ID AP4A_BOVIN Reviewed; 147 AA.
AC Q29RJ1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 29-MAY-2013, entry version 54.
DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical];
DE EC=3.6.1.17;
DE AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase;
DE Short=Ap4A hydrolase;
DE Short=Ap4Aase;
DE Short=Diadenosine tetraphosphatase;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 2;
DE Short=Nudix motif 2;
GN Name=NUDT2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Asymmetrically hydrolyzes Ap4A to yield AMP and ATP.
CC Plays a major role in maintaining homeostasis.
CC -!- CATALYTIC ACTIVITY: P(1),P(4)-bis(5'-guanosyl) tetraphosphate +
CC H(2)O = GTP + GMP.
CC -!- COFACTOR: Divalent ions (By similarity).
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC -!- SIMILARITY: Contains 1 nudix hydrolase domain.
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DR EMBL; BC114149; AAI14150.1; -; mRNA.
DR IPI; IPI00742579; -.
DR RefSeq; NP_001070570.1; NM_001077102.1.
DR UniGene; Bt.2818; -.
DR ProteinModelPortal; Q29RJ1; -.
DR SMR; Q29RJ1; 1-144.
DR STRING; 9913.ENSBTAP00000042493; -.
DR PRIDE; Q29RJ1; -.
DR Ensembl; ENSBTAT00000045076; ENSBTAP00000042493; ENSBTAG00000031793.
DR GeneID; 768044; -.
DR KEGG; bta:768044; -.
DR CTD; 318; -.
DR eggNOG; COG0494; -.
DR GeneTree; ENSGT00390000002416; -.
DR HOGENOM; HOG000261976; -.
DR HOVERGEN; HBG002853; -.
DR InParanoid; Q29RJ1; -.
DR KO; K01518; -.
DR OMA; WDFPKGN; -.
DR OrthoDB; EOG4FTW20; -.
DR BioCyc; CATTLE:768044-MONOMER; -.
DR NextBio; 20918399; -.
DR GO; GO:0005739; C:mitochondrion; IEA:Compara.
DR GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IEA:EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.79.10; -; 1.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR015797; NUDIX_hydrolase_dom-like.
DR InterPro; IPR003565; Tetra_PHTase.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR PRINTS; PR01405; TETRPHPHTASE.
DR SUPFAM; SSF55811; NUDIX_hydrolase; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Complete proteome; GTP-binding; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 147 Bis(5'-nucleosyl)-tetraphosphatase
FT [asymmetrical].
FT /FTId=PRO_0000260767.
FT DOMAIN 1 139 Nudix hydrolase.
FT MOTIF 43 64 Nudix box.
FT MOD_RES 2 2 N-acetylalanine (By similarity).
SQ SEQUENCE 147 AA; 16775 MW; 1BC4523DF285D130 CRC64;
MALRACGLII FRRRLIPKVD NTAIEFLLLQ ASDGIHHWTP PKGHVEPGES DLETALRETQ
EEAGIEAGQL TIIEGFRREL SYVARAKPKI VIYWLAEVKD CDVEVRLSRE HQAYRWLELE
DACQLAQFEE MKAALQEGHQ FLCSTAT
//
