(data stored in SCRATCH zone)

SWISSPROT: Q3Z4R7_SHISS

ID   Q3Z4R7_SHISS            Unreviewed;       550 AA.
AC   Q3Z4R7;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 88.
DE   SubName: Full=UDP-sugar hydrolase {ECO:0000313|EMBL:AAZ87245.1};
GN   Name=ushA {ECO:0000313|EMBL:AAZ87245.1};
GN   OrderedLocusNames=SSON_0469 {ECO:0000313|EMBL:AAZ87245.1};
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ87245.1, ECO:0000313|Proteomes:UP000002529};
RN   [1] {ECO:0000313|EMBL:AAZ87245.1, ECO:0000313|Proteomes:UP000002529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046 {ECO:0000313|EMBL:AAZ87245.1,
RC   ECO:0000313|Proteomes:UP000002529};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC       {ECO:0000256|RuleBase:RU362119}.
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DR   EMBL; CP000038; AAZ87245.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87245; AAZ87245; SSON_0469.
DR   KEGG; ssn:SSON_0469; -.
DR   HOGENOM; HOG000247216; -.
DR   KO; K11751; -.
DR   OMA; KRLFKPY; -.
DR   BioCyc; SSON300269:G1GL2-539-MONOMER; -.
DR   Proteomes; UP000002529; Chromosome.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; -; 1.
DR   InterPro; IPR008334; 5'-Nucleotdase_C.
DR   InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR   InterPro; IPR006146; 5'-Nucleotdase_CS.
DR   InterPro; IPR006179; 5_nucleotidase/apyrase.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR11575; PTHR11575; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; SSF55816; 1.
DR   PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR   PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3Z4R7.
DR   SWISS-2DPAGE; Q3Z4R7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002529};
KW   Hydrolase {ECO:0000256|RuleBase:RU362119,
KW   ECO:0000313|EMBL:AAZ87245.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW   Signal {ECO:0000256|RuleBase:RU362119}.
FT   SIGNAL        1     25       {ECO:0000256|RuleBase:RU362119}.
FT   CHAIN        26    550       {ECO:0000256|RuleBase:RU362119}.
FT                                /FTId=PRO_5005143212.
FT   DOMAIN       35    254       Metallophos. {ECO:0000259|Pfam:PF00149}.
FT   DOMAIN      363    509       5_nucleotid_C. {ECO:0000259|Pfam:
FT                                PF02872}.
SQ   SEQUENCE   550 AA;  60806 MW;  701B88A37B22FD39 CRC64;
     MKLLQRGVAL ALLTTFTLAS ETALAYEQDK TYKITVLHTN DHHGHFWRNE YGEYGLAAQK
     TLVDGIRKEV AAEGGSVLLL SGGDINTGVP ESDLQDAEPD FRGMNLVGYD AMAIGNHEFD
     NPLTVLRQQE KWAKFPLLSA NIYQKSTGER LFKPWALFKR QDLKIAVIGL TTDDTAKIGN
     PEYFTDIEFR KPADEAKLVI QELQQTEKPD IIIAATHMGH YDNGEHGSNA PGDVEMARAL
     PAGSLAMIVG GHSQDPVCMA AENKKQVDYV PGTPCKPDQQ NGIWIVQAHE WGKYVGRADF
     EFRNGEMKMV NYQLIPVNLK KKVTREDGKS ERVLYTPEIA ENQQMISLLS PFQNKGKAQL
     EVKIGETNGR LEGDRDKVRF VQTNMGRLIL AAQMDRTGAD FAVMSGGGIR DSIEAGDISY
     KNVLKVQPFG NVVVYADMIG KEVIDYLTAV AQMKPDSGAY PQFANVSFVA KDGKLNDLKI
     KGEPVDPAKT YRMATLNFNA TGGDGYPRLD NKPGYVNTGF IDAEVLKAYI QKSSPLDVSV
     YEPKGEVSWQ
//

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