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Database: UniProt
Entry: F0H224_9FIRM
LinkDB: F0H224_9FIRM
Original site: F0H224_9FIRM 
ID   F0H224_9FIRM            Unreviewed;       461 AA.
AC   F0H224;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   07-JUN-2017, entry version 30.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF9246_1383 {ECO:0000313|EMBL:EGC83470.1};
OS   Anaerococcus hydrogenalis ACS-025-V-Sch4.
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Anaerococcus.
OX   NCBI_TaxID=879306 {ECO:0000313|EMBL:EGC83470.1, ECO:0000313|Proteomes:UP000005277};
RN   [1] {ECO:0000313|EMBL:EGC83470.1, ECO:0000313|Proteomes:UP000005277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-025-V-Sch4 {ECO:0000313|EMBL:EGC83470.1,
RC   ECO:0000313|Proteomes:UP000005277};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JAN-2011) 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:EGC83470.1}.
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DR   EMBL; AEXN01000032; EGC83470.1; -; Genomic_DNA.
DR   RefSeq; WP_004817789.1; NZ_AEXN01000032.1.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EGC83470; EGC83470; HMPREF9246_1383.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000005277; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EGC83470.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005277};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EGC83470.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EGC83470.1};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   461 AA;  51171 MW;  21E18B47A4B87563 CRC64;
     MTEYKRKNVW ENLSSDQEKE LESLSKDYMD FLDKAKTERL AAKEIVKYAK EAGYVDLDEK
     IKSGKINPGD KIYAINKNKA VAMFHIGEED LEKGLAIVGG HIDSPRLDLK PVPLMEENGI
     SYLKTHYYGG VKKYNWTNMP LALHGVVFTK NGDKVEISLG DKEDEPVFYI SELLIHLSKK
     LMTKPAEEVV TGEQLSIIVG NRPLLDEKEN PVKKNILKIL NEKYGIEEED FITAELEVVP
     AGKAREVGFD RSMIASHGHD DRVCSYAALR ALLDIDKTKK TLVGLFVDKE EIGSVGATGM
     TSQFFENTLL EIMNLKEEFN LIKFKRALRN SKVLSADVTL AEDPNFKDAT ESQNSAQISH
     GVALTKYTGS GGKGGSNDAD AEYLSEVRLA FNKDGVIFQT GELGKVDQGG GGTIAYILAE
     YGMDVVDCGT PVISMHAPIE LISKADFYST FTAYRAFYKN I
//
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