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Database: UniProt
Entry: A0A0S8CLV0_9BACT
LinkDB: A0A0S8CLV0_9BACT
Original site: A0A0S8CLV0_9BACT 
ID   A0A0S8CLV0_9BACT        Unreviewed;       473 AA.
AC   A0A0S8CLV0;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-APR-2018, entry version 10.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=AMK69_16860 {ECO:0000313|EMBL:KPK23996.1};
OS   Nitrospira bacterium SG8_3.
OC   Bacteria; Nitrospirae.
OX   NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK23996.1};
RN   [1] {ECO:0000313|EMBL:KPK23996.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_3 {ECO:0000313|EMBL:KPK23996.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur
RT   cycling among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK23996.1}.
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DR   EMBL; LJNR01000329; KPK23996.1; -; Genomic_DNA.
DR   PATRIC; fig|1704023.3.peg.2021; -.
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   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KPK23996.1};
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   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   473 AA;  52144 MW;  6A445065410A4A0A CRC64;
     MKSKLSKKKV EELRKRLVRK PQLVWDLVKP AEKKKIFEFA ERYKGFLDAA KTEREGVQAI
     EAFAKKKGFK DISKGGGGKK FYKINKNKSI AMAVLGKSPL SSGINVIASH IDSPRLDLKQ
     NPLYEEVDLA FLKTHYYGGI KKYQWLARPL AIHGTVLKKD GKPFNFHIGE SHNEPVFTIA
     DLLPHLSHKL QSDKKVSEAF EGEKLNVLVG SLPLGDDETK ERFKLAVLEY LFSAYGIIEE
     DLMSAEIEIV PAGRARDVGL DRGLIGAYGQ DDRACAYASL DALGGMEAPG STTVALFMDK
     EEIGSDGSTG AKSRFLEDFV SDLFEVAGQE ASAKTLRSCL MKSRALSADA NAALDPDYQE
     VHEKRNAARI GYGVCITKFT GSRGKYGSSD ANAEYVADIR RLFNENKVVW QTGEIGKVDE
     GGGGTIAKFL AVYGMEVLDC GTPILSMHSP FEIASKADIY MTYKAYHAFF NSK
//
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