ID A0A182KA65_9DIPT Unreviewed; 740 AA.
AC A0A182KA65;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 34.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR007652-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR007652-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR007652-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 AlphaFoldDB; A0A182KA65; -.
DR STRING; 43041.A0A182KA65; -.
DR EnsemblMetazoa; ACHR007652-RA; ACHR007652-PA; ACHR007652.
DR VEuPathDB; VectorBase:ACHR007652; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000075881; Unassembled WGS sequence.
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:SF221; DUAL 3',5'-CYCLIC-AMP AND -GMP PHOSPHODIESTERASE 11; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 1.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 244..581
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 586..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 332..336
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 373
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 485
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 485
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 538
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 740 AA; 83606 MW; 5D7F20801716057C CRC64;
MPIKDASGDV VGVAQVINKQ GDQCFSTADE KIFSSYLQFC GIGLRNAQLY EKSQLEVKRN
QVLLDLARMI FEEQSTIEHM VFRILTHMQS LIQCQRVQIL LVHEASKGSF SRVFDFEAND
LSGDDGDART SPFESRFPIN VGITGYVATT GETVNICNAY EDDRFDPSVD EGLNFRHKTI
LCMAIKNSLS QIIGVIQLIN KFDDLTFTKN DENFVEAFAI FCGMGIHNTH MYEKAIIAMA
KQSVTLEVLS YHASATMDDA YRLRQLKVPS SAFFKLHDFK FDDLSLDDDH TLKACIRMFL
DLDLVERFHI EYEVLCRWLL SVKKNYRNVT YHNWRHAFNV TQMMFAILTS TQWWKIFGEI
ECLALIIACL CHDLDHRGTN NSFQIKASSP LAQLYSTSTM EHHHFDQCLM IINSPGNQIL
SNMSSEDYSR VIRVLEDAIL STDLAVYFRK RGAFLNLVEP TSELSSWQAE EPRSLLRAMS
MTVCDLSAIT KPWEIEKRVA DLVSSEFFEQ GDMERQELNI TPIDIMNREK EDQLPLMQVG
FIDSICIPIY EAFATLSDKL TPLIDGVLEN KQHWIEMAQS AKDAYANNNN TSENNNNNKS
PCTEHAEEED LKNGECVGSP LGSPASNGTT QRKLSLEPDC TDSGHHHSIG SQEPTTHSCR
SIKEKIVGRL GVDLASSPPY TDKPSFLVVG QKGNGWVNGD KVRLIRLSSS DGKTSELLLD
DQLQRHPTVD DDQTVDALLE
//
