ID   CPD1_DEBHA              Reviewed;         237 AA.
AC   Q6BGW3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase;
DE            Short=CPDase;
DE            EC=3.1.4.37;
GN   Name=CPD1; OrderedLocusNames=DEHA2G23430g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382139; CAG91069.2; -; Genomic_DNA.
DR   RefSeq; XP_462558.2; XM_462558.2.
DR   AlphaFoldDB; Q6BGW3; -.
DR   STRING; 4959.XP_462558.2; -.
DR   EnsemblFungi; CAG91069; CAG91069; DEHA2G23430g.
DR   GeneID; 2905514; -.
DR   KEGG; dha:DEHA2G23430g; -.
DR   VEuPathDB; FungiDB:DEHA2G23430g; -.
DR   eggNOG; ENOG502RY6J; Eukaryota.
DR   HOGENOM; CLU_088289_0_0_1; -.
DR   InParanoid; Q6BGW3; -.
DR   OMA; FEPHITI; -.
DR   OrthoDB; 1620665at2759; -.
DR   Proteomes; UP000000599; Chromosome G.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IEA:UniProtKB-EC.
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..237
FT                   /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT                   /id="PRO_0000280677"
FT   REGION          117..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        21
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        167
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   237 AA;  26816 MW;  21E9D4DA5627A12E CRC64;
     MTLMSSLNTL FPGQPPKFEP HITISSNIDV DLDHPDKTKS DVYRILSASL VAIDSLPKNH
     SNLVTLGKVD SQRKFFKKLY FQVARDPNLV SFATIIRELF VQLPADIEQE NMKKNPHLYT
     TDSHGNTVKK KSKQSQDGRI EAIDMPRIQS EAQEQASLWS VTEFDPHLSL VYNDLHPIDS
     ALWRTIKTRI QDYLNIDNCD SDDLTDNGLG WDNGILKLVL CEGDVNDWVV LGSADLH