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Database: UniProt
Entry: N2ABZ9_9CLOT
LinkDB: N2ABZ9_9CLOT
Original site: N2ABZ9_9CLOT 
ID   N2ABZ9_9CLOT            Unreviewed;       432 AA.
AC   N2ABZ9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   28-FEB-2018, entry version 19.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=C824_04226 {ECO:0000313|EMBL:EMZ23635.1};
OS   Clostridium sp. ASF502.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=97139 {ECO:0000313|EMBL:EMZ23635.1, ECO:0000313|Proteomes:UP000012582};
RN   [1] {ECO:0000313|EMBL:EMZ23635.1, ECO:0000313|Proteomes:UP000012582}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASF502 {ECO:0000313|EMBL:EMZ23635.1,
RC   ECO:0000313|Proteomes:UP000012582};
RX   PubMed=24723722;
RA   Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT   "Draft genome sequences of the altered schaedler flora, a defined
RT   bacterial community from gnotobiotic mice.";
RL   Genome Announc. 2:e00287-14(2014).
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:EMZ23635.1}.
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DR   EMBL; AQFU01000065; EMZ23635.1; -; Genomic_DNA.
DR   RefSeq; WP_004083267.1; NZ_KB822470.1.
DR   EnsemblBacteria; EMZ23635; EMZ23635; C824_04226.
DR   PATRIC; fig|97139.3.peg.4614; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000012582; 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   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
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:UP000012582};
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:UP000012582};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   432 AA;  47725 MW;  EFB3999D29BB00C7 CRC64;
     MHTLAIEISQ LFEFLKNGTS AFHVTAHSKK VLTEAGFTEL KLKEPWPLER GGRYFCCPFD
     TTLYAFTIGR DCDLSRGIHI GGAHTDFPAI KIKPKPEIFT QGYMQLNTEL YGGPILSTFF
     DRSLSLAGKV VTRGSSYDRP VSHLIDFQRP VACLPNLAIH MNRTANEKGT PVDNQKHLLP
     ILGTLNDMLS KDSTLVKLLA EKLDVDPSEI LDYDLCLYNL EQPELAGITE EFLCAPRLDD
     ITSVCALVHA LAESQNPDRV NLVCLFDHEE IGSLSKQGAD SFLPNVIIGK IWQAFGKSMI
     DCMADLSDGL MLSADVAHAY HPNYPAVQDV TNYPVINQGF VFKSASNQSY AWDCEALASM
     IALCEDRQIP YQRFAKHSNT KGGGTIASIL SSHLPVRTID TGAGILAMHS SREMMGVKDQ
     IALSRFAKAF FE
//
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