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Database: UniProt
Entry: A0A126T6R7_9GAMM
LinkDB: A0A126T6R7_9GAMM
Original site: A0A126T6R7_9GAMM 
ID   A0A126T6R7_9GAMM        Unreviewed;       434 AA.
AC   A0A126T6R7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   25-OCT-2017, entry version 8.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=JT25_015100 {ECO:0000313|EMBL:AMK77787.1};
OS   Methylomonas denitrificans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK77787.1, ECO:0000313|Proteomes:UP000030512};
RN   [1] {ECO:0000313|EMBL:AMK77787.1, ECO:0000313|Proteomes:UP000030512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJG1 {ECO:0000313|EMBL:AMK77787.1,
RC   ECO:0000313|Proteomes:UP000030512};
RX   PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA   Kits K.D., Klotz M.G., Stein L.Y.;
RT   "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT   Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT   FJG1.";
RL   Environ. Microbiol. 17:3219-3232(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}.
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DR   EMBL; CP014476; AMK77787.1; -; Genomic_DNA.
DR   RefSeq; WP_036276904.1; NZ_CP014476.1.
DR   EnsemblBacteria; AMK77787; AMK77787; JT25_015100.
DR   KEGG; mdn:JT25_015100; -.
DR   KO; K01267; -.
DR   Proteomes; UP000030512; Chromosome.
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:AMK77787.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030512};
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:UP000030512};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   434 AA;  47798 MW;  086C1D4E75F4D753 CRC64;
     MTAQRQAQDL LDFIDASPSP WHAVATIEQR LLDYQFQRIQ ENESWSLAPG GRYYVIRDDS
     SIAAFVIGKQ ALAKTGFKIL GAHTDSPGLR VKPQPLLDSD KLLRLAVEVY GGPILATFAD
     RDLSLAGRIA YLDSDGNIAS RLVRFDEPLL RLPNLAIHMN RGVNEDGLKL KKQTELPLIF
     SASVEQQLPS DRFRQVLEQA SNIAADRILS WELNAYDTQK GVLWGDGQLF YADSQLDNLA
     SCHAGLTALL DAPTLDTDST LVCAFFDHEE IGSESCKGAA GSFLPDVLER IANSVGNNPD
     DYRRSLANSF MISADMAHAY QPNFPGAYEP GHKIIVNHGP VIKVNVNHRY ASECISEATF
     IRICQLAEVP YQKYAHHGDL PCGSTIGPIA SAKLGIRSVD VGSPMWAMHS IRESAGVLDH
     TYMIRALRGF FSNR
//
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