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Database: UniProt
Entry: A0PZD8_CLONN
LinkDB: A0PZD8_CLONN
Original site: A0PZD8_CLONN 
ID   A0PZD8_CLONN            Unreviewed;       469 AA.
AC   A0PZD8;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   28-MAR-2018, entry version 73.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=NT01CX_1659 {ECO:0000313|EMBL:ABK60395.1};
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK60395.1, ECO:0000313|Proteomes:UP000008220};
RN   [1] {ECO:0000313|EMBL:ABK60395.1, ECO:0000313|Proteomes:UP000008220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT {ECO:0000313|EMBL:ABK60395.1,
RC   ECO:0000313|Proteomes:UP000008220};
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A.,
RA   Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W.,
RA   Vogelstein B., Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium
RT   novyi-NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK60395.1; -; Genomic_DNA.
DR   RefSeq; WP_011721747.1; NC_008593.1.
DR   ProteinModelPortal; A0PZD8; -.
DR   STRING; 386415.NT01CX_1659; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; ABK60395; ABK60395; NT01CX_1659.
DR   GeneID; 4541977; -.
DR   KEGG; cno:NT01CX_1659; -.
DR   PATRIC; fig|386415.7.peg.766; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000008220; 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   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   ECO:0000313|EMBL:ABK60395.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008220};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ABK60395.1};
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:UP000008220};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   469 AA;  52305 MW;  D7C6CA975AC269B2 CRC64;
     MAENKVKLEK NYEYAWDKYS EEELKEVFLL NDRYINFMSN CKTERECVDE FIKIAEDNGY
     KNINDLIAEN GKLNPGDKVY ANNMGKTLAM FVIGNEPFEK GLSILGAHVD SPRLDLKQNP
     LYEDSDLALF DTHYYGGIKK YQWVTLPLAI HGVIAKKTGE VVKVVIGEDE NDPVVGISDL
     LIHLAGNQMD KKLAKGVEGE DLNVLIGSMP IKDKEAKNRV KQNILRLLND KYGIDEEDFV
     SAELEVVPAG RARHYGLDKS MVMAYGHDDR VCAYTSFEAI LKVENPSKTC VALLVDKEEI
     GSVGATGMHS KFFENVVAEV MNLLGDYNEL KLRRTLTNSK MLSSDVSAAF DPNYPSVMEK
     RNCAYFGKGV VFNKYTGARG KSGSNDASAE YMGEIRDIME KHNVSWQTAE LGKVDEGGGG
     TIAYILAEYG MNVIDCGVAV QNMHAPWEVV SKADVYETMR AYCAFLKEA
//
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