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Database: UniProt
Entry: A0A0F2JJQ7_9FIRM
LinkDB: A0A0F2JJQ7_9FIRM
Original site: A0A0F2JJQ7_9FIRM 
ID   A0A0F2JJQ7_9FIRM        Unreviewed;       458 AA.
AC   A0A0F2JJQ7;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=UF75_1965 {ECO:0000313|EMBL:KJR47615.1};
OS   Desulfosporosinus sp. I2.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1617025 {ECO:0000313|EMBL:KJR47615.1, ECO:0000313|Proteomes:UP000033442};
RN   [1] {ECO:0000313|EMBL:KJR47615.1, ECO:0000313|Proteomes:UP000033442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I2 {ECO:0000313|EMBL:KJR47615.1,
RC   ECO:0000313|Proteomes:UP000033442};
RA   Mardanov A.V., Karnachuk O.V., Beletsky A.V., Kadnikov V.V.,
RA   Ravin N.V.;
RL   Submitted (FEB-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:KJR47615.1}.
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DR   EMBL; JYNH01000029; KJR47615.1; -; Genomic_DNA.
DR   RefSeq; WP_045574298.1; NZ_JYNH01000029.1.
DR   EnsemblBacteria; KJR47615; KJR47615; UF75_1965.
DR   PATRIC; fig|1617025.3.peg.2042; -.
DR   Proteomes; UP000033442; 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   PANTHER; PTHR28570; PTHR28570; 1.
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:KJR47615.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033442};
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:UP000033442};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   458 AA;  50745 MW;  1462FE9BA2D107A5 CRC64;
     MGTKKLKSAW DHYSLSENEG LAMRDYISFL SEGKTERESW QILEGWAKNA GFQRLDETTS
     FKAGQKVRLS VRGKAGIFAI AGLRPLGEGF RLVAAHIDAP RLDLKQRPLY EEEGLAFFKT
     HYYGGIKKYQ WTALPLALHG VVFLRDGAKI EIVIGEDDKD PILTIPDLLP HLAKEQNDKK
     LREAITGEGL NILLGHKPSP GEGDERVKSS ILDILKERYG IEEDDFVSAE LEIVPAGKAR
     FAGLDRSFIA GYGQDDRVCA YAAWKAIEEL EQPEWTTIVL LSDKEEIGSE SNTGMKARYL
     ENFIAELINL QNGSYDGLLV RRALAKSKAL SADVAAGFDP NYSEVMDKRN AAFLGRGIVI
     SKYTGSGGKY GSNDANPEFV AEIRQIFDEA KIDWQTAELG KVDQGGGGTI AQYMAVYGME
     VLDCGVGVLS MHAPWETISV IDLVMMIRAY HAFLTYKK
//
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