ID A0A094EXK3_9PEZI Unreviewed; 938 AA.
AC A0A094EXK3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=V498_08065 {ECO:0000313|EMBL:KFY83451.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY83451.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY83451.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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}.
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:KFY83451.1}.
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DR EMBL; JPKA01002635; KFY83451.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EXK3; -.
DR HOGENOM; CLU_010668_3_0_1; -.
DR Proteomes; UP000029270; 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}.
FT DOMAIN 291..643
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 94..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 653..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..881
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..912
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 101927 MW; 2E32405A4E3F04E6 CRC64;
MDAACNVVYV DRGARQERLV RRGEVLTEVA RSGGDADADE GARRLQVNVH TLLGTFNKVY
VCPTGLSCLA RIARLNSGPT ADRVPTLALI DIPEDDDDNE RKVPVPVPIE EDEPLQEGEN
DAGEVSSART VGEEPGVPNL YGSHLIRQIT TDTKQQGVAN IVLSVAVARR SVEIPSSTPS
TPTPTSRYSA SNQPPSPAAM RLPPNQTSDM KYVDLGAVDV LDNPINRESL PSLAIHIYRV
HKEFERRGRH LQAPTQKHES PWPGVPTPYP FPYLREVMVQ DLAGQICGTI VDHPLDPVVI
DIGEGDQRVI TNAIGDWNFS AHDLDDNGLL FATVRMLEHA LQMEGMEEWR LPTDELLNFV
VASRNGYNDF VPYHNFRHVV DVLQAVFLLL VRIGALPPFP PGASIETEPK SKLVKLLRPF
EALTLLIAAI GHDIGHPGVN NMFLVKSKAP LASLYNDKSV LESYHAAVYC QLLKRLWPAV
VKNEEMKVLL TSCILSTDMG IHNQYMEKLE KLQESMQNLS DDDEIQNSDL VTYRHVACNL
LIKCADISNV ARPFLCASVW TAILTEEFAR QASMEEKIQL IPSTLFAPPA TEIISLGKSQ
TGFMSFYALP LFTGVADLMP TTDFCVKEIE SNKREWEDRI RIEEARLRAI REQRAREEAA
QQQARDREGS DDSVDSNNPP TAPAAESSAT GAAAGTSSGG PSGSSGAASG GQSSSAPSGG
QDSADVPPAL VRGQQPQSSS RPNSSSVTWD EASANSRPVT SSSARRVLDT SQVVTHRRSE
TTDGSASVPE SGGWEGSART GDSGKSEEKA ECISTARTSV ESTGMRGVNG VNGVNGTKRK
SLVNSVSTPD LRSDSKGRMM RGESGGRERD HHHRKKGDKG DGSGVFASMR ELSRRPSLGK
FKFWKKREAG GFGPKETQIP PMPNVMGRRG REGGVSAG
//
