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Protein

Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase

Gene

adprm

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-choline and CDP-ethanolamine, but not other non-reducing ADP-sugars or CDP-glucose.By similarity

Catalytic activityi

CDP-choline + H2O = CMP + phosphocholine.
ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate.
CDP-glycerol + H2O = CMP + sn-glycerol 3-phosphate.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi13Zinc 1By similarity1
Metal bindingi15Zinc 1By similarity1
Metal bindingi60Zinc 1By similarity1
Metal bindingi60Zinc 21 Publication1
Metal bindingi96Zinc 21 Publication1
Metal bindingi228Zinc 21 Publication1
Metal bindingi265Zinc 21 Publication1
Metal bindingi267Zinc 1By similarity1

GO - Molecular functioni

  • 2',3'-cyclic-nucleotide 2'-phosphodiesterase activity Source: ZFIN
  • ADP-ribose diphosphatase activity Source: ZFIN
  • CDP-glycerol diphosphatase activity Source: ZFIN
  • manganese ion binding Source: ZFIN
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase (EC:3.6.1.13, EC:3.6.1.16, EC:3.6.1.53)
Alternative name(s):
ADPRibase-Mn
CDP-choline phosphohydrolase
Gene namesi
Name:adprm
ORF Names:zgc:64213
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Unplaced

Organism-specific databases

ZFINiZDB-GENE-040426-1406. adprm.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002865701 – 322Manganese-dependent ADP-ribose/CDP-alcohol diphosphataseAdd BLAST322

Proteomic databases

PaxDbiQ7T291.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi7955.ENSDARP00000096471.

Structurei

Secondary structure

1322
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 11Combined sources7
Beta strandi27 – 31Combined sources5
Helixi35 – 49Combined sources15
Beta strandi53 – 57Combined sources5
Helixi65 – 68Combined sources4
Helixi72 – 84Combined sources13
Beta strandi88 – 92Combined sources5
Helixi96 – 101Combined sources6
Helixi104 – 108Combined sources5
Helixi127 – 129Combined sources3
Beta strandi134 – 139Combined sources6
Beta strandi142 – 146Combined sources5
Beta strandi154 – 157Combined sources4
Helixi162 – 174Combined sources13
Beta strandi187 – 189Combined sources3
Helixi190 – 193Combined sources4
Helixi203 – 219Combined sources17
Beta strandi222 – 229Combined sources8
Helixi238 – 240Combined sources3
Helixi245 – 253Combined sources9
Beta strandi258 – 263Combined sources6
Beta strandi270 – 273Combined sources4
Beta strandi279 – 282Combined sources4
Helixi286 – 288Combined sources3
Beta strandi295 – 301Combined sources7
Beta strandi303 – 312Combined sources10
Beta strandi317 – 320Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NXFX-ray1.70A2-322[»]
ProteinModelPortaliQ7T291.
SMRiQ7T291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7T291.

Family & Domainsi

Sequence similaritiesi

Belongs to the ADPRibase-Mn family.Curated

Phylogenomic databases

eggNOGiENOG410IJ2N. Eukaryota.
COG1409. LUCA.
HOGENOMiHOG000154875.
HOVERGENiHBG100432.
InParanoidiQ7T291.
KOiK01517.
PhylomeDBiQ7T291.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7T291-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDPVFTFGL IADVQYADIE DGENYLRTRR RYYRGSADLL RDAVLQWRRE
60 70 80 90 100
RVQCVVQLGD IIDGHNRRRD ASDRALDTVM AELDACSVDV HHVWGNHEFY
110 120 130 140 150
NFSRPSLLSS RLNSAQRTGT DTGSDLIGDD IYAYEFSPAP NFRFVLLDAY
160 170 180 190 200
DLSVIGREEE SEKHTHSWRI LTQHNHNLQD LNLPPVSVGL EQRFVKFNGG
210 220 230 240 250
FSEQQLQWLD AVLTLSDHKQ ERVLIFSHLP VHPCAADPIC LAWNHEAVLS
260 270 280 290 300
VLRSHQSVLC FIAGHDHDGG RCTDSSGAQH ITLEGVIETP PHSHAFATAY
310 320
LYEDRMVMKG RGRVEDLTIT YS
Length:322
Mass (Da):36,645
Last modified:October 1, 2003 - v1
Checksum:i8C2BB1A16650934F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC054642 mRNA. Translation: AAH54642.1.
RefSeqiNP_956715.1. NM_200421.1.
UniGeneiDr.82669.

Genome annotation databases

GeneIDi393393.
KEGGidre:393393.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC054642 mRNA. Translation: AAH54642.1.
RefSeqiNP_956715.1. NM_200421.1.
UniGeneiDr.82669.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NXFX-ray1.70A2-322[»]
ProteinModelPortaliQ7T291.
SMRiQ7T291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7955.ENSDARP00000096471.

Proteomic databases

PaxDbiQ7T291.

Protocols and materials databases

DNASUi393393.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi393393.
KEGGidre:393393.

Organism-specific databases

CTDi56985.
ZFINiZDB-GENE-040426-1406. adprm.

Phylogenomic databases

eggNOGiENOG410IJ2N. Eukaryota.
COG1409. LUCA.
HOGENOMiHOG000154875.
HOVERGENiHBG100432.
InParanoidiQ7T291.
KOiK01517.
PhylomeDBiQ7T291.

Miscellaneous databases

EvolutionaryTraceiQ7T291.
PROiQ7T291.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_ApaH.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiADPRM_DANRE
AccessioniPrimary (citable) accession number: Q7T291
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 1, 2003
Last modified: November 30, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.