ID A0A0R3XC14_HYDTA Unreviewed; 483 AA.
AC A0A0R3XC14;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase {ECO:0000256|ARBA:ARBA00014478};
DE EC=3.1.4.37 {ECO:0000256|ARBA:ARBA00012317};
GN ORFNames=TTAC_LOCUS11074 {ECO:0000313|EMBL:VDM36054.1};
OS Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0001109101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TTAC_0001109101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM36054.1, ECO:0000313|Proteomes:UP000274429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000610};
CC -!- SUBUNIT: Exists as monomers and homodimers.
CC {ECO:0000256|ARBA:ARBA00011781}.
CC -!- SUBCELLULAR LOCATION: Melanosome {ECO:0000256|ARBA:ARBA00004223}.
CC Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CNPase
CC family. {ECO:0000256|ARBA:ARBA00008662}.
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DR EMBL; UYWX01022872; VDM36054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R3XC14; -.
DR STRING; 6205.A0A0R3XC14; -.
DR WBParaSite; TTAC_0001109101-mRNA-1; TTAC_0001109101-mRNA-1; TTAC_0001109101.
DR Proteomes; UP000046396; Unplaced.
DR Proteomes; UP000274429; Unassembled WGS sequence.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0009214; P:cyclic nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.90.1740.10; 2',3'-cyclic nucleotide 3'-phosphodiesterase superfamily; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR008431; CNPase.
DR InterPro; IPR047325; CNPase_cat.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10156; 2',3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR10156:SF0; 2',3'-CYCLIC-NUCLEOTIDE 3'-PHOSPHODIESTERASE; 1.
DR Pfam; PF13671; AAA_33; 1.
DR Pfam; PF05881; CNPase; 1.
DR SUPFAM; SSF55144; LigT-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW Reference proteome {ECO:0000313|Proteomes:UP000274429};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 314..429
FT /note="Cyclic nucleotide phosphodiesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF05881"
FT REGION 28..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 54403 MW; 06993D431DDF0F63 CRC64;
MGQTCVKLCS QSCVSRFLRG LGVRRPPPQR VENHLIEESS DDSNATGDNI KSPSKCKYVD
YPFLVNREIG EWIVFTKFMI ILRGPPGSGK SRLAGYIKMR FPTAHICSSD NYHSSSIKYF
EDYQFDSDRH ESALHDCEAE AKLYASRGIS PLVIDNANMR SYECRPYTEI ARAFDYNVIM
VIPRTPWRFD VRSLAEYNAH NLSAEMISSM VSQFEPIVYP LYYGWAFAGS PSSNTHLSIP
IEKGDKLLPN EVTEKMIKEF HDSFFSALDL PYVRKRLALI CGFNQDINRD QLATFWSSAV
NPWFGDVSEP YRTDKPARPH CTAFFAQHGH APGASEYAQK TAVREALLGS IDELCVEGLF
ITKRTVGLRI HLSDPDQLAL WGGLDNEPVD GHVTPQSRPQ GCRAHVTLAL ASGVPAVETG
FDALRIMDAE LRQLPDVYTA DMPDGILREL PISSSADSES LDNIFYYQYS TAKTIRLMYT
AFY
//