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Database: UniProt
Entry: I0RDH0_MYCXE
LinkDB: I0RDH0_MYCXE
Original site: I0RDH0_MYCXE 
ID   I0RDH0_MYCXE            Unreviewed;       418 AA.
AC   I0RDH0;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-SEP-2017, entry version 32.
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=MXEN_21085 {ECO:0000313|EMBL:EID09173.1};
OS   Mycobacterium xenopi RIVM700367.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID09173.1, ECO:0000313|Proteomes:UP000003584};
RN   [1] {ECO:0000313|EMBL:EID09173.1, ECO:0000313|Proteomes:UP000003584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIVM700367 {ECO:0000313|EMBL:EID09173.1,
RC   ECO:0000313|Proteomes:UP000003584};
RX   PubMed=22628510; DOI=10.1128/JB.00482-12;
RA   Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA   van Soolingen D., Bitter W., Pain A.;
RT   "Complete Genome Sequence of Mycobacterium xenopi Type Strain
RT   RIVM700367.";
RL   J. Bacteriol. 194:3282-3283(2012).
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:EID09173.1}.
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DR   EMBL; AJFI01000109; EID09173.1; -; Genomic_DNA.
DR   RefSeq; WP_003923245.1; NZ_AJFI01000109.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EID09173; EID09173; MXEN_21085.
DR   PATRIC; fig|1150591.3.peg.4241; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000003584; 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:EID09173.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003584};
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:UP000003584};
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       150    150       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       393    393       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   418 AA;  44476 MW;  71DFCA7FD803256E CRC64;
     MTATPAGLCE FIDASPSPFH VCATVARALR AAGYVELAET EAWPCAGKFF TVRAGSVVAW
     HSAGASAAPF RVIGAHTDSP NLRVKQRPDR VVAGWQVVAL QPYGGAWLNS WLDRDLGISG
     RLSVRDGARV SHRLVRIDDP ILRVPQLAIH LAEDRKSLTL DPQHHVNAVW AAGDSTRSFV
     GYVAERAGVG PDDVLGFDLM THDLAPSTLA GVDDQFLSAP RLDNQASCYA GLEALLAAEP
     DRYLPVLVLF DHEEVGSSSD HGAQSELLLT TLERVVLAAG GDREDFLRRM AGSMMASADM
     AHATHPNYPD RHEPGHPVTI NGGPVLKVQP NLRYATDGRT AAAFALACRQ AGVALQRYEH
     RADLPCGSTI GPIASARTGI PTVDVGAPQL AMHSARELMG AADVTAYSAA LQAFLAPQ
//
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