ID A0A1Y2AU50_9TREE Unreviewed; 1361 AA.
AC A0A1Y2AU50;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 28-JUN-2023, entry version 15.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=BCR39DRAFT_560921 {ECO:0000313|EMBL:ORY25747.1};
OS Naematelia encephala.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Naemateliaceae; Naematelia.
OX NCBI_TaxID=71784 {ECO:0000313|EMBL:ORY25747.1, ECO:0000313|Proteomes:UP000193986};
RN [1] {ECO:0000313|EMBL:ORY25747.1, ECO:0000313|Proteomes:UP000193986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=68-887.2 {ECO:0000313|EMBL:ORY25747.1,
RC ECO:0000313|Proteomes:UP000193986};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORY25747.1}.
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DR EMBL; MCFC01000054; ORY25747.1; -; Genomic_DNA.
DR STRING; 71784.A0A1Y2AU50; -.
DR InParanoid; A0A1Y2AU50; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000193986; 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:UP000193986}.
FT DOMAIN 628..1034
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 87..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1361 AA; 147204 MW; D16141553D538616 CRC64;
MSLTEIQLSP RDTTRSSAKR DLYIHPLHAD HSSPSLAVCA SRKPVMATPP LHLGGPSLSL
LVLLPSSAHM QQYHTPIVPV TRPHPLLSRQ SGSTIPSLKS IHSSSSGAER GGAPVQPIDG
VVNAGRRLSL APNIEAGTQT RLDSYSLSPS AFASSPISPK STPSRASANQ ASETPEASTS
TVPAFGSRRS TPGRAASGKR RPLTAVGAQD AGSLLGSHRA SVQMPLGMTP GGGSTGRTRP
GWEGDEIVGV LRGSGMEVTV IRHASHLPAI LSPKHSTAPT YASFSQQTLT TARLSSPDVG
LSHVILVPLC DSPSLPSLSI LLAQGTTPTA VCFQQDLLER AKRTEDEWLP SALEQISLVS
EMRERAARSS HKGSERPIVL AYSANPALAA TTIAACLSAG ASGVLKPPYD LSTAQLVKVM
VQAARESGIT STVERPSSNL LPTPQSIYTN LREGERRVVL PPTALSSGAE HEAEKVLNAA
VGSRKPSKSQ SPVVSRSRES SIAALYPRKA SLRTNHLFPH RPESPTSLLS GSDETFPEGD
HHLSTVTGMY WYHPSYTNRR RSVDVAGLAV ALRRAERAFL KSQLRKAPRG VLTANVKQGY
MFPGTPPSSA ALTNDSGYTD HPRSAQCEED SKDTQLAELL SAMYYQSQLA IDVRMSDYAA
LSAPLDSDQR HRLVAALSTW DFKPHHFDEG DLFRVAGIMF EGLLAMEGLR ELNVSRDQMN
RLLFAIRAIY HAPNPYHNYV HAIDVLQATY SFLIGIGVVP PWSYLRNLGP NSPAWEPPDE
LVMPVLGLGT RRARDVLRPQ DILAVVIAAM GHDVGHPGLS NAFMKNAKTP LSQVYEDKSV
LENMHCMLVV QLLRKHGFGF LFSTSPLERI PARAAIDTRG FRKVLYSSVL ATDMSLHFAW
MAELKKLNQT LSQEDEWDEG EDSTEADRIM ICQALIKCAD ISNPTRPIDV SEHWSSVLLK
EWAVQASLEQ DLHLPVSVIG SADAALQAKG QIGFIDLFTQ PLFEAVSDVL PELQCYADSC
ASNRQLWQSR LDHFMDEAAA DRSSTLIQPS VDGAAQDGRF RTLFPLLLPS PLVDSAALEP
GPAIIPTTTP SSVHTPTHTH PHTNTNTNVH PNQHGHTHTC SPASKAMRAV YHANLLDQPE
QCNGAGPSTS TIPVSLLEPS EPQSDADQIL AERDPSIREP EQESESTLKP LTTISWPPEP
DSSIFTDPLR REDPKPLRHA ELMRIATSPQ LRHLLNTTSL AQILRIIDSI LSPAARSSTL
SKLLGIDNDS LARPGESTLL SQRDSPPPLE ELLEAVAGGV STQKGEGEAG WWLGREGTKE
GRIWVGEEEK TLMRTWASVV CGAIDGNQGD AWGNGNLAWE V
//
