ID R1EXT3_BOTPV Unreviewed; 577 AA.
AC R1EXT3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=UCRNP2_774 {ECO:0000313|EMBL:EOD52412.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD52412.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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|RuleBase:RU363067}.
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DR EMBL; KB915749; EOD52412.1; -; Genomic_DNA.
DR RefSeq; XP_007580098.1; XM_007580036.1.
DR AlphaFoldDB; R1EXT3; -.
DR STRING; 1287680.R1EXT3; -.
DR KEGG; npa:UCRNP2_774; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_010668_4_1_1; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000013521; 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; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
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 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU363067};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521}.
FT DOMAIN 208..555
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 113..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 64728 MW; 8B1994A3A9A4FA7C CRC64;
MDHGACSVIY LDRRAHPERL RRDNVLASLN ARDARQVQAQ SPGYFNFGKS TSTHEVLSNV
ETLLSIFTEI DVHRSGSAAL DRIWHLYNAS SSDNAPIIVL IDLPYDEERR MKRLSREPRT
PSPTATRTPG QDQTEPEDLY GMHLLRHISA EIQDRRLPRI VIPIILLSGL DYEIAPDSSS
PGPNGSQVLT DTVRLTRYLD AGAVDTLSDI EVSPERRKQI AAAVGTWAFS AHDWNDDELL
FGSLVMIKHA LSMPEVERWR MGEDELLIFL QASRSAYNEF VLYHNFRHVV DVLQALFYFL
VRIGALPAYP LDSSSTPVEQ PPIASLLKPF DSLTLLISAI GHDVGHPGVN NAFLVALNAP
LAQLYNDRSV LESFHCAAYS QILRRYWPGA FEDVAMRKLM INSILATDMG LHFKYMADLG
NLQEKLAHNN GGIDGWSPKV LEEYRDLICG LLIKCADISN VARRFKTAVQ WAAILTDEFS
NQGQMEQELS LPTCLFGGPP VRDDIIKLGE SQIGFMNIFA RPLFESVADI LPNMRFSVNE
IIENKVVWQK KIEEAKERLL PKLDGAVGTS ILDQARN
//
