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Database: UniProt
Entry: U3GX97_9CORY
LinkDB: U3GX97_9CORY
Original site: U3GX97_9CORY 
ID   U3GX97_9CORY            Unreviewed;       414 AA.
AC   U3GX97;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   22-NOV-2017, entry version 23.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=CARG_04820 {ECO:0000313|EMBL:AGU15103.1};
OS   Corynebacterium argentoratense DSM 44202.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1348662 {ECO:0000313|EMBL:AGU15103.1, ECO:0000313|Proteomes:UP000016943};
RN   [1] {ECO:0000313|EMBL:AGU15103.1, ECO:0000313|Proteomes:UP000016943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44202 {ECO:0000313|EMBL:AGU15103.1};
RX   PubMed=24092787;
RA   Bomholt C., Glaub A., Gravermann K., Albersmeier A., Brinkrolf K.,
RA   Ruckert C., Tauch A.;
RT   "Whole-Genome Sequence of the Clinical Strain Corynebacterium
RT   argentoratense DSM 44202, Isolated from a Human Throat Specimen.";
RL   Genome Announc. 1:e00793-13(2013).
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}.
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DR   EMBL; CP006365; AGU15103.1; -; Genomic_DNA.
DR   RefSeq; WP_020976255.1; NC_022198.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; AGU15103; AGU15103; CARG_04820.
DR   KEGG; caz:CARG_04820; -.
DR   PATRIC; fig|1348662.3.peg.947; -.
DR   KO; K01267; -.
DR   Proteomes; UP000016943; Chromosome.
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; 2.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016943};
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:UP000016943};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   414 AA;  44585 MW;  5F021552EAAA60A4 CRC64;
     MTALPSIEEF IASSPSSYHA AENIAAILNT AGFTRQDETD TWQATPGGHY MVRGGALMAW
     WVPENASPAT SGFRIIGSHT DSPGLKLKPT ISFDKEGFHQ APVEIYGGPI LASWLDRELQ
     LAGQIIDADG NRRLVATGPV LRVPHLAIHL YRQDELKLER QQHMQPIYGL VESPELATLL
     DGVRTHDLIT ADTQPPRAFG IKNEFLAAGR LDNLSSVYPS LEALLDVVAD SNATSSIKDV
     LVLAAFDHEE IGSSSRYGAA GPILEDVLKR TAYALGAGED DLYAMFARSS CISADAAHSV
     HPNFASKHDP NTHPVLGAGP VLKVNANQRY ASDARSNDIW LRASEKAGVA VQQFVGNNDV
     PCGSTIGPIT ATRLGILTVD VGIPLLSMHS AREMCAYSDL KDFTEVLAAY YTLD
//
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