ID   CPD1_YARLI              Reviewed;         216 AA.
AC   Q6CGD3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase;
DE            Short=CPDase;
DE            EC=3.1.4.37;
GN   Name=CPD1; OrderedLocusNames=YALI0A20295g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382127; CAG84217.2; -; Genomic_DNA.
DR   RefSeq; XP_500279.2; XM_500279.2.
DR   AlphaFoldDB; Q6CGD3; -.
DR   SMR; Q6CGD3; -.
DR   STRING; 4952.CAG84217; -.
DR   EnsemblFungi; CAG84217; CAG84217; YALI0_A20295g.
DR   GeneID; 2906534; -.
DR   KEGG; yli:YALI0A20295g; -.
DR   VEuPathDB; FungiDB:YALI0_A20295g; -.
DR   HOGENOM; CLU_088289_0_0_1; -.
DR   InParanoid; Q6CGD3; -.
DR   OMA; FEPHITI; -.
DR   Proteomes; UP000001300; Chromosome A.
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_0000280681"
FT   ACT_SITE        39
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        153
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   216 AA;  24632 MW;  289153FDB9F84770 CRC64;
     MGTSLWLQPP RNSPIWQQLA TTIQGLKPIF SDSENFEPHI TLTSNISVNT QGQVDFVLDR
     AVAAAKCVPQ GFQIHLSSVK YGSRFFKKVY LQVEPTPELL SLARICREDF VYMPEAMSQA
     RNYQAMSAEE RQKIDTQVGQ RAAEWTRNEY DPHVSLVYSD LYPVEDADRR TIETRLEDTF
     GSGYDESGLG WKNGRFALVR CEGPVDEWEV LGVRDF