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Database: UniProt
Entry: U2T0F4_9FIRM
LinkDB: U2T0F4_9FIRM
Original site: U2T0F4_9FIRM 
ID   U2T0F4_9FIRM            Unreviewed;       435 AA.
AC   U2T0F4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   25-OCT-2017, entry version 19.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF1546_00177 {ECO:0000313|EMBL:ERK68222.1};
OS   Oscillibacter sp. KLE 1745.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Oscillospiraceae;
OC   Oscillibacter.
OX   NCBI_TaxID=1226323 {ECO:0000313|EMBL:ERK68222.1, ECO:0000313|Proteomes:UP000016601};
RN   [1] {ECO:0000313|EMBL:ERK68222.1, ECO:0000313|Proteomes:UP000016601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE 1745 {ECO:0000313|EMBL:ERK68222.1,
RC   ECO:0000313|Proteomes:UP000016601};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R.,
RA   Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M.,
RA   Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C.,
RA   Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Warren W.,
RA   Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (JUN-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:ERK68222.1}.
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DR   EMBL; AWVO01000011; ERK68222.1; -; Genomic_DNA.
DR   RefSeq; WP_021748053.1; NZ_KI271701.1.
DR   EnsemblBacteria; ERK68222; ERK68222; HMPREF1546_00177.
DR   PATRIC; fig|1226323.3.peg.148; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000016601; 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   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:ERK68222.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016601};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ERK68222.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:ERK68222.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016601};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   435 AA;  47702 MW;  C3A31A4E6573FE39 CRC64;
     MERDYSGELL RFIQEHPSVY HVIEGQRRIL LEAGYEQLLE SQHWTLREGG KYFLTRNHSA
     LIAFQVPKKR FRGFMLMASH SDSPALKVKE NPEITVGGLY KKLNVELYGG ALLAPWLDRP
     LSVAGRLLVR TSEGVRMQLV NVDRDLFLIP SLAIHMNRSV NDGYAYKVQR DLLPLYGAAE
     APDLTALVAE TAGISPESVI GHDLFVYNRQ APSIWGADRE FMSSPRLDDL QCAFSSLCGF
     LESAPEESLP VHVVFDNEEI GSSTRQGAAS PFLEDTLRRI TEALGLTFGE YLEKLPQSFL
     LSADNAHGMH PNYADKCDPV NRPRLGGGVV VKYSGNQKYA TDAVSAAIVR VLAKKAGVKL
     QVFTNHSDIP GGTTLGNISV QHVPVKTADV GIAQLAMHSP YETCGTGDTA ELIGLARKLF
     SSSLAENGDG DYTIV
//
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