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Database: UniProt
Entry: A0A101T1P1_9ACTN
LinkDB: A0A101T1P1_9ACTN
Original site: A0A101T1P1_9ACTN 
ID   A0A101T1P1_9ACTN        Unreviewed;       432 AA.
AC   A0A101T1P1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   25-OCT-2017, entry version 9.
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=AQJ66_17635 {ECO:0000313|EMBL:KUN83978.1};
OS   Streptomyces bungoensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN83978.1, ECO:0000313|Proteomes:UP000053024};
RN   [1] {ECO:0000313|EMBL:KUN83978.1, ECO:0000313|Proteomes:UP000053024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN83978.1,
RC   ECO:0000313|Proteomes:UP000053024};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces bungoensis DSM 41781, type
RT   strain for the species Streptomyces bungoensis.";
RL   Submitted (OCT-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:KUN83978.1}.
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DR   EMBL; LMWX01000025; KUN83978.1; -; Genomic_DNA.
DR   RefSeq; WP_061922477.1; NZ_KQ948857.1.
DR   EnsemblBacteria; KUN83978; KUN83978; AQJ66_17635.
DR   Proteomes; UP000053024; 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:KUN83978.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053024};
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:UP000053024};
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       408    408       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   432 AA;  45806 MW;  4E0DF1B6773B0747 CRC64;
     MSAPARFDRG HTDDLMSFLA ASPSPYHAVA NTAERLEKAG FRQVAETDAW DASSGGRYVL
     RGGAIVAWYV PEGAAPHTPF HIIGAHTDSP NLRVKPRPDT GAHGWRQVAV EIYGGPLLNS
     WLDRDLGLAG RLTLRDGSSV LVDVDRPLLR VPQLAVHLDR TVTSEGLKLD KQRHMQPVWG
     LGDDLRDGDL IAFLEQEAGL AAGTVAGWDL MAHPVEAPAY LGRDRELVAG PRMDNLLSVH
     AGVAALTAAA ASGAALTRIP VLAAFDHEEN GSQSDTGADG PLLGTVLERS VFARGGSYED
     RARAFAATVC LSSDTGHAVH PNYGERHDPT HHPHVNGGPL LKVNVNNRYA TDGSGRAVFA
     AACERAGVPL QSFVSNNSMP CGTTIGPITA ARHGIRTVDI GVAILSMHSA RELCGADDPF
     LLANSLLAFL QD
//
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