(data stored in ACNUC30567 zone)

HOGENOM: ACHLI_1_PE838

ID   ACHLI_1_PE838                        STANDARD;      PRT;   200 AA.
AC   ACHLI_1_PE838; A9NGK2;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Non-canonical purine NTP pyrophosphatase; EC=3.6.1
DE   19;AltName: Full=Non-standard purine NTP pyrophosphatase;AltName:
DE   Full=Nucleoside-triphosphate diphosphatase;AltName:
DE   Full=Nucleoside-triphosphate pyrophosphatase; Short=NTPase;
DE   (ACHLI_1.PE838).
GN   OrderedLocusNames=ACL_0869;
OS   ACHOLEPLASMA LAIDLAWII PG-8A.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Acholeplasma.
OX   NCBI_TaxID=441768;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACHLI_1.PE838.
CC       Acholeplasma laidlawii PG-8A chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:NTPA_ACHLI
CC   -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine
CC       nucleotides such as XTP and ITP/dITP to their respective
CC       monophosphate derivatives. Might exclude non-canonical purines
CC       from DNA precursor pool, thus preventing their incorporation into
CC       DNA and avoiding chromosomal lesions (By similarity).
CC   -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
CC       nucleotide + diphosphate.
CC   -!- COFACTOR: Binds 1 divalent metal cation ion per subunit; can use
CC       either magnesium or manganese (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the HAM1 NTPase family.
CC   -!- GENE_FAMILY: HOG000293319 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A9NGK2; -.
DR   EMBL; CP000896; ABX81482.1; -; Genomic_DNA.
DR   RefSeq; YP_001620858.1; NC_010163.1.
DR   ProteinModelPortal; A9NGK2; -.
DR   STRING; A9NGK2; -.
DR   GeneID; 5803384; -.
DR   GenomeReviews; CP000896_GR; ACL_0869.
DR   KEGG; acl:ACL_0869; -.
DR   OMA; GVYTADW; -.
DR   BioCyc; ALAI441768:ACL_0869-MON; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01405; Non_canon_purine_NTPase; 1; -.
DR   InterPro; IPR002637; Ham1p-like.
DR   InterPro; IPR020922; Nucleoside-triphosphatase.
DR   PANTHER; PTHR11067; Ham1p_like; 1.
DR   Pfam; PF01725; Ham1p_like; 1.
DR   TIGRFAMs; TIGR00042; TIGR00042; 1.
DR   HOGENOMDNA; ACHLI_1.PE838; -.
KW   Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding.
SQ   SEQUENCE   200 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDIIFASNNY HKFIEMESIL KPHQITLLKD FQIDEKEIIE SGLTFEANAQ IKARAFAKRF
     NQVAIADDSG IIIEAISPLP GIYSKRYSGL GDTVNNIKVL DVLKNKENRQ ARFVCAIAIA
     FPDGKIFTYV GNMLGNIALN LKGSMGFGYD PIFIPDGKQE TLGELGSTYK DEHSHRRHAL
     NNFLEAKDEI IDYWRYTWKK
//

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