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Database: UniProt
Entry: A0A0F2TCF8_9ACTN
LinkDB: A0A0F2TCF8_9ACTN
Original site: A0A0F2TCF8_9ACTN 
ID   A0A0F2TCF8_9ACTN        Unreviewed;       435 AA.
AC   A0A0F2TCF8;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-NOV-2017, entry version 12.
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=VM95_18350 {ECO:0000313|EMBL:KJS60854.1};
OS   Streptomyces rubellomurinus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=359131 {ECO:0000313|EMBL:KJS60854.1, ECO:0000313|Proteomes:UP000033699};
RN   [1] {ECO:0000313|EMBL:KJS60854.1, ECO:0000313|Proteomes:UP000033699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31215 {ECO:0000313|EMBL:KJS60854.1,
RC   ECO:0000313|Proteomes:UP000033699};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-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:KJS60854.1}.
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DR   EMBL; JZKH01000035; KJS60854.1; -; Genomic_DNA.
DR   RefSeq; WP_045698086.1; NZ_JZKH01000035.1.
DR   EnsemblBacteria; KJS60854; KJS60854; VM95_18350.
DR   PATRIC; fig|359131.3.peg.4287; -.
DR   Proteomes; UP000033699; 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:KJS60854.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033699};
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:UP000033699};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        89     89       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       160    160       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       411    411       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   435 AA;  45934 MW;  9B1DAA8C72F3E4CA CRC64;
     MSTAAQQAYF DRTHSDDLIA FLGTSPSPYH AVASAAERLE KAGFRKVSET EAWDAAPGGR
     YLVRGGALIA WYLPEGAGPE TPFRVVGTHT DSPNLRVKPV PDTGSAGWRQ VAVEIYGGVP
     LNTWLDRDLG LSGRLALKDG SARLVQLDEP LLRVPQLAIH LDRSVNDGMK LDRQRHLTPI
     WGLGPVDEGS LIAYVAERAG LAAEDVVGWD LMTHDIQPAS YLGRDRELLA APRLDNLLSV
     HAGTAALAAV ASSEGAAALP YIPVLAAFDH EETGSESDTG AQSPLLGNVL DRTIHARGGT
     PEDRARALAG TVCLSSDMGH AVHPNYPERH EPGHHPVPNG GPILKVNVNN RYATDGVGRA
     VFAAACEKAG VPWQTFVSNN AVACGTTIGP ITAARLGIKT VDCGIAALSM HSARELCGAE
     DPHLLASALK AFLEG
//
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