ID A0A1Y1YPY4_9FUNG Unreviewed; 777 AA.
AC A0A1Y1YPY4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=K493DRAFT_279121 {ECO:0000313|EMBL:ORY00083.1};
OS Basidiobolus meristosporus CBS 931.73.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC Basidiobolus.
OX NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORY00083.1, ECO:0000313|Proteomes:UP000193498};
RN [1] {ECO:0000313|EMBL:ORY00083.1, ECO:0000313|Proteomes:UP000193498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORY00083.1,
RC ECO:0000313|Proteomes:UP000193498};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:ORY00083.1}.
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DR EMBL; MCFE01000088; ORY00083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1YPY4; -.
DR STRING; 1314790.A0A1Y1YPY4; -.
DR InParanoid; A0A1Y1YPY4; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000193498; 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:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; SSF52172; CheY-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000193498}.
FT DOMAIN 1..54
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 402..769
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 171..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..93
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 357..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 777 AA; 88084 MW; E5B45A8E1C81AFF6 CRC64;
MVRSTEALKD LPVIMMADPE QLELACNCLQ LGADDYVLKP VRLETVKTVW RSVWRKRKEQ
KVILMLEEER NKRKSLELAV DKLQDQMLQA IETPINLITR TVTDLLQSTG MSDEAKNTLA
SILSSLKSTN LYRPAFEKLL HNENLNAETR NWLSSEVIKD APLSIPPEGV NLDKSRFSRP
SRHRRASSLE GSTNSLFNEN NFWPSDTWDY SRINVSEISP DYRSMRNHSY YHSLNNRRNS
DTQQLTRFAS GLRSRRQRIH SIHDQVSNEE PFGPQGPSLN YLLEMPGLEN EESIDDLKYE
TGLKHDYPYD QTLENIPEYC PDGDEDSNGM AETLVEQTLD TDEVASLPVE SLPITEATTD
RNSPSKCMTT NHHGLSLDPE LRPKEELAQI TTVPPTPTSD VEYTETPLSP STLYPKPQRA
TLLNSWEFDV WSYTETELLP FLVDIFNELG FIEHYSIPLE TLTSFFHAVK DGYNTSQNPY
HNFRHAFDVT QAGYLFLREA CCNLDLVTAA STANKDPVCA VSDTESATKP SGTGASDNVL
EGSEGYVFTM NERFAFIIAC LCHDLSHDGH TNNFHVATSS ELAVLYNDSS VLENFHAHQT
FVLLRTLPEA NILSNLPASV VAELRSIIIK CILATDMGKH MEVMANFNEC VTSGWRWDDR
SHRLRLLEML MKCADISNTV RPLHLARVWS DLIQEEMFNQ GDEERDIQLP VSAFGDRENP
QQPRLAITFA DFVATPLFKA IAGILPSISV HVSSCHATRE YWNVYMREKS SRTATPT
//
