ID A0A0D2EF57_9EURO Unreviewed; 1024 AA.
AC A0A0D2EF57;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=PV04_01096 {ECO:0000313|EMBL:KIW72937.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW72937.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW72937.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW72937.1,
RC ECO:0000313|Proteomes:UP000054266};
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 Capronia semiimmersa CBS27337.";
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; KN846956; KIW72937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2EF57; -.
DR STRING; 5601.A0A0D2EF57; -.
DR HOGENOM; CLU_010668_0_0_1; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000054266; 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; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3}.
FT DOMAIN 282..630
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 636..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..844
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 358
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 358..362
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 419
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 532
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 587
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1024 AA; 112179 MW; D02D1E4BB03B211A CRC64;
MDPSACRVIY IDERFNTERW ISREGLSPTT PARAGSHVEF SDLPPDLQTN VNAFLTVFNQ
VYVCSSGRAF STKLSELHDQ VKLDCTPILA CFDVGSESKH GYLRSRPKFF PSSDSPLPSP
SLLRKEITFS SESDESYGLQ LVSRIASDLQ VEEGVKLIIP VAIVQPKRSD SYDQALDSVR
QPEVSRAPFG PEADPVAIED SSDVIDTQLM LQCLDAGALD VVKSPLDKAG IMGLTVHAYR
IYKNAKKEQA GFMAMARRNR KQSWVGMEDE KPYAYLREAM HRDLFVQESR KAVVAAAVGR
WDFSGHDFTE DELVYAGYYM LNHCLEMEAC EQWSMSQRDL LHFMQGCRIA YNSFVLYHNF
RHAVDVLQSV FFFLVQIGTL PPYPTGAEPS PFADKKSPIA RLLGPFEALT LLVSAIGHDV
GHPGVNNMFL VKLNAPLAQL YNDQSVLEAF HCAAYSQILR RHWPVAFQDK ALRKLMISTI
LATDMGIHSD YMQQLGNLQE KIHESKATDG WSPKDVDWAR TLACGLLIKC ADISNVARPW
LVAEKWTHLL QKEFAHQGEM EQAVGLETTL FGGPPELGNM LKLANGQIGF MTIFAHPLFA
NVADIIPAMR FAADEILTNK GVWFTRAEHE KKLQLIKKGT GPGDGGSISP RTQSPVGRVP
ESGKERHLPV SPLRGRGESP EKSIPESGRG RKGGNTTPHN SSRPSSLAAA AAIAIPGVDT
PHLHGSGSRS SQDLKASDRV RSGSALVNGE HIPLELTLDG TPIEENDGPT SSSTPRQGLS
ARDISSESLM AQVDTRRDNI VSMRAGAEAI PPEALQESRI SDAETMQKFK FATSKEDEPV
RTFDPEKTYS PSNPGIRASA PAGDTERKQT GRDGLMSSEN ENASGTKLRG GGGEEVLTPS
GSATSYASDK SEDVSRHQSS FQAVRNRAAS APLHSASPVL RPSFSMGSNS TTSREGSKYD
VHTTILSNGS LEGSSERDRK ASAKTMGRRR SRLKLGLAFW KRNRSDKSVE AGLERPDSQG
SGGY
//
