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Database: UniProt
Entry: F5XSW7_MICPN
LinkDB: F5XSW7_MICPN
Original site: F5XSW7_MICPN 
ID   F5XSW7_MICPN            Unreviewed;       432 AA.
AC   F5XSW7;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   28-FEB-2018, entry version 40.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=MLP_43610 {ECO:0000313|EMBL:BAK37375.1};
OS   Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 /
OS   NBRC 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Microlunatus.
OX   NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK37375.1, ECO:0000313|Proteomes:UP000007947};
RN   [1] {ECO:0000313|EMBL:BAK37375.1, ECO:0000313|Proteomes:UP000007947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC   / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA   Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A.,
RA   Sasagawa M., Fukada J., Nakamura S., Katano Y., Hanada S.,
RA   Kamagata Y., Nakamura N., Yamazaki S., Fujita N.;
RT   "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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; AP012204; BAK37375.1; -; Genomic_DNA.
DR   RefSeq; WP_013865209.1; NC_015635.1.
DR   STRING; 1032480.MLP_43610; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; BAK37375; BAK37375; MLP_43610.
DR   KEGG; mph:MLP_43610; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; MPHO1032480:G1H6F-4223-MONOMER; -.
DR   Proteomes; UP000007947; 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:BAK37375.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007947};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:BAK37375.1};
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:UP000007947};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   432 AA;  45309 MW;  C4369A8976B30177 CRC64;
     MSAALEHARD LAEFVTASPT SFHAAAEGRQ RLTAAGFSVV DERAAFETAP GAYVLVRDGA
     LLAWRIPAGA GPGTPYRIVG AHTDSPGFVL KPRPDISASG WQQLGMEVYG GPLLNSWLDR
     ELGLAGRVIL TSGEQRLVRT GAIMRIPQLA IHLDRSVNDE GIKLDRQLHT APVWSVGRSD
     LRIMDQIALL VGCASDDIAG ADLSAYATTP PEIFGPTDEF LASGRLDNLS SVHAGLAALI
     STAEADASDT SAAGSEAITM LAAFDHEEVG SASRSGAAGP LLADVLSRIS AALGASLDDH
     QRALAGSICL SADTGHAVHP NYAQRHDPAN RPLLNGGPLL KINANQRYAT DAVGAASWRR
     ACDAAGVPIQ EFVSNNAVPC GSTIGPLTAT RLGIRTVDVG IPLLSMHSAR ELAGVRDPLH
     LRRAIEAFFQ QR
//
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