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Database: UniProt
Entry: G5GLX2_9FIRM
LinkDB: G5GLX2_9FIRM
Original site: G5GLX2_9FIRM 
ID   G5GLX2_9FIRM            Unreviewed;       427 AA.
AC   G5GLX2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   23-MAY-2018, entry version 30.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF9334_00253 {ECO:0000313|EMBL:EHG22217.1};
OS   Selenomonas infelix ATCC 43532.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales;
OC   Selenomonadaceae; Selenomonas.
OX   NCBI_TaxID=679201 {ECO:0000313|EMBL:EHG22217.1, ECO:0000313|Proteomes:UP000004129};
RN   [1] {ECO:0000313|EMBL:EHG22217.1, ECO:0000313|Proteomes:UP000004129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43532 {ECO:0000313|EMBL:EHG22217.1,
RC   ECO:0000313|Proteomes:UP000004129};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA   Baranova O.V., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Selenomonas infelix ATCC 43532.";
RL   Submitted (AUG-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHG22217.1}.
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DR   EMBL; ACZM01000003; EHG22217.1; -; Genomic_DNA.
DR   RefSeq; WP_006691704.1; NZ_JH376797.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EHG22217; EHG22217; HMPREF9334_00253.
DR   PATRIC; fig|679201.3.peg.258; -.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; SINF679201-HMP:GMSC-259-MONOMER; -.
DR   Proteomes; UP000004129; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000004129};
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   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   427 AA;  46294 MW;  E6A93BBA8DB8C3AF CRC64;
     MTFEEKRCAE ELVDFIEAAT SPYHAVEQSN KSLCAVPMEE NEKVAAGQIY SFPLYHTGMV
     FVVIGENAAQ GPLRIACAHT DFPCLRVKPN PVLREHGYGK LNVEVYGGLI RSTWLDRPLS
     LAGAVALRGV DPFAPTLRLV DFRRPLMIVP NLAIHMNRKV NEGVELKPQK DLLPLFFQNG
     DGDEDDTKKL LVLLAEELGV SAEDILSYDL NAYPYECGCL LGCDDAFLSA PRLDNLSSVK
     ACMDAIREWN GEGIRVVALF DNEEVGSRTK QGAGSTALAI LLERVCYKLG LDREEYLRKV
     MEGFCLSVDV AHALHPNAPE KADPTNQPVL GGGTVLKVAA NQSYAGDPEA FAVVAGLCEG
     AGIPYQVFTN HSDAAGGATL GSILSTQVPM RTMDIGAPIL GMHSARETMG ARDQFALTQL
     LMSFFSA
//
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