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Database: UniProt
Entry: A0A0Q6BF35_9PROT
LinkDB: A0A0Q6BF35_9PROT
Original site: A0A0Q6BF35_9PROT 
ID   A0A0Q6BF35_9PROT        Unreviewed;       434 AA.
AC   A0A0Q6BF35;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-FEB-2018, entry version 12.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=ASG34_04600 {ECO:0000313|EMBL:KQT44040.1};
OS   Methylophilus sp. Leaf416.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylophilus.
OX   NCBI_TaxID=1736373 {ECO:0000313|EMBL:KQT44040.1, ECO:0000313|Proteomes:UP000050891};
RN   [1] {ECO:0000313|EMBL:KQT44040.1, ECO:0000313|Proteomes:UP000050891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf416 {ECO:0000313|EMBL:KQT44040.1,
RC   ECO:0000313|Proteomes:UP000050891};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT44040.1, ECO:0000313|Proteomes:UP000050891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf416 {ECO:0000313|EMBL:KQT44040.1,
RC   ECO:0000313|Proteomes:UP000050891};
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:KQT44040.1}.
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DR   EMBL; LMQS01000001; KQT44040.1; -; Genomic_DNA.
DR   RefSeq; WP_055827030.1; NZ_LMQS01000001.1.
DR   EnsemblBacteria; KQT44040; KQT44040; ASG34_04600.
DR   Proteomes; UP000050891; 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   Gene3D; 2.30.250.10; -; 1.
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|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KQT44040.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050891};
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:UP000050891};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   434 AA;  46922 MW;  937DD2B1DBC6C5CE CRC64;
     MQVSIEARQR AQALLNFIDV SPSPWHAVTQ VEQVLAAQGF TQLNESDAWQ FTQGGKYYVV
     RDGGSIIAFV LGQAAIAEHG FRIVGAHTDS PGLRLKPKAA YSTEGIAQLG VEVYGGPILA
     TFTDRDLGLA GRVIVKTVSG LSSHLVKLDQ PIARLPNLAI HMNREVNEKG LVLNKQTGLP
     LIFGHAANSE AAKQLLSDTL ASSLQVNAAD ILSWDLAFYD TQRGSFWGIE QEFIANSQLD
     NLASCHAAME AMIGTEKPQA TSICALFDHE EVGSESATGA GGSFLLDVME RICHSHDLSH
     EDKLRSYSQS FFISADMAHA FHPSHAGSYE PCHHVQVNQG PVIKTNANQR YSTNAATAAR
     FIQLCDRAGV PYQQYAHRTD LGCGSTIGPI MAAQLGIATV DVGNPMWAMH SIRESAGVLD
     HEYMIATLKQ HFAS
//
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