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Database: UniProt
Entry: A0A0N0I3M5_9ACTN
LinkDB: A0A0N0I3M5_9ACTN
Original site: A0A0N0I3M5_9ACTN 
ID   A0A0N0I3M5_9ACTN        Unreviewed;       430 AA.
AC   A0A0N0I3M5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   22-NOV-2017, entry version 10.
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=ADL27_01455 {ECO:0000313|EMBL:KPC97011.1};
OS   Streptomyces sp. NRRL F-6602.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1609099 {ECO:0000313|EMBL:KPC97011.1, ECO:0000313|Proteomes:UP000037856};
RN   [1] {ECO:0000313|EMBL:KPC97011.1, ECO:0000313|Proteomes:UP000037856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL F-6602 {ECO:0000313|EMBL:KPC97011.1,
RC   ECO:0000313|Proteomes:UP000037856};
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:KPC97011.1}.
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DR   EMBL; LGKH01000001; KPC97011.1; -; Genomic_DNA.
DR   EnsemblBacteria; KPC97011; KPC97011; ADL27_01455.
DR   PATRIC; fig|1609099.3.peg.309; -.
DR   Proteomes; UP000037856; 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   PANTHER; PTHR28570; PTHR28570; 1.
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:KPC97011.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037856};
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:UP000037856};
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       406    406       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   430 AA;  45513 MW;  2466717B7A0C19C4 CRC64;
     MSDAMPFDRG HTDGLLSFLA ASPSPYHAVA NAAARLAEAG FQQVHETDAW DGTPGGKYVL
     RGGALIAWYV PEGATPATPF RIVGAHTDSP NLRVKPVPDT GAQGWRQIAV EIYGGTLLNT
     WLDRDLGLSG RLTLRDGSTR LVHVDRPLLR VPQLAIHLDR QVNDGLKLER QRHMTPIWGL
     GRPGEGDLVR FLAEESGLDA DAVAGWDLMA HSVEPPAYLG RDRELVAGPR MDNLLSVHAG
     VAALAAVAEA GTAPAAIPVL AAFDHEENGS QSDTGAQGPL LGTVLERSVA ARGGTFEDRA
     RALAGTVCFS SDTGHAVHPN YPERHEPGHH PMPNGGPILK VNVNQRYATD GSGRALFAAA
     CERAGVPWQS FVSHNDMPCG TTIGPLTAAR HGITTVDIGV AILSMHSARE LCGADDPFLL
     ANCLTAFLGE
//
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