ID G4ZPF5_PHYSP Unreviewed; 1153 AA.
AC G4ZPF5;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=PHYSODRAFT_505033 {ECO:0000313|EMBL:EGZ15779.1};
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ15779.1, ECO:0000313|Proteomes:UP000002640};
RN [1] {ECO:0000313|EMBL:EGZ15779.1, ECO:0000313|Proteomes:UP000002640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497 {ECO:0000313|EMBL:EGZ15779.1,
RC ECO:0000313|Proteomes:UP000002640};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
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DR EMBL; JH159155; EGZ15779.1; -; Genomic_DNA.
DR RefSeq; XP_009529528.1; XM_009531233.1.
DR AlphaFoldDB; G4ZPF5; -.
DR STRING; 1094619.G4ZPF5; -.
DR EnsemblProtists; EGZ15779; EGZ15779; PHYSODRAFT_505033.
DR GeneID; 20658424; -.
DR KEGG; psoj:PHYSODRAFT_505033; -.
DR InParanoid; G4ZPF5; -.
DR OMA; IHCILAT; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
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; 3.30.450.40; -; 3.
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:SF198; CAMP-SPECIFIC 3',5'-CAMP PHOSPHODIESTERASE 4; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 3.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 3.
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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000002640}.
FT DOMAIN 775..1113
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 63..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..57
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1096..1130
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 657..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 854
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 854..858
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 858
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 896
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1017
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1017
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1070
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1153 AA; 128628 MW; 7BE001F54A6D1290 CRC64;
MADDQVKLVR VPVRELTTAM DGARAALDEN RRLAAELAQS EEEARELEIK LLKRQHQPDC
CTGARAEHRP YRPGDLLNPA SPKRMRPKSE MFGTSMRNLI GEQAETMNQL AEREENLRAL
MDAMREVSQA SDSLDIVSNA LRAAQHVLPA EKYTVGILSE KKDRVDLYSN PPMDLHGKRY
LTEEGSVLVD SATTFGRVVL TGRPLEVADV SGSEVVDVFE EQMELLEFEP EALLCAPIFN
VHGILVGVFQ VITRKQLPEL GLLPAPAPPP EPLWFSSTPR SDLTKLGQNQ ENQEKAAFDP
RDKESFDYIC VTAGTALWNL SLAKAHQAMQ SRIECLLKLN RNIAAELSSS AVLHQIIAVS
YELLRAEHIA LYVRDEGTEE FFLFVTEPHH SHLRHGGYDE AFLKAHNGIV GVVMRTGQLV
LTNSAPTHLA FDPKFDELWT SLKTKQVLCA PVKDAGGHVL AVVCATNKVD GDEFTSDDAL
YLNYAAEAAG ISLHKSNLLR SVLMSQRLTE ARLQLADFVN NNGERAYSPS GAEDETSAAA
SVARFVRVVM AEGKKLMHCD RFGFLLVDPL KKELWIIQED GESVRMPLTN GLSGLIATTG
RSICTRDAYT HPHFDPTLDR KTGYRTTTVL GMPVFEDHTP TNPKIVAVVM AINKKDDNDD
EANNAKTDDD DAPPVTRQHV PFTTSDADCM TQYCREIQFA LGRLSLDISY YKVVSDCGLG
TPVDDLNEPE IISSIVQKFC QSSELDVLEE VAAAAIADDP DDEEQPTPFA AIPFPQRLPQ
RRISTARESG HVIGVGDVTR WDFSCLDLSN PDIFAATSVL FRSLGLLERF QVAQETFSTF
LSHVASHYRP NAFHNLQHAF QVTHATYCLL RRSGVANSYF ARVEVFAMLV AALCHDLDHP
GNTNDFEVKA HSQLALTHND DAVLERHHCR VAFVILSHPG ANLLARLPSR ACFVYVRRLL
IHCILATDMA KHFEKCKALE GLSKRHLLVN SDGGRGARRS RSKHRFVFMA IIIHAADLSG
QALPYTQAVR WGMRVLSEFQ QQAKNEAEMH VPVESFMTNL HHAKTRVTVQ LNFINYVLRP
IWLPLATLCP AIRVYADSLE SNRERYKAEL DKLQREAEEI EELARVYVRG NSSRSLVEHS
SSTRRLSSLS QKN
//
