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Database: UniProt
Entry: A0A2C6M5I7_9FIRM
LinkDB: A0A2C6M5I7_9FIRM
Original site: A0A2C6M5I7_9FIRM 
ID   A0A2C6M5I7_9FIRM        Unreviewed;       153 AA.
AC   A0A2C6M5I7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   28-MAR-2018, entry version 4.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=P378_15780 {ECO:0000313|EMBL:PHJ37477.1};
OS   Desulfotomaculum profundi.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=1383067 {ECO:0000313|EMBL:PHJ37477.1, ECO:0000313|Proteomes:UP000222564};
RN   [1] {ECO:0000313|EMBL:PHJ37477.1, ECO:0000313|Proteomes:UP000222564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bs107 {ECO:0000313|EMBL:PHJ37477.1,
RC   ECO:0000313|Proteomes:UP000222564};
RA   Aullo T., Berlendis S., Lascourreges J.-F., Dessort D.,
RA   Saint-Laurent S., Schraauwers B., Mas J., Magot M.,
RA   Ranchou-Peyruse A.;
RT   "Biodegradation of hydrocarbons in the deep terrestrial subsurface :
RT   characterization of a microbial consortium composed of two
RT   Desulfotomaculum species originating from a deep geological
RT   formation.";
RL   Submitted (SEP-2013) 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:PHJ37477.1}.
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DR   EMBL; AWQQ01000091; PHJ37477.1; -; Genomic_DNA.
DR   Proteomes; UP000222564; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000222564};
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:UP000222564};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   153 AA;  16525 MW;  188BBDA3951263F8 CRC64;
     MADIGSRLHP QFNELALYRV FAKSIAISAD VTAGLDPNYE GVLEKMNAAR INGGVVVTKY
     TGAKGKYHTN DASAEYVAFV RNLLNQNQIT WQTGELGKVD QGGGGTIAHM IAELGFEVID
     CGVALLSMHS PMEIASKADI FECYRAYKAF FGA
//
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