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Database: UniProt
Entry: A0A0I9VHC3_9MYCO
LinkDB: A0A0I9VHC3_9MYCO
Original site: A0A0I9VHC3_9MYCO 
ID   A0A0I9VHC3_9MYCO        Unreviewed;       423 AA.
AC   A0A0I9VHC3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-NOV-2017, entry version 11.
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=ABH38_03295 {ECO:0000313|EMBL:KLO38688.1};
OS   Mycobacterium haemophilum.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO38688.1, ECO:0000313|Proteomes:UP000036334};
RN   [1] {ECO:0000313|EMBL:KLO38688.1, ECO:0000313|Proteomes:UP000036334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA   Greninger A.L., Cunningham G., Miller S.;
RT   "Genome sequence of Mycobacterium haemophilum.";
RL   Submitted (MAY-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:KLO38688.1}.
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DR   EMBL; LDPR01000002; KLO38688.1; -; Genomic_DNA.
DR   RefSeq; WP_047315255.1; NZ_LDPT01000002.1.
DR   EnsemblBacteria; KLO38688; KLO38688; ABH38_03295.
DR   PATRIC; fig|29311.18.peg.745; -.
DR   Proteomes; UP000036334; 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:KLO38688.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036334};
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:UP000036334};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        76     76       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       153    153       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       396    396       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   423 AA;  44592 MW;  7D505B25A48A7134 CRC64;
     MSASAAGLCE FIDASPSPFH VCATVAARLL GAGYTELNEA DPWPPQPGRY FTVRAGSLVA
     WNGDASASAF RIVGAHTDSP NLRVKQHPDR LVAGWQVVAL QPYGGAWLNS WLDRDLGVCG
     RLSVRSAGNG AGITDRLVRI DDPILRVPQL AIHLAEDRKS LTLDPQRHVN AVWGVGDKAG
     SLMGYVAERA GVAAADVLAA DLMTHDLAPS TVMGAAANLL SAPRLDNQAS CYAGMEALLA
     AEPRGFLPVL VLFDHEEVGS ASDRGAQSNL LSTVLERIVL AAGGGRDDYL RRLPASLLAS
     ADMAHATHPN YPERHEPSHL IEVNAGPVLK VHPNLRYATD GRTAAAFELA CHQAGVGLQR
     YEHRADLPCG STIGPLASAR TGIPTVDVGA AQLAMHSARE LMGAHDVAAY SAALQAFLSA
     ELF
//
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