ID   CPD1_CANAL              Reviewed;         246 AA.
AC   Q59PZ7; A0A1D8PTB3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase;
DE            Short=CPDase;
DE            EC=3.1.4.37;
GN   Name=CPD1; OrderedLocusNames=CAALFM_CR06690CA;
GN   ORFNames=CaO19.703, CaO19.8322;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017630; AOW31366.1; -; Genomic_DNA.
DR   RefSeq; XP_019331093.1; XM_019475548.1.
DR   AlphaFoldDB; Q59PZ7; -.
DR   STRING; 237561.Q59PZ7; -.
DR   GeneID; 3646624; -.
DR   KEGG; cal:CAALFM_CR06690CA; -.
DR   CGD; CAL0000174269; orf19.8322.
DR   VEuPathDB; FungiDB:CR_06690C_A; -.
DR   eggNOG; ENOG502RY6J; Eukaryota.
DR   HOGENOM; CLU_088289_0_0_1; -.
DR   InParanoid; Q59PZ7; -.
DR   OMA; FEPHITI; -.
DR   OrthoDB; 1620665at2759; -.
DR   PRO; PR:Q59PZ7; -.
DR   Proteomes; UP000000559; Chromosome R.
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..246
FT                   /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT                   /id="PRO_0000280675"
FT   REGION          133..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        40
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        188
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   246 AA;  28220 MW;  88AA0244CF418255 CRC64;
     MGVALWLCPK RNTPTYDKLI TVMSSLNTLF PGSPPKFEPH ITITTNISLD LADQSKTKDD
     VDRILSASAV AMNSLPKNHE SLVKLGNVNS QRKFFKKLYF EVEKDPNLVS FARIIRELFV
     IVPQDIEKEN IKQNPQLYTK DNNGNTIRRK PSKKKSKTTE VKEFDTSFIR QAAAYKAAEW
     SVQEFDPHIS LVYSDLWPLH SALWRNINTR ISDIDWDIEW EFGVLKLVLC EGDVNDWVVL
     GSVDIH