ID A0A0L7RJ81_9HYME Unreviewed; 1045 AA.
AC A0A0L7RJ81;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=WH47_05013 {ECO:0000313|EMBL:KOC71027.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC71027.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC71027.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC71027.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC ChEBI:CHEBI:58115; EC=3.1.4.35;
CC Evidence={ECO:0000256|ARBA:ARBA00000583};
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 -!- SUBUNIT: Interacts with PrBP. {ECO:0000256|ARBA:ARBA00038662}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342};
CC Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004342}. Membrane
CC {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004423}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|ARBA:ARBA00007648, ECO:0000256|RuleBase:RU363067}.
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DR EMBL; KQ414581; KOC71027.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7RJ81; -.
DR STRING; 597456.A0A0L7RJ81; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF216; PHOSPHODIESTERASE; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW cGMP {ECO:0000256|ARBA:ARBA00022535};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 618..941
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 133..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 694
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 694..698
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 698
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 734
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 735
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 735
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 735
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 845
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 845
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 898
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1045 AA; 118957 MW; 54FB7C165205BA4D CRC64;
MVQVSQNDNI EVFKTMKIST KPMSSKASEQ SESPEETVTV IPCKYPGKTK TQEESKLPLS
SSIKTDIKDS EIVRICRSKR ITCQDTIHEY DEDDGLTMEK VGRYLEAHPE AAEAWLRENA
SLELRQRLQG VALPQPNSPT RSIHQEENLL SRSKRNSVTS DLFQSWLASS SPAKRSRSPS
RTYSSLVGRR EELNRLDESD LFMELIRDVA NELDINVLCH KILVNVGLLT HADRGSLFLA
KGPFDDRYLV AKLFDVTQDT ELEEAVQRAK NEEIKIPFGV GIAGYVAQTK EIINIKDAYK
DPRFNSSIDM RTGYKTTLIL SMPISNYEGD VIGVAQIINK TNGSNEFTDR DVEVFQRYLT
FCGIGIQNAQ LFELSVQEYR RNQILLNLAR NIFEEQNNLE CLVTKIMTEA KELLKCARCA
VYLLDLDCGE AGHLEKIVER PGKSTQESRK PLSRRESNNI EMEDIFTQHA LNDHNKFTTI
FEMDNETQEA KVYRPSGNEL STPLGQIAKY VAATGQILNI GDVATWLKKD VVQSGSEPIK
SILCMPIVNG QRTVIGVAQL INKDNGTSFT DSDVSIFEAF AIFCGLGIHN TQMYESACKL
MAKQKVALEC LSYHATASND DTLKLTSEPI PSAESFNLYS FTFIDFDLTD EDTCRATIRM
FKQCDLIGKF HIPYEVLCRW VLSVKKNYRP VKYHNWRHAL NVAQTMFAML KTGKMEQFMT
DLEILGLLVA CLCHDLDHRG TNNAFQTKTE SPLAILYSTS TMEHHHFDQC VMILNSDSNN
IFQNLSMEDY RKVMKVVESA ILSTDLAVYF KKKNKFMELI DEGEFDWQSE EKKELLCGMM
MTACDVSAIA KPWEVQHRVA KLVADEFFDQ GDLERLQLNQ QPVAMMDRER KDELPQMQVG
FIDVICIPLY KVLADTFPWI MPLYEGTMEN RKHWQDLAEK VEMGLTWIDR DTIDDPVEEF
VSYEPKDIEF TVTTLNCAHS DRKDVPEKSA LGRFASLRKG GRTLSKGVRH RISRSLYARS
TPEDAAKSKA LIPDRKSRNK LCLLI
//
