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Database: UniProt
Entry: A0A132PR98_9MYCO
LinkDB: A0A132PR98_9MYCO
Original site: A0A132PR98_9MYCO 
ID   A0A132PR98_9MYCO        Unreviewed;       415 AA.
AC   A0A132PR98;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-SEP-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=AFM11_08665 {ECO:0000313|EMBL:KWX24727.1};
OS   Mycobacterium wolinskyi.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX24727.1, ECO:0000313|Proteomes:UP000070612};
RN   [1] {ECO:0000313|EMBL:KWX24727.1, ECO:0000313|Proteomes:UP000070612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC_01 {ECO:0000313|EMBL:KWX24727.1,
RC   ECO:0000313|Proteomes:UP000070612};
RA   de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA   Limbago B.M., Noble-Wang J.;
RT   "A draft genome sequence of Mycobacterium wolinskyi.";
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:KWX24727.1}.
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DR   EMBL; LGTW01000004; KWX24727.1; -; Genomic_DNA.
DR   RefSeq; WP_067846559.1; NZ_LGTW01000004.1.
DR   EnsemblBacteria; KWX24727; KWX24727; AFM11_08665.
DR   PATRIC; fig|59750.3.peg.5583; -.
DR   Proteomes; UP000070612; 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:KWX24727.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070612};
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:UP000070612};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        73     73       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       147    147       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       390    390       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   415 AA;  44086 MW;  C40C2B2CF2BAD0A6 CRC64;
     MAASPQSLCE FIDASPSPFH VCATAARRLL EAGFTELDET DAWPATGNFF TVRAGSLVAW
     KTGDGPFRVV GGHTDSPNLR VKQHPDRVVA GWQVVALQPY GGAWLNSWLD RDLGISGRLS
     VRRGTGIEHK LVRIDDPILR VPQLAIHLSE DRKGVSPDPQ RHVNAVWGLG ERPRSFVGFV
     AEHAGVAEGD VLGFDLMTHD LAPSAVTGAG GEFVSAPRLD NQATCYAGLE AFLAADADGH
     VPVLALFDHE EVGSTSDHGA QSELLPTVLE RITLSAGGTR EDFLRRVAGS MVASGDMAHA
     THPNYPDRHE PGHQIAVNAG PVLKVQPNLR YATDGRTAAA FALACDQAGV PLQRYEHRAD
     LPCGSTIGPM TSARTGIPTV DVGAAQLAMH SAREFMGAHD VAAYSSALRA FLSPA
//
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