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Database: UniProt
Entry: C8W052_DESAS
LinkDB: C8W052_DESAS
Original site: C8W052_DESAS 
ID   C8W052_DESAS            Unreviewed;       465 AA.
AC   C8W052;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Dtox_4357 {ECO:0000313|EMBL:ACV65020.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV65020.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV65020.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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; CP001720; ACV65020.1; -; Genomic_DNA.
DR   RefSeq; WP_015759689.1; NC_013216.1.
DR   ProteinModelPortal; C8W052; -.
DR   STRING; 485916.Dtox_4357; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; ACV65020; ACV65020; Dtox_4357.
DR   KEGG; dae:Dtox_4357; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; DACE485916:GHUF-4155-MONOMER; -.
DR   Proteomes; UP000002217; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACV65020.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
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:UP000002217};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   465 AA;  51209 MW;  D17E3C38D8B662CF CRC64;
     MANINGLFYE RKNVWERIDD DEKEAVLSFC EDYKIFLNKV KTEREAVQFC SEFVQAKGFK
     DISTIEKLKP GDSVFVEKNQ KALVMAVIGS RPIVEGLNLI GAHIDSPRLD LKPQTLFEKE
     NLGLLKTHYY GGIKKYQWTS IPLSLHGVII KSDGSKFDFI IGEKEDESVF TITDLLPHLA
     KEQMEKKMSE AIPGESLNIL CGSNPVTDKN IKEKVKAYIL EYLYSNYGII EEDFISAEIE
     AVPAWGARDI GFDRSLIGSY GQDDRVCAFT SMKALVDAGI PETTSLVILA DKEEIGSNGN
     TGMMSTLLEN SVAEIAAKLN PGDCSELLLR RVLAKSKALS ADVNAGLDPN YEDVMEKMNA
     AKLGYGLVIT KYTGSRGKSS SNDANAEFIA YIRNLLNKEN IIWQTGELGK IDQGGGGTIA
     YLMAASGMDV VDCGVALLGM HSTFEVAAKT DIYMAYKGYK AFFNA
//
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