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Database: UniProt
Entry: V2Z3N4_9FIRM
LinkDB: V2Z3N4_9FIRM
Original site: V2Z3N4_9FIRM 
ID   V2Z3N4_9FIRM            Unreviewed;       431 AA.
AC   V2Z3N4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   07-JUN-2017, entry version 16.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=GCWU0000282_003109 {ECO:0000313|EMBL:ESL01550.1};
OS   Catonella morbi ATCC 51271.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Catonella.
OX   NCBI_TaxID=592026 {ECO:0000313|EMBL:ESL01550.1, ECO:0000313|Proteomes:UP000018227};
RN   [1] {ECO:0000313|EMBL:ESL01550.1, ECO:0000313|Proteomes:UP000018227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51271 {ECO:0000313|EMBL:ESL01550.1,
RC   ECO:0000313|Proteomes:UP000018227};
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., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (JUN-2013) 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:ESL01550.1}.
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DR   EMBL; ACIL03000021; ESL01550.1; -; Genomic_DNA.
DR   RefSeq; WP_023355950.1; NZ_KI535371.1.
DR   ProteinModelPortal; V2Z3N4; -.
DR   EnsemblBacteria; ESL01550; ESL01550; GCWU0000282_003109.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000018227; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ESL01550.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018227};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ESL01550.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:ESL01550.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018227};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   431 AA;  47376 MW;  65F44443E1CA0FDE CRC64;
     MDKYLEASKR LIGFLDANPS PFHVIAALGK MYENAGFKRL SEKERFEVKK GGNYYVTRNN
     SSIIAFKIPK KDFKGFNITA AHSDSPTFKI KANAEITAEK NFVKLNVEKY GGMLMAPWFD
     RPLGIAGRVM VKKGTKIEEN LIHIDRDIIM IPNLAIHMNR EANDGYKYNA QTDTQPIFAE
     LGSDVTLYDI IAKELGVSKD AILDTDLFLT NRVKGTVWGA NNEFIAAGRL DDLQCVFAGA
     ESIIEAKNKN NIAVHCVFDN EEVGSGTKQG AASTFLKDVL TRVNKALGGD EESYLQAVAR
     SFMVSADNAH SVHPNYTEKA DPCNRPVVNK GVVIKYNANQ KYTTDAVSGA VFRDICAEAE
     VPVQTFTNRS DVAGGSTLGN ISNAQVSLNA VDIGMAQWAM HSPYESGGVK DTYYLEAAMK
     KFFETDISAK I
//
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