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Database: UniProt
Entry: A0A0Q5VKI9_9ACTN
LinkDB: A0A0Q5VKI9_9ACTN
Original site: A0A0Q5VKI9_9ACTN 
ID   A0A0Q5VKI9_9ACTN        Unreviewed;       420 AA.
AC   A0A0Q5VKI9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 9.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=ASG36_18105 {ECO:0000313|EMBL:KQS56914.1};
OS   Geodermatophilus sp. Leaf369.
OC   Bacteria; Actinobacteria; Geodermatophilales; Geodermatophilaceae;
OC   Geodermatophilus.
OX   NCBI_TaxID=1736354 {ECO:0000313|EMBL:KQS56914.1, ECO:0000313|Proteomes:UP000051830};
RN   [1] {ECO:0000313|EMBL:KQS56914.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS56914.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS56914.1, ECO:0000313|Proteomes:UP000051830}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf369 {ECO:0000313|EMBL:KQS56914.1,
RC   ECO:0000313|Proteomes:UP000051830};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQS56914.1}.
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DR   EMBL; LMQA01000004; KQS56914.1; -; Genomic_DNA.
DR   EnsemblBacteria; KQS56914; KQS56914; ASG36_18105.
DR   Proteomes; UP000051830; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KQS56914.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051830};
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:UP000051830};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   420 AA;  44006 MW;  6CF8621DDEEF5404 CRC64;
     MDLTLGDDLR SFVDASPSPG HAAAEIARRL IEGGFRELTE TDLWELSPGD AVFTVRGASV
     VAVRVGTEPA HEAGLRIIGA HTDSPTFRVR PRHDVRQAGY RLVGVEPYGG GLWHTWLDRE
     LTVAGRLALR GGTTTLVTLP GAPLRLPSLA IHLDRSVREG LTLDPQRHLQ PVWGSDLDTE
     PGLLEALAAA AGVAAGDIVG HDLVLADTQP AARAGADGSW IAAPRLDDLA CCHSGLLALL
     GVSAETRHTQ VLVCNDHEEV GSGSASGARG SFLEDVISRL AGSQPQAFAR TIAASKLVSA
     DMAHAVHPTR SERHEPSHQP VLGGGPVLKL NANQAYATDA VSGGWFTERC EAAGVPVQHF
     VSRADLPCGS TIGPLTATRL GLSTVDVGAP QLAMHSVREL ASAADVPLMV AAFRNCLQIS
//
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