIEW AGRISEEYFA
QTDEEKRQGL PVVMPVFDRN TCSIPKSQIS FIDYFITDMF DAWDAFADLP NLMQHLDNNF
KYWKGLDERK LRSLRPPPE
//
