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Database: UniProt
Entry: A0A098YAI5_9ACTN
LinkDB: A0A098YAI5_9ACTN
Original site: A0A098YAI5_9ACTN 
ID   A0A098YAI5_9ACTN        Unreviewed;       423 AA.
AC   A0A098YAI5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   07-JUN-2017, entry version 11.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=IN07_10525 {ECO:0000313|EMBL:KGH46776.1};
OS   Modestobacter caceresii.
OC   Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
OC   Modestobacter.
OX   NCBI_TaxID=1522368 {ECO:0000313|EMBL:KGH46776.1, ECO:0000313|Proteomes:UP000029713};
RN   [1] {ECO:0000313|EMBL:KGH46776.1, ECO:0000313|Proteomes:UP000029713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNN45-2b {ECO:0000313|EMBL:KGH46776.1,
RC   ECO:0000313|Proteomes:UP000029713};
RA   Bukarasam K., Bull A., Girard G., van Wezel G., Goodfellow M.;
RT   "Biosystematic studies on Modestobacter strains isolated from extreme
RT   hyper-arid desert soil and from historic building.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {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:KGH46776.1}.
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DR   EMBL; JPMX01000041; KGH46776.1; -; Genomic_DNA.
DR   RefSeq; WP_036335594.1; NZ_JPMX01000041.1.
DR   EnsemblBacteria; KGH46776; KGH46776; IN07_10525.
DR   Proteomes; UP000029713; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KGH46776.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029713};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029713};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   423 AA;  44367 MW;  0F9F8E41B9729DCC CRC64;
     MPDLSLGDDL RAFVDTSPSP SHAVAELARR LRAAGFTELA EADRWELAPG GQHFVVRHGS
     LIAFRVGSAS PAEAGLRLVG AHTDSPTFKV RPRDDVRQAG YRLVGVEPYG GGLWHTWLDR
     ELTVAGRVAL RGGGTALVRL PGAALRLPSL AIHLDRSVRE GLKLDPQREL VPVWSQDLGT
     EPGLREALAT EVGAAVQDVV GHDLVLADTQ PAGRTGADGS WIAAPRLDNL ASCHAGVTAL
     IAAAATSRTQ LLVANDHEEV GSGSMSGARG SFLEDVVRRL VAVLDAGDPQ ALPRALAQSR
     LVSADMAHAV HPTRSDRHEP GHQPQLGSGP VLKVNANQAY ATDAVTSGWF AERCAEASVP
     VQWFVTRADL PCGSTIGPLT ATRLGIATVD VGAPMLAMHS ARELASALDV PLMVGALTAC
     FAD
//
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