ID A0A0W8C8U0_PHYNI Unreviewed; 1162 AA.
AC A0A0W8C8U0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=AM587_10017485 {ECO:0000313|EMBL:KUF80468.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF80468.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF80468.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-2015) 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 -!- 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}.
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:KUF80468.1}.
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DR EMBL; LNFO01004567; KUF80468.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8C8U0; -.
DR EnsemblProtists; KUF80468; KUF80468; AM587_10017485.
DR OMA; IHCILAT; -.
DR Proteomes; UP000052943; 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; PF01590; GAF; 3.
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:UP000052943}.
FT DOMAIN 832..1162
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 65..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..57
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 787..812
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 905
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 905..909
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 946
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 947
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 947
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 947
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1068
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1068
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1121
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1162 AA; 129786 MW; 29A106B8108FD54A CRC64;
MSNDEVKLVR VPVRELKTAM NGARAALDEN RRLVAELAQS EEEAKELELK LLKRQHQLEC
CTGSRMETRP YRPGDALKST PRRPRPKSEM FGDSIRNLIG EQAETLNQLA DREENLRALM
DAMREISRAS DSLDVVSNAL RAAQHVLPAE KYTVGILNEK KDRVELYSNP PMDLPGKRYL
IEEGSALVDS ATTFGRVVLT GTPLEVADVS GSEVIDVFEE QMEVLKFEPE ALLCAPIFNV
HGVLVGVFQV ITRKILPELG LHSTPATPSD SQWYSSTPRT ALARLGRNQG AQQKGAFDPR
DKENFDYICV TAGTALWNLS LAKAHQAMQS RIECLLKLNR NIAAEVSASA VLHQIIAVAY
ELLHAEHIAL YVRDEGTDEY YLFVTDCKDE MAIAGFPGTK TRHKLKDKAS EKPHTGYDET
FLKAHNGIVG VVMRTGQLIL TNSASAHPAF DPKYDEFWTF KTKQVLCAPV KDASGQVLAV
VCATNKVDGD EFTADDALYL NYAAEAAGIS LHKSNLLRSV LMSQRLTEAR LQLADFVNNN
GERAYSNSSH EPDDETSAAA SVARFVRVVM AEGRKLLHCD RFGFLLVDPL KKELWITQED
GERVRMPLTN GLSGLIATTG KIINTRDAYT HPHFDPSLDR KTGYRTTSVL GMPIFEDHTP
TNPKIVAVVI AINKKDDDDT NVTEDVASRR IPRHRVPFTA SDAECMTQYC REIQFALGRL
SLDISYYKVV SDCGLSAPGE SLIKSAEAQE QLDGINEPEI VASIVQKYCQ SSELDALEEM
ATVANTDDPD EVEDVDEVNG GEYDDEGSEK DDEDEHVTAF LAIPFPPRSX QRRISTPREN
GHVIGVGDVT RWDFSCLDLS NVDIFAAVSV LFRSLGLLER FQVAQETFFT FLSHVASHYR
PNAYHNLQHA FQVTHATYCL LRRSGVAHSY FARVEIFAML IAALCHDLDH PGNTNDFEVK
THSQLALTHN DDAVLERHHC RVAFIILSHP GANLFGRLPT RACFVYVRRL LIHCILATDM
AKHFEKCKAL EGLSKRHLLV NTNGGRGAKR GRSKHRFVFM AILIHAADLS GQALSYTQAT
RWGMRVLSEY QQQAKSEAEL HFPVESFMAN LHHAKTRVTV QLNFINYVLR PIWLPLATLC
PAMKVYADSL ESNRERYKAE LD
//
