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Database: UniProt
Entry: A0A139V7X5_MYCPH
LinkDB: A0A139V7X5_MYCPH
Original site: A0A139V7X5_MYCPH 
ID   A0A139V7X5_MYCPH        Unreviewed;       417 AA.
AC   A0A139V7X5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   18-JUL-2018, entry version 16.
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=MPHL43239_18210 {ECO:0000313|EMBL:KXW62265.1};
OS   Mycolicibacterium phlei DSM 43239 = CCUG 21000.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1226750 {ECO:0000313|EMBL:KXW62265.1, ECO:0000313|Proteomes:UP000070233};
RN   [1] {ECO:0000313|EMBL:KXW62265.1, ECO:0000313|Proteomes:UP000070233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43239 \ CCUG 21000 {ECO:0000313|Proteomes:UP000070233};
RX   PubMed=26941228;
RA   Das S., Pettersson B.M., Behra P.R., Ramesh M., Dasgupta S.,
RA   Bhattacharya A., Kirsebom L.A.;
RT   "The Mycobacterium phlei genome: expectations and surprises.";
RL   Genome Biol. Evol. 0:0-0(2016).
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:KXW62265.1}.
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DR   EMBL; ANBO01000034; KXW62265.1; -; Genomic_DNA.
DR   RefSeq; WP_061481658.1; NZ_ANBO01000034.1.
DR   EnsemblBacteria; KXW62265; KXW62265; MPHL43239_18210.
DR   PATRIC; fig|1226750.3.peg.3639; -.
DR   Proteomes; UP000070233; 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   Gene3D; 2.30.250.10; -; 1.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
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:KXW62265.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000070233};
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:UP000070233};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        75     75       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       149    149       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       392    392       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   417 AA;  44935 MW;  6904C9DDA32161C9 CRC64;
     MAASPQSLCE FIDASPSPFH VCATAADRLR AAGFRELSEA DAWPSDGDFF VVRAGSLIAW
     RSTRDRRPFR IVGAHTDSPN LRVKQHPDRY VAGWRVVALQ PYGGAWLNSW LDRDLGISGR
     LSIRQGNTIE HRLIRIDDPI LRVPQLAIHL SEDRKAVELN PQRHVNAVWG TGGESRSFLG
     YVAERAGVAA DDILGADLMT HDLTPSRLVG ADQELVSAPR LDNQATCYAG LEAFLAAEPG
     AYLPVLVLFD HEEVGSQSDH GAQSDLLLTT LERITLVQGG GREDFLRRLP DSLVASGDMA
     HATHPNYPDR HEPGHLIEVN GGPVLKVQPN LRYATDGRTA AAFALACQQA GVPLQRYEHR
     ADLPCGSTVG PMTAAGTGIP TVDVGAPQLA MHSAREVMGA HDVAAYAAAL QAFLSPA
//
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