ID A0A1W4WYY5_AGRPL Unreviewed; 818 AA.
AC A0A1W4WYY5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=LOC108737157 {ECO:0000313|RefSeq:XP_018325357.1,
GN ECO:0000313|RefSeq:XP_018325358.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018325358.1};
RN [1] {ECO:0000313|RefSeq:XP_018325357.1, ECO:0000313|RefSeq:XP_018325358.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_018325357.1,
RC ECO:0000313|RefSeq:XP_018325358.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00007648, ECO:0000256|RuleBase:RU363067}.
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DR RefSeq; XP_018325357.1; XM_018469855.2.
DR RefSeq; XP_018325358.1; XM_018469856.2.
DR EnsemblMetazoa; XM_018469855.2; XP_018325357.1; LOC108737157.
DR EnsemblMetazoa; XM_018469856.2; XP_018325358.1; LOC108737157.
DR GeneID; 108737157; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000192223; Unplaced.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC.
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:SF111; CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE 10A; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF01590; GAF; 1.
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};
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:UP000192223};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 490..808
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 564
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 564..568
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 602
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 603
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 713
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 713
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 765
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 818 AA; 93506 MW; 421A2B7CBBA1AD40 CRC64;
MWSALVRGLA NLLTNRQTPQ GMQSSRRGSD RVPTPPVCGI TGLTASQVSN YLRANQDFLE
RFVTEEVELE QLERWLIRRS QQLKRKEKET SSTKNNNSSG RKTSLSRWKF CVHADKRQML
LDLTHSLQLK PTKDHVLWEL ANCICSAVNA DGFRLYIAEH SNAHNLFLYQ ENSDNSDISK
KEKAITGKTV PTYVARTREA VRLSRNNTDN RFPNAFTGLS QAAHLQCQAV LQPDGQLVAV
LELWRKEGDT PFYEEDEEIA SSYIVWGGVA LHYAELYFSM NQQRRLNDFL LAVVKSIFQD
MVSMDILVTK IMNFAQRLVD ADRASLFLLD SKNKELYATI FDVGLETSRE NVDDDSEENA
KKASNNTSKE IRFPLGTGIA GQVAMTGEVL NITDAYADER FNRTVDQLTG YRTRTILCMP
IFIRGSIIGV VQMVNKRTGS FTKDDEQAFE MFAVYCGLAL HHAKLYDKIR KSEQKYKVAL
EVLSYHNSCT EDEVETVQQN KLPEKVEVLI DDYYFNPFQL EDYEKAGHAI YMFTDLFGLS
RFDKQSLLRF TLTVKKNYRR VPYHNWAHGF SVANCMYTII KHSGGVFQTN EGLALYIGSL
CHDLDHRGKN NKFMLESASP IAAIYSTSTM EHHHFNQTVT ILQQEGHNIF AKLSNSEYKQ
MLGLLKHCIL ATDLALFFPN KAKLTEIVEQ KAFSWDDEEH RLLLLAISMT SSDLCASAKP
WDIQTETVKV IFEEFYQQGD AERAAGRQPI PMMDRYQPDQ QAASQVGFLT GICIPCYTLL
YTIIPETKPL LDKCNENLRR WQEIDREVQE KKKLGGDI
//
