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Database: UniProt
Entry: A0A084JN87_9FIRM
LinkDB: A0A084JN87_9FIRM
Original site: A0A084JN87_9FIRM 
ID   A0A084JN87_9FIRM        Unreviewed;       464 AA.
AC   A0A084JN87;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, 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=IO98_08855 {ECO:0000313|EMBL:KEZ90421.1};
OS   [Clostridium] celerecrescens.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=29354 {ECO:0000313|EMBL:KEZ90421.1, ECO:0000313|Proteomes:UP000028525};
RN   [1] {ECO:0000313|EMBL:KEZ90421.1, ECO:0000313|Proteomes:UP000028525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=152B {ECO:0000313|EMBL:KEZ90421.1,
RC   ECO:0000313|Proteomes:UP000028525};
RA   Honkalas V.S., Dabir A.P., Arora P., Dhakephalkar P.K.;
RT   "Draft genome of Clostridium celerecrescens 152B isolated from
RT   sediments associated with methane hydrate from Krishna Godavari
RT   basin.";
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:KEZ90421.1}.
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DR   EMBL; JPME01000011; KEZ90421.1; -; Genomic_DNA.
DR   RefSeq; WP_038280220.1; NZ_JPME01000011.1.
DR   EnsemblBacteria; KEZ90421; KEZ90421; IO98_08855.
DR   Proteomes; UP000028525; 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:KEZ90421.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028525};
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:UP000028525};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   464 AA;  51660 MW;  280567AA54E99041 CRC64;
     MEKTKGQQLQ EELTFKFPHI AKEAPYQREE AEMFCEGYKR FLDNGKTERE CVREAVAMLE
     MQGYRPFEAG RNYKTGDKVY YVNRGKAIIA TTFGKAGMEQ GLRINGAHID SPRLDLKPNP
     VFEKNDLAYF KTHYYGGIRK YQWGTVPLAI HGVIIKKNGE IVELNIGEKE GDPVFCVTDL
     LPHLAGEQND RKLRDGLKGE ELNVLISSIP FIDEAELKEP VKLLALKLLN DRYGITEADF
     FRAEIELVPA QKACDVGLDH SMIGAYGQDD RVCAYTALMA EIDANMPEYT TVTVLADKEE
     VGSEGNTGLD SDFVLHYIQD LAAMAGVDAR KVLRNSICLS SDVNAAYDPT FGMVYEDRNS
     CFLNKGCVLT KYTGVRGKSG SNDASAELMA KIIAMMEQDG IYWQIGELGA VDQGGGGTIA
     KYVAHMNVDV VDLGVPILSM HSPFELSSKL DVYNTYKAFR AFYK
//
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