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Database: UniProt
Entry: G9YJ17_9FIRM
LinkDB: G9YJ17_9FIRM
Original site: G9YJ17_9FIRM 
ID   G9YJ17_9FIRM            Unreviewed;       455 AA.
AC   G9YJ17;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   22-NOV-2017, entry version 29.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF0080_01661 {ECO:0000313|EMBL:EHM39061.1};
OS   Anaeroglobus geminatus F0357.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Anaeroglobus.
OX   NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM39061.1, ECO:0000313|Proteomes:UP000005481};
RN   [1] {ECO:0000313|EMBL:EHM39061.1, ECO:0000313|Proteomes:UP000005481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0357 {ECO:0000313|EMBL:EHM39061.1,
RC   ECO:0000313|Proteomes:UP000005481};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) 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:EHM39061.1}.
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DR   EMBL; AGCJ01000073; EHM39061.1; -; Genomic_DNA.
DR   RefSeq; WP_006790628.1; NZ_JH417605.1.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EHM39061; EHM39061; HMPREF0080_01661.
DR   PATRIC; fig|861450.3.peg.1534; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000005481; 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   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|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EHM39061.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005481};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EHM39061.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EHM39061.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005481};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   455 AA;  50552 MW;  8B3A6E1436FABFB8 CRC64;
     MKAFDKENNV WSRFSEKERV KMEEYCKNYR FFLDTARTER LAVKEILSQA ESAGFRSIDS
     YTKLAAGDKV YWNQKNKAVV LAVIGKEPLE AGAKIVGSHI DCPRLDLKAA PVFEKDKLVY
     FKTHYYGGIL KYQWVCQPLS LICVVCMSNG RKVDVSIGDG PDDPVFYIND LLPHLGKDQA
     AKKLNDAIEG EMLMPIIGTH GEEEKTKPAV LKLFKDKYGI EEEDFASAEL EIIPAQKSRD
     VGLDRSMIMA HGHDDRVCSY ASNAGILDAK AGAKTQIALF ADKEEIGSVG NTGVQSSYFL
     DFMAELLALQ GKTEELYLRR MLRHSRVLSA DVNAALDPIF ASAYEESNAA RFGYGICLSK
     YTRRRGKSGS NDANAEFLAE VRRIFNENNV PWQTGELGKV DQGGGGTIAY IMADWGCEVV
     DCGVAMLSMH APLELVSKAD AYCAYLAYKA FFESK
//
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