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Database: UniProt
Entry: A0A1Y4K7R1_9ACTN
LinkDB: A0A1Y4K7R1_9ACTN
Original site: A0A1Y4K7R1_9ACTN 
ID   A0A1Y4K7R1_9ACTN        Unreviewed;       468 AA.
AC   A0A1Y4K7R1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   28-FEB-2018, entry version 6.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=B5F23_02720 {ECO:0000313|EMBL:OUP39049.1};
OS   Olsenella sp. An188.
OC   Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales;
OC   Atopobiaceae; Olsenella.
OX   NCBI_TaxID=1965579 {ECO:0000313|EMBL:OUP39049.1, ECO:0000313|Proteomes:UP000196278};
RN   [1] {ECO:0000313|EMBL:OUP39049.1, ECO:0000313|Proteomes:UP000196278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An188 {ECO:0000313|EMBL:OUP39049.1,
RC   ECO:0000313|Proteomes:UP000196278};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T.,
RA   Cizek A., Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUP39049.1}.
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DR   EMBL; NFKF01000002; OUP39049.1; -; Genomic_DNA.
DR   Proteomes; UP000196278; 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:OUP39049.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000196278};
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:UP000196278};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   468 AA;  50530 MW;  ABD5DB6D538560FC CRC64;
     MERPNAWKRY SAEQLDALHY LCEGYKSFIS DNKTERECVA ASVRMAEEAG YVNLAERVAS
     GEPLKPGDKV YAVNRGKSLM LAHLGTEPLE RGVNILGAHV DSPRLDVKQD PLEERNELVT
     LDTHYYGGVK KYQWVTMPLA IHGVVCKKDG TTVDVVIGED EADPVFCITD LLPHLGSQQM
     TKKASEVIEG EMLDVLVGNR PIVVEEGAEK DDEAEKSPVK AGVVALLREQ LGIEEEDLLS
     AELEIVPAGA ARDLGLDRSM ILGYGQDDRV CAYTSLVAQL DCKEPARTAV TLLVDKEEIG
     SVGATGMTSH FFEDTMAEIL ELAGETGALA LRRCLAASSM LSSDVSAGFD PAFASVFEPK
     NSAYLGHGLT FNKFTGSRGK SGSNDADAEY VATIRRVMDE GGVAWQTAEL GKVDAGGGGT
     IAYILATYGM SVIDCGVPVL SMHAPWEATS KADVYEAYRG YQEFLKLA
//
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