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Database: UniProt
Entry: A0A1V2TJC8_9NOCA
LinkDB: A0A1V2TJC8_9NOCA
Original site: A0A1V2TJC8_9NOCA 
ID   A0A1V2TJC8_9NOCA        Unreviewed;       430 AA.
AC   A0A1V2TJC8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   28-MAR-2018, entry version 8.
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=B0T46_07190 {ECO:0000313|EMBL:ONM49615.1};
OS   Nocardia donostiensis.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=1538463 {ECO:0000313|EMBL:ONM49615.1, ECO:0000313|Proteomes:UP000188836};
RN   [1] {ECO:0000313|EMBL:ONM49615.1, ECO:0000313|Proteomes:UP000188836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=X1655 {ECO:0000313|EMBL:ONM49615.1,
RC   ECO:0000313|Proteomes:UP000188836};
RX   PubMed=26914251; DOI=10.1007/s10482-016-0667-8;
RA   Ercibengoa M., Bell M., Marimon J.M., Humrighouse B., Klenk H.P.,
RA   Potter G., Perez-Trallero E.;
RT   "Nocardia donostiensis sp. nov., isolated from human respiratory
RT   specimens.";
RL   Antonie Van Leeuwenhoek 109:653-660(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:ONM49615.1}.
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DR   EMBL; MUMY01000004; ONM49615.1; -; Genomic_DNA.
DR   RefSeq; WP_077115672.1; NZ_MUMY01000004.1.
DR   Proteomes; UP000188836; 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:ONM49615.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000188836};
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:UP000188836};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        82     82       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       156    156       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       401    401       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   430 AA;  45889 MW;  3E2811A48030A87D CRC64;
     MSVSVTAASA VGLCAFIDES PSPFHVCHTV AQDLDEHGFT RLDETQPWPQ NGRGRHYVVR
     GGSLVAWADA HRATPFRVVG AHTDSPNLRV KQHPDLVSAG WQLVGLEPYG GAWLNSWLDR
     DLGISGRLSV RAGDTVSERL VRINEPILRV PQLAIHLSED RRGVSPDPQR HVNAIWGVGD
     EPRSFLAFVA EHAGIDPDSV LGWELMTHDL SPSHIIGRDR DLVSAPRLDN QGTCYAGLRA
     FLAAVDTPGA AVPVLAMFDH EEVGSQSDRG AQSELLPTVL ERIVLARGGG RADYLAALAG
     SVCASGDMAH ATHPNYPDRH EPAHHIQING GPVLKVNQNL RYATDATGAG AFALACDQAG
     VRLQRYVHRA DLPCGSTVGP MTAARTGIPT VDVGAPQLAM HSARELMGVA DIADYAAALA
     AFLTPETAGR
//
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