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Database: UniProt
Entry: B0S2P9_FINM2
LinkDB: B0S2P9_FINM2
Original site: B0S2P9_FINM2 
ID   B0S2P9_FINM2            Unreviewed;       420 AA.
AC   B0S2P9;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   28-MAR-2018, entry version 68.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=FMG_1221 {ECO:0000313|EMBL:BAG08639.1};
OS   Finegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Finegoldia.
OX   NCBI_TaxID=334413 {ECO:0000313|EMBL:BAG08639.1, ECO:0000313|Proteomes:UP000001319};
RN   [1] {ECO:0000313|EMBL:BAG08639.1, ECO:0000313|Proteomes:UP000001319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29328 {ECO:0000313|EMBL:BAG08639.1,
RC   ECO:0000313|Proteomes:UP000001319};
RX   PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA   Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA   Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT   "Complete genome sequence of Finegoldia magna, an anaerobic
RT   opportunistic pathogen.";
RL   DNA Res. 15:39-47(2008).
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; AP008971; BAG08639.1; -; Genomic_DNA.
DR   RefSeq; WP_012290905.1; NC_010376.1.
DR   ProteinModelPortal; B0S2P9; -.
DR   STRING; 334413.FMG_1221; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; BAG08639; BAG08639; FMG_1221.
DR   GeneID; 34165331; -.
DR   KEGG; fma:FMG_1221; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; KSGCHAI; -.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; FMAG334413:GJ6M-1276-MONOMER; -.
DR   Proteomes; UP000001319; 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:BAG08639.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001319};
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:UP000001319};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   420 AA;  47166 MW;  8ECDA340C1E00323 CRC64;
     MNITKELMNF IDNSPSVFHV IDNFKKTLTE NGFTELKFKD NWKIENGKGY FVTNNDSSII
     AFKGSSDFDN IRLIGSHSDS PTFRIKPNSI VNKDGFLTLN TEVYGGPILS TWFDRPLSVA
     GRVVLKSDNP FKPEIKHINV DKNLLIIPNV AIHMNREVNN GYKFNAQKDT LPLLALSEKD
     SKISFEEILA RNTGINADDI LDFDLFLYDR QKGEFVGEND EFYSVGRIDN LGMAFNSIKS
     LIDSNVTNTL ALTMVFDNEE IGSSTKQGAG STLLSDCFKK IVEDNDKNFY EVLHNSYLIS
     ADQAHSLHPN YTEMADPTNR PLINNGPVIK YAANGAYTSD AVSSSVFKKL CLDKNIPCQE
     FTNRSDKRGG STIGPITVSN LDIQSIDIGN AILSMHSVRE LGGCKDNEYI YELFKYYYEY
//
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