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Database: UniProt
Entry: A0A0D7QQS0_9MICO
LinkDB: A0A0D7QQS0_9MICO
Original site: A0A0D7QQS0_9MICO 
ID   A0A0D7QQS0_9MICO        Unreviewed;       440 AA.
AC   A0A0D7QQS0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   28-FEB-2018, entry version 12.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=TZ00_04220 {ECO:0000313|EMBL:KJC64873.1};
OS   Agreia bicolorata.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Agreia.
OX   NCBI_TaxID=110935 {ECO:0000313|EMBL:KJC64873.1, ECO:0000313|Proteomes:UP000032503};
RN   [1] {ECO:0000313|EMBL:KJC64873.1, ECO:0000313|Proteomes:UP000032503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-1804 {ECO:0000313|EMBL:KJC64873.1,
RC   ECO:0000313|Proteomes:UP000032503};
RX   PubMed=11760949; DOI=10.1099/00207713-51-6-2073;
RA   Evtushenko L.I., Dorofeeva L.V., Dobrovolskaya T.G.,
RA   Streshinskaya G.M., Subbotin S.A., Tiedje J.M.;
RT   "Agreia bicolorata gen. nov., sp. nov., to accommodate actinobacteria
RT   isolated from narrow reed grass infected by the nematode Heteroanguina
RT   graminophila.";
RL   Int. J. Syst. Evol. Microbiol. 51:2073-2079(2001).
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:KJC64873.1}.
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DR   EMBL; JYFC01000002; KJC64873.1; -; Genomic_DNA.
DR   RefSeq; WP_044439580.1; NZ_JYFC01000002.1.
DR   EnsemblBacteria; KJC64873; KJC64873; TZ00_04220.
DR   PATRIC; fig|110935.6.peg.1102; -.
DR   Proteomes; UP000032503; 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   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:KJC64873.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032503};
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:UP000032503};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   440 AA;  46319 MW;  99DF815C82E9ACDE CRC64;
     MDSSTTDAYI DDFARFIEAS PSSYHAVAEA ARRLDEAGFS RLDEASDWPA AGADGGAASA
     EPAASARHYV VRDGAIIAWL RPAEATATTP FRVLGSHTDS PAFKLKPKPT IANRGWLQAG
     VEVYGGPLLN SWLDRELELA GRLVTRDGVE HLVRTGPYLR IPQLAIHLDR EVNSGLTLDK
     QRHLTPVFGV GHAGDLLAHL AHLAGVPAWD VAGYDLLTAD TQGPARFGKD GELFAAGRMD
     NLSSVYAGLV ALIAAADETQ AEQEHISVLA AFDHEELGSE SRSGASGPLL DDVLSRIGAG
     LGATSSDRLR AYAASWCLSA DAGHAIHPNY PERHDPVNTP IAGGGPLLKI NANQRYATDA
     FGAALWARAC ERAGVSYQEF VSNNAVPCGS TIGPLTATRL GIRTVDVGVP LLSMHSAREL
     CHVNDPVALS AAVGAFFAGA
//
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