ID G8YUS7_PICSO Unreviewed; 621 AA.
AC G8YUS7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=Piso0_000197 {ECO:0000313|EMBL:CCE72610.1};
GN ORFNames=GNLVRS01_PISO0A04070g {ECO:0000313|EMBL:CCE72610.1};
OS Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS 10061 / NRRL Y-12695) (Hybrid yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE72610.1, ECO:0000313|Proteomes:UP000005222};
RN [1] {ECO:0000313|Proteomes:UP000005222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX DOI=10.1534/g3.111.000745;
RA Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT genome resolution following polyploidization.";
RL G3 (Bethesda) 2:299-311(2012).
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; FO082059; CCE72610.1; -; Genomic_DNA.
DR AlphaFoldDB; G8YUS7; -.
DR STRING; 559304.G8YUS7; -.
DR eggNOG; KOG3689; Eukaryota.
DR HOGENOM; CLU_028903_0_0_1; -.
DR InParanoid; G8YUS7; -.
DR OMA; FISHFAD; -.
DR Proteomes; UP000005222; Chromosome A.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005222}.
FT DOMAIN 207..621
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
SQ SEQUENCE 621 AA; 70741 MW; 9FD4A8F11ECED013 CRC64;
MTEVLRLRYR RSERKQTEIS GYDNLEKSEE RMFGRFGELI EFLYRKGNSE EDSAHATVVV
VDESRKRDGN TLDGLPYEDK KALLRFFFGH LNMIVVSYED LNHPDIVKDI NRISRCVEMM
SVTRSGRVAT WTGAGKCCAQ SSVHCDSVMP ISPQPLNETP KEQANLDCQG SAVIDVVQSM
TSMLRTTLGQ MELTFERRQH FYRLITQEID FLRILSNSSR SHLSRLCHAV GQWSFPAHEL
SNDDLVYCVF LMLKFSLDYY VSECSSDIPQ GLHIPSSNEL LALIFTVRDT YNNGNPFHNF
RHAADVLQAC FYYLVRLKCL PSFEQLAADP NGEEMNVFTY TFDNKEPTIL VPKADQGDSS
RGVSSSGAEQ KLEDDLKTLS HLKPLQSFSL LLAALGHDVG HPGVTNAFLT KYNTPTSMLY
NDRSVLESFH ACVFVNRILL VAWPDLLTVV VEEESKYTVR NLIVSSILAT DMAEHFDYVR
QLTCYKSFHN KKLCQGSNHL DYVKLTTSLL IKCADISNVT RPLRVSSQWA LVLAREFDEI
AHMESVLSAS LQHVSIPTIY PKIPYQVEDV LRVRPDLRNG QIFFIDTFAE SLFGSVSDAW
PQLTYTKDII YSNKSFWINF S
//
