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Database: UniProt
Entry: A0A091VY44_NIPNI
LinkDB: A0A091VY44_NIPNI
Original site: A0A091VY44_NIPNI 
ID   A0A091VY44_NIPNI        Unreviewed;       428 AA.
AC   A0A091VY44;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=nucleoside diphosphate phosphatase {ECO:0000256|ARBA:ARBA00038863};
DE            EC=3.6.1.6 {ECO:0000256|ARBA:ARBA00038863};
DE   AltName: Full=Guanosine-diphosphatase ENTPD5 {ECO:0000256|ARBA:ARBA00042111};
DE   AltName: Full=Uridine-diphosphatase ENTPD5 {ECO:0000256|ARBA:ARBA00042507};
GN   ORFNames=Y956_12018 {ECO:0000313|EMBL:KFR08114.1};
OS   Nipponia nippon (Crested ibis) (Ibis nippon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC   Nipponia.
OX   NCBI_TaxID=128390 {ECO:0000313|EMBL:KFR08114.1, ECO:0000313|Proteomes:UP000053283};
RN   [1] {ECO:0000313|EMBL:KFR08114.1, ECO:0000313|Proteomes:UP000053283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFR08114.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036163};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437;
CC         Evidence={ECO:0000256|ARBA:ARBA00036163};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58069, ChEBI:CHEBI:60377; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036856};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881;
CC         Evidence={ECO:0000256|ARBA:ARBA00036856};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036354};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157;
CC         Evidence={ECO:0000256|ARBA:ARBA00036354};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036844};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208;
CC         Evidence={ECO:0000256|ARBA:ARBA00036844};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00036381};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877;
CC         Evidence={ECO:0000256|ARBA:ARBA00036381};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC         phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00035811};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800;
CC         Evidence={ECO:0000256|ARBA:ARBA00035811};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC       {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR   EMBL; KL411498; KFR08114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091VY44; -.
DR   STRING; 128390.A0A091VY44; -.
DR   eggNOG; KOG1385; Eukaryota.
DR   Proteomes; UP000053283; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF35; NUCLEOSIDE DIPHOSPHATE PHOSPHATASE ENTPD5; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003833};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053283};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..428
FT                   /note="nucleoside diphosphate phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001881773"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT   BINDING         202..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ   SEQUENCE   428 AA;  48092 MW;  1E54EF565CC2086C CRC64;
     MAFSRLLILL ALAFSSLSFV LSHSNREMWF QDFFPPNMCP INAKANTFYG IMFDAGSTGT
     RIHIYTFVQK SPENLPELEG EIFESVKPGL SAYADQPEKG AETVKRLLDM AIDAVPPHLW
     EKTPVVLKAT AGLRLLSEEK AQALLLEVRE VFEESPFLVP EDSVSIMDGS YEGILAWITV
     NFLTGQLSGQ NQHTVGTLDL GGASTQITFL PRFEETLKET PGDFLTSFEM FNSTYKLYTH
     SYLGFGLKAA RLATLGALDM EAVDGQMFRS SCLPKQLEAE WHFGGVKYRY GGNKEGETGF
     KPCYLEVLKV VKGKLHQPDE IRGSSFYAFS YYYDRAVDTN LIDYEQGGVL EVKDFERKAK
     EVCDNMERYK SASPFLCMDL TYITALLKEG FGFRDNTLLQ LTKKVNNIET SWTLGATFHL
     LQSLGITY
//
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