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Database: UniProt
Entry: A0A3B3REL7_9TELE
LinkDB: A0A3B3REL7_9TELE
Original site: A0A3B3REL7_9TELE 
ID   A0A3B3REL7_9TELE        Unreviewed;       368 AA.
AC   A0A3B3REL7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase {ECO:0000256|ARBA:ARBA00016378};
DE            EC=3.6.1.13 {ECO:0000256|ARBA:ARBA00012453};
DE            EC=3.6.1.16 {ECO:0000256|ARBA:ARBA00012443};
DE            EC=3.6.1.53 {ECO:0000256|ARBA:ARBA00012529};
DE   AltName: Full=ADPRibase-Mn {ECO:0000256|ARBA:ARBA00032579};
DE   AltName: Full=CDP-choline phosphohydrolase {ECO:0000256|ARBA:ARBA00030848};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000016839.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000016839.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC         Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC         EC=3.6.1.13; Evidence={ECO:0000256|ARBA:ARBA00001454};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC         Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC         EC=3.6.1.53; Evidence={ECO:0000256|ARBA:ARBA00001583};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP-choline + H2O = CMP + 2 H(+) + phosphocholine;
CC         Xref=Rhea:RHEA:32487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58779, ChEBI:CHEBI:60377, ChEBI:CHEBI:295975;
CC         EC=3.6.1.53; Evidence={ECO:0000256|ARBA:ARBA00001789};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP-glycerol + H2O = CMP + 2 H(+) + sn-glycerol 3-phosphate;
CC         Xref=Rhea:RHEA:21692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:58311, ChEBI:CHEBI:60377; EC=3.6.1.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001209};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the ADPRibase-Mn family.
CC       {ECO:0000256|ARBA:ARBA00006362}.
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DR   AlphaFoldDB; A0A3B3REL7; -.
DR   STRING; 1676925.ENSPKIP00000016839; -.
DR   Ensembl; ENSPKIT00000041340.1; ENSPKIP00000016839.1; ENSPKIG00000002994.1.
DR   GeneTree; ENSGT00390000014667; -.
DR   OrthoDB; 276166at2759; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047734; F:CDP-glycerol diphosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07396; MPP_Nbla03831; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041869; MPP_ADPRM.
DR   PANTHER; PTHR16509; -; 1.
DR   PANTHER; PTHR16509:SF1; MANGANESE-DEPENDENT ADP-RIBOSE_CDP-ALCOHOL DIPHOSPHATASE; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          48..314
FT                   /note="Calcineurin-like phosphoesterase"
FT                   /evidence="ECO:0000259|Pfam:PF00149"
SQ   SEQUENCE   368 AA;  42733 MW;  54CFDCE3B3ED27F2 CRC64;
     MFNFKCPFRN KCVSERRVVG WWTKHEGLSS RLISRASKMD DSIQPLFTFG VIADIQYADI
     DDGYNFTHTR KRYYRNSLQL LRRANEKWKT ETVQPSFILQ LGDIIDGFNK KYEASQKALD
     TVLTEFDRTG IAVHHVWGNH EFYNFSRQDL ITSLNSQNTD FAMREDEIKQ KHPDNEQSYA
     YHFSPAPNFR FVVLDAYDVS LIGRQENSEQ YNQALKILQE HNGNYDLNQP PAYSGLEQRF
     VKFNGGFGQD QLEWLDRLLS LSDQKLEKVT IVSHLPIHPS STDPVCLAWN YDDVLSILYS
     HKSVVCFMAG HDHDGGYHQD ISGIHHLTFE GVIETRPNND AFGTVYVYED RMKLKGNGRV
     PHRSLNYE
//
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