CPD1_ASHGO
ID CPD1_ASHGO Reviewed; 216 AA.
AC Q758H6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase;
DE Short=CPDase;
DE EC=3.1.4.37;
GN Name=CPD1; OrderedLocusNames=AEL214C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Involved in the metabolism of ADP-ribose 1',2'-cyclic
CC phosphate which is produced as a consequence of tRNA splicing.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-
CC phosphate + H(+); Xref=Rhea:RHEA:14489, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:66954, ChEBI:CHEBI:78552; EC=3.1.4.37;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CPD1 family.
CC {ECO:0000305}.
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DR EMBL; AE016818; AAS52471.1; -; Genomic_DNA.
DR RefSeq; NP_984647.1; NM_210000.1.
DR AlphaFoldDB; Q758H6; -.
DR SMR; Q758H6; -.
DR STRING; 33169.AAS52471; -.
DR EnsemblFungi; AAS52471; AAS52471; AGOS_AEL214C.
DR GeneID; 4620829; -.
DR KEGG; ago:AGOS_AEL214C; -.
DR eggNOG; ENOG502RY6J; Eukaryota.
DR HOGENOM; CLU_088289_0_0_1; -.
DR OMA; ANSPCYD; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0009187; P:cyclic nucleotide metabolic process; IBA:GO_Central.
DR InterPro; IPR012386; Cyclic-nucl_3Pdiesterase.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR PANTHER; PTHR28141; PTHR28141; 1.
DR Pfam; PF07823; CPDase; 1.
DR SUPFAM; SSF55144; SSF55144; 1.
PE 3: Inferred from homology;
KW Golgi apparatus; Hydrolase; Reference proteome.
FT CHAIN 1..216
FT /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT /id="PRO_0000280674"
FT ACT_SITE 39
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 137
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 216 AA; 23536 MW; D25A00FC5A81327D CRC64;
MAVALWYCPP ANSPCYDTVN SLILSLQTLF PDAVLFEPHV TITSQLRCDS ADDAAAVLAA
ACAALRACRP QLDARGSPVV RFDAVAVGRR YFDKVHLACA HDRFLYGVAQ VIRELFVQDP
PDPAAAADWV HSSFRPHLSL VYSDLYHVDQ ALLRVLRQRI GDALGAALLP HPPAPGLQAL
WALQPPLDGW SIPGSFKVVR CEGPVRDWHV LAAADL
