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Database: UniProt
Entry: A0A0N0SFB1_9ACTN
LinkDB: A0A0N0SFB1_9ACTN
Original site: A0A0N0SFB1_9ACTN 
ID   A0A0N0SFB1_9ACTN        Unreviewed;       431 AA.
AC   A0A0N0SFB1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-SEP-2017, entry version 7.
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   ORFNames=ADK54_31640 {ECO:0000313|EMBL:KOU37575.1};
OS   Streptomyces sp. WM6378.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1415557 {ECO:0000313|EMBL:KOU37575.1, ECO:0000313|Proteomes:UP000037774};
RN   [1] {ECO:0000313|EMBL:KOU37575.1, ECO:0000313|Proteomes:UP000037774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM6378 {ECO:0000313|EMBL:KOU37575.1,
RC   ECO:0000313|Proteomes:UP000037774};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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:KOU37575.1}.
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DR   EMBL; LGDD01000315; KOU37575.1; -; Genomic_DNA.
DR   RefSeq; WP_053729191.1; NZ_LGDD01000315.1.
DR   EnsemblBacteria; KOU37575; KOU37575; ADK54_31640.
DR   PATRIC; fig|1415557.3.peg.6967; -.
DR   Proteomes; UP000037774; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KOU37575.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037774};
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:UP000037774};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        86     86       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       157    157       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       407    407       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   431 AA;  46254 MW;  F6D36AA1FDFD9706 CRC64;
     MSTPPRFDRG HTDDLMTFLA ASPSQYHAVA NAAARLEKAG FRQVQETDAW DGTHGGKYVL
     RGGAIVAWYV PEDAQPHTPY RIVGAHTDSP NLRVKPQPDS GAYGWRQVAV EIYGGTLLNT
     WLDRDLGIAG RLTLRDGSHR LVNVDRPLLR VPQLAVHLDR SVNTDGLKLD RQRHLQPIWG
     LGDDVQEGDL IRFLEQEAEL DEGEVAGWDL MLHSVEAPAY LGRDRELVAG PRMDNLLSVH
     AGAAALAAVS ASEDLPFIPV LAAFDHEEDG SQADTGADGP LLGNVMERSV FARGGTYEDR
     ARAFAGTVCL SSDTGHAVHP NYAERHDPTH HPRANGGPIL KVNVNARYAT DGAGRAVFAA
     ACERAGVPWQ TFVSNNAMPC GTTIGPITAA RHGIQTVDIG VAILSMHSAR ELCGADDPHL
     LAGALAAFLA A
//
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