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Database: UniProt
Entry: A0A0J6YU48_9BACT
LinkDB: A0A0J6YU48_9BACT
Original site: A0A0J6YU48_9BACT 
ID   A0A0J6YU48_9BACT        Unreviewed;       458 AA.
AC   A0A0J6YU48;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-OCT-2017, entry version 10.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=UR09_06095 {ECO:0000313|EMBL:KMP10488.1};
OS   Nitrospina sp. SCGC_AAA799_A02.
OC   Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinae; Nitrospinia;
OC   Nitrospinales; Nitrospinaceae; Nitrospina.
OX   NCBI_TaxID=1628278 {ECO:0000313|EMBL:KMP10488.1, ECO:0000313|Proteomes:UP000035948};
RN   [1] {ECO:0000313|EMBL:KMP10488.1, ECO:0000313|Proteomes:UP000035948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC_AAA799_A02 {ECO:0000313|EMBL:KMP10488.1};
RA   Ngugi D.K., Blom J., Stepanauskas R., Stingl U.;
RT   "Diversification and niche adaptations of Nitrospina-like bacteria in
RT   the poly-extreme interfaces of the Atlantis II Deep brine from the Red
RT   Sea.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KMP10488.1}.
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DR   EMBL; JZKI01000065; KMP10488.1; -; Genomic_DNA.
DR   EnsemblBacteria; KMP10488; KMP10488; UR09_06095.
DR   PATRIC; fig|1628278.3.peg.1264; -.
DR   Proteomes; UP000035948; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KMP10488.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000035948};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035948};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   458 AA;  49840 MW;  992302DCD483ACBA CRC64;
     MKKIKSSFLK RSRSLLELID RSPTPFHAVA ELGRLLKDGG YAELKEQDSW NLSPGGKYFV
     TRNGSSLTAF CAGSSSPESA GFKIIGAHTD SPNLRLKPNP AYVKNGYVQL GVEVYGGALL
     TTWTDRDLSL AGRVILRSPS GKKARTVGGA KSKKRASQSD HGCESRLIRF DRPLLRIPQL
     AIHLNRSVNE KGLILNPQTH LPPILSLIDG KLKSKKYLED LVAAELKCKA SEILGLELHL
     YDVQKGTLAG VHQEFIFASR LDNLASCHAA TSALLEAPGK DSATRVIAFY DNEEVGSETA
     QGGGSPFLKD ILERITAGAK KPREAFMRSV ARSLFISADM AHAVHPNYSE KHDVNHLPLI
     NAGPVIKSNA GQKYATEGIS AARFEQLCDR ANVPIQKFSI RSDLKCGSTI GPVTAANLGI
     RAVDAGNPML SMHSAREMAG SKDHDYLIRV FKEFFKPE
//
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