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Database: UniProt
Entry: A0A0U5AWN9_9BACT
LinkDB: A0A0U5AWN9_9BACT
Original site: A0A0U5AWN9_9BACT 
ID   A0A0U5AWN9_9BACT        Unreviewed;       453 AA.
AC   A0A0U5AWN9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=THC_1419 {ECO:0000313|EMBL:BAU23784.1};
OS   Caldimicrobium thiodismutans.
OC   Bacteria; Thermodesulfobacteria; Thermodesulfobacteriales;
OC   Thermodesulfobacteriaceae; Caldimicrobium.
OX   NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU23784.1, ECO:0000313|Proteomes:UP000068196};
RN   [1] {ECO:0000313|Proteomes:UP000068196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196};
RA   Kojima H., Umezawa K., Fukui M.;
RT   "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT   bacterium isolated from a hot spring.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
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; AP014945; BAU23784.1; -; Genomic_DNA.
DR   RefSeq; WP_068515325.1; NZ_AP014945.1.
DR   EnsemblBacteria; BAU23784; BAU23784; THC_1419.
DR   KEGG; cthi:THC_1419; -.
DR   PATRIC; fig|1653476.3.peg.1470; -.
DR   Proteomes; UP000068196; 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; 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:BAU23784.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000068196};
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:UP000068196};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   453 AA;  51332 MW;  57A005731E3FC1D1 CRC64;
     MEHVFDKLKA EEIKELEGLI KKYLDFLSEI KTERECVEQF KEDLLKKGFQ EKARDKGFFT
     YRNKFLACWR RGKRPLQEGL KLIISHIDTP RLDLKLHPLF EDQDLAFLKT HYYGGIKKYH
     WVAMPLALHG VVVKKDGSII NLVLGEREDE PLFTICDLLP HLGRKKQEEK RLAEAIPAEN
     LNILIGGIPI EKSGKGKKEE KERIKKRILK LFEEKYGISE EDFFSAEIFA VPAGRARLVG
     LDSAFVGGYG QDDRICAFTS FQALLSIEKP LYTTLVLFMD REEIGSEGNT SAKSRIFESL
     VYELMKAEEL SPTPDVFFEI MSKTKALSAD VTAGIDPNYL EVHDKLNDAK LGYGVVISRY
     TGHGGKYMAN EAHAEYISYL RSLFEKEGVV YQVASMGKVD EGGGGTVSKY FASYGMDVVD
     IGPPLLSMHS PFEIAHKGDL YMTYRAFKAF LKG
//
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