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Database: UniProt
Entry: L7LAU3_9ACTN
LinkDB: L7LAU3_9ACTN
Original site: L7LAU3_9ACTN 
ID   L7LAU3_9ACTN            Unreviewed;       425 AA.
AC   L7LAU3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   25-OCT-2017, entry version 25.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467,
GN   ECO:0000313|EMBL:GAC57871.1};
GN   ORFNames=GOHSU_27_00070 {ECO:0000313|EMBL:GAC57871.1};
OS   Gordonia hirsuta DSM 44140 = NBRC 16056.
OC   Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=1121927 {ECO:0000313|EMBL:GAC57871.1, ECO:0000313|Proteomes:UP000053405};
RN   [1] {ECO:0000313|EMBL:GAC57871.1, ECO:0000313|Proteomes:UP000053405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 16056 {ECO:0000313|EMBL:GAC57871.1,
RC   ECO:0000313|Proteomes:UP000053405};
RA   Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Katsumata H., Baba S.,
RA   Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia hirsuta NBRC 16056.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00467, 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:GAC57871.1}.
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DR   EMBL; BANT01000027; GAC57871.1; -; Genomic_DNA.
DR   RefSeq; WP_005940887.1; NZ_BANT01000027.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; GAC57871; GAC57871; GOHSU_27_00070.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000053405; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:GAC57871.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053405};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053405};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        83     83       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       157    157       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       399    399       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   425 AA;  44872 MW;  60135D2D8C386ECF CRC64;
     MIATSATAEG LGAFIDASPS PFHVCATVAA RLEAAGYRCL RETDSWGDGA VAGRRYVLRG
     GSLIAWNADD RDAPVPLRIV GGHTDSPNLR VKQHPDRQSA GWSTVALEPY GGAWLNSWLD
     RDLGLSGRLA YDDDGTVAHA LIVIDEPVLR VPQLAIHLSA DRKGVQLDPQ RHVDAIRGIG
     EAEPLIEWVA QRAGLAPGAV LGWELMTHDL TPSRLIGADG ALLSAPRLDN QGTCYAGLAA
     LLDAQPSAQV PMLALFDHEE VGSGSERGAS SDFLITVCER LVAGLGGSRE DFFATMAASF
     HVSGDMAHAT HPNYADRHEP GHQIAVDGGP VLKVNQNLRY ASDATGEAEF ALACRRAGVP
     LQRYVHRADL PCGSTIGPLT AARTGLRTVD VGAPQLAMHS ARELMGAADV PMYSAALQAF
     LSAPA
//
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