ID A0A0D1XCZ7_9PEZI Unreviewed; 753 AA.
AC A0A0D1XCZ7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=PV09_08286 {ECO:0000313|EMBL:KIW00101.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW00101.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW00101.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW00101.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
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DR EMBL; KN847567; KIW00100.1; -; Genomic_DNA.
DR EMBL; KN847567; KIW00101.1; -; Genomic_DNA.
DR RefSeq; XP_016209969.1; XM_016362152.1.
DR RefSeq; XP_016209970.1; XM_016362153.1.
DR STRING; 253628.A0A0D1XCZ7; -.
DR GeneID; 27316259; -.
DR VEuPathDB; FungiDB:PV09_08286; -.
DR HOGENOM; CLU_010668_4_1_1; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000053259; 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:SF219; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE, ISOFORM I; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 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:UP000053259}.
FT DOMAIN 287..634
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 20..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 83987 MW; C38CA470BEA6D975 CRC64;
MDHGACNVIY LDRRAQAKTV RRDSVFPNSE TSNASMPSSQ DEDYFDIPSR LPEELRNNIQ
SILTTFNEVH LCQSGSICLD KLAELQQSSK SPCPTVLLID VPYDEEQRRK RLSREPRTPS
PTSFRTRPKT NESLEAADIY GVPFLTHISA EIHARNLSRM IVPVVVLSGF DREWAANSSL
PSPSVHGSQV LSDTFRLTRY LDNGAVDVLA SPMSRDSVQG LAVHAYRIYK EVSASEAAFM
AQKRNRKLSW VGVDETKPYA YLREAMVSNL MERICNPGMV PEKYDVTDVE IEPDRKEVVA
QSIGTWEFSA HDFTDDELLH AALQMLQHAL TMPEVEKWRM SEENLLTFLM ATRAAYNDFV
LYHNFRHVVD VLQACFYSLC SIGALPPYPH PRGKLKPIRC PISTLIKPFD ALTLLVAAIG
HDVGHPGVNN AFLVVLNSPL AQLYNDQSVL ESFHCAAYSQ ILRRHWPACF EDTAMRKLMI
NDILATDMGV HFKYMSEMGN LQEKYTHNGG KLDGWNVKVQ EGYRDLICGL LIKCADISNV
ARSFPVAAQW ASILTDEFSN QGNMEIELGI PTQLFGGPPV RDNVVKMGES QIGFINVFAR
PLFENVAKLL PGMSFAVDTI LENERIWQVR IREEKDAQER GIVRNETVES GLLSPRSGSP
ARDASSTQKS APAVLEAGAL TTQPEGSPRP FTSNGHPVAP VDTYQAQRAD AHLKPGDNKN
IYLSSSSTTD VASAVNGNAK RGGTWKKIKK IFR
//