ID   CPD1_NEUCR              Reviewed;         212 AA.
AC   Q7S724; V5IKP0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase;
DE            Short=CPDase;
DE            EC=3.1.4.37;
GN   Name=cpd-7; Synonyms=cpd1; ORFNames=NCU05539;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; CM002241; ESA42188.1; -; Genomic_DNA.
DR   EMBL; CM002241; ESA42189.1; -; Genomic_DNA.
DR   RefSeq; XP_011394956.1; XM_011396654.1.
DR   RefSeq; XP_011394957.1; XM_011396655.1.
DR   AlphaFoldDB; Q7S724; -.
DR   SMR; Q7S724; -.
DR   STRING; 5141.EFNCRP00000005508; -.
DR   EnsemblFungi; ESA42188; ESA42188; NCU05539.
DR   EnsemblFungi; ESA42189; ESA42189; NCU05539.
DR   GeneID; 3876648; -.
DR   KEGG; ncr:NCU05539; -.
DR   VEuPathDB; FungiDB:NCU05539; -.
DR   HOGENOM; CLU_108991_1_0_1; -.
DR   InParanoid; Q7S724; -.
DR   Proteomes; UP000001805; Chromosome 5, Linkage Group VI.
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..212
FT                   /note="2',3'-cyclic-nucleotide 3'-phosphodiesterase"
FT                   /id="PRO_0000280679"
FT   ACT_SITE        51
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        146
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   212 AA;  23721 MW;  3B522B1CC2491F53 CRC64;
     MPGSSLWLIP PPSHPLYPIL SFLISQHLPS DFPSEAGAAD ARLIPEFFAP HMTLSSGISP
     DLYGDDPQRW LDSIPWPSAD EVQVRFEGIS SQDTYYRRCY ARVKLDEGIK KIAGLARARG
     VNGEDDAKGA KTQEWLEWWR KEFGPHVSLM YGDVPISDDR LKEVAKVVEE AGVKLAEPEG
     NVEGNGWNGG VVWLVPTDRD IRDWKPIAKR VL