ID B8Q2Y0_EUPSC Unreviewed; 347 AA.
AC B8Q2Y0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=3',5'-cyclic-GMP phosphodiesterase {ECO:0000256|ARBA:ARBA00012319};
DE EC=3.1.4.35 {ECO:0000256|ARBA:ARBA00012319};
DE Flags: Fragment;
OS Euprymna scolopes (Hawaiian bobtail squid).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Decapodiformes; Sepiida; Sepiolidae; Sepiolinae; Euprymna.
OX NCBI_TaxID=6613 {ECO:0000313|EMBL:ACB05690.1};
RN [1] {ECO:0000313|EMBL:ACB05690.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Light organ {ECO:0000313|EMBL:ACB05690.1};
RX PubMed=19509343; DOI=10.1073/pnas.0904571106;
RA Tong D., Rozas N.S., Oakley T.H., Mitchell J., Colley N.J.,
RA McFall-Ngai M.J.;
RT "Evidence for light perception in a bioluminescent organ.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9836-9841(2009).
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
CC 3',5'-cyclic GMP: step 1/1. {ECO:0000256|ARBA:ARBA00037913}.
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DR EMBL; EU344791; ACB05690.1; -; mRNA.
DR AlphaFoldDB; B8Q2Y0; -.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
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; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
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:SF230; HIGH AFFINITY CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 9A; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3}.
FT DOMAIN 14..335
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 90..94
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 131
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 240
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 291
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:ACB05690.1"
SQ SEQUENCE 347 AA; 40676 MW; DC5F17C647CE08A4 CRC64;
RHEGSLSDEK KISLRRNIPT YPKYTLSQET IDYLKQPTFD IWYWEPNEML SLLEHMYHEI
GLVDEFNINP ITLKRWLLCV QENYRNNPFH NFRHCFCVAQ MMYGMIHLCE LNKFMPIEDL
GILLTAAVCH DLDHPGYNNT YQINARTVLA IRYNDISPLE NHHCAVAFQI LSNPECNIFS
NCDQEKFKRI RAGMTMLILA TDMARHTEIM DKFGSVLHVF DFKNKEHVDT LKMVLIKCCD
ISNEVRPMEV SEPWVDCLLE EYFNQADREK LEGLPVAPFM DREKVTKPSA QIGFIKFVLL
PMFENVAKLF LKIESNMVVQ LHGALERYKE MKLHEDAMKS NQTISKS
//
