ID A0A2A4JSA6_HELVI Unreviewed; 980 AA.
AC A0A2A4JSA6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 22-FEB-2023, entry version 19.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=B5V51_13590 {ECO:0000313|EMBL:PCG74290.1};
OS Heliothis virescens (Tobacco budworm moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Heliothinae; Heliothis.
OX NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG74290.1, ECO:0000313|Proteomes:UP000218220};
RN [1] {ECO:0000313|EMBL:PCG74290.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HvINT- {ECO:0000313|EMBL:PCG74290.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:PCG74290.1};
RA Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA Gould F.;
RT "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT response to modern agricultural practices.";
RL Submitted (SEP-2017) 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|ARBA:ARBA00007648, ECO:0000256|RuleBase:RU363067}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PCG74290.1}.
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DR EMBL; NWSH01000779; PCG74290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4JSA6; -.
DR STRING; 7102.A0A2A4JSA6; -.
DR Proteomes; UP000218220; 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; -; 1.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 532..855
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 608
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 608..612
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 612
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 648
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 760
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 760
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 812
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 980 AA; 113580 MW; EA0125668711FD56 CRC64;
MIADDDGGLK ETTKSPTSRH SQSSKARSPG ARSPHLLPPI HNGTATSSGH NLPVYQPAQD
RSWSRFHSGC HQKHSMYLDW SAVRTDKKTR NIPKRDKARS MTSFKDAEEQ EVAEYLENNK
DFLDAYILER VPAEVLEKLL HKKLKRAYVK PSTPYHRPEI NCRKPENCNK DIFTDLLRVL
QAEPNEHSVL WQLAEYMSRT VGVDAFRLYK LYPDHPTFVQ FFVESEDDVR SLVRAYTDQV
RLVLEVAKAG TCRRVSRLEN PRIFPETPVA LFRSLGKNVK QANHVMYQPI LAMNGKTAYV
IEMWRVKDKF RDIDEEISSN FLVLGSLALH YCNMYLDKKR ERNMSDFLLD VVKAIFEEMV
LLDQLIKRIL EFAQRLVHAD RASLFLVDYR NFELVSTVFD LKYEPGHDRD MEKKEIRMPI
NRGIAGHVAL SGETMNIPDA YSDHRFNREV DETTGYKTIS ILCMPIKVEG RVIGVVQMVN
KRNGDHFDRE DEVSFEIFST FFGLSLHHAR LYDRIMRKEQ KYRVALEVLS YHNTCRENEV
MAMLSDQEPI SINLNDYYLD PYKFSEFEKC KSVIKMFSNL FDLANFDIST LTRFVLTVKK
NYRTVPYHNF DHGWTVAHTM HVILENDFEK RFNYKMRLAL FVACLCHDLD HRGYTNKYMS
EIASPLAAMY TTSTLEHHHF NITVTILQQD GHNIFSHISS EDYKEILGYI KHSILATDLA
AFFPNLAKIN QLHEGKAPNF DWEIQSHKEL AMAISMTAAD LSASAKPWYI QIKTVKVIFE
EFYDQGDKER AAGREPIPMM DRNKPDEQPS SQVGFLSQIC IPCYSILYHI LPHTRPMYIM
ALKNLERWKD RADNIEKSKL DISFITSGSV TDEDSDITLL GDEIEEETTK LETKSEEIKP
KLKIKDELSP VGEVVHDSLS WEEFEEELSE SKKLQTSGIW KDIDGATWID EEGVVVQRRD
MKSIVNKENG EKDELLVGKM
//
