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Database: UniProt
Entry: U2DTW1_CLOS4
LinkDB: U2DTW1_CLOS4
Original site: U2DTW1_CLOS4 
ID   U2DTW1_CLOS4            Unreviewed;       465 AA.
AC   U2DTW1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   22-NOV-2017, entry version 17.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF0262_00982 {ECO:0000313|EMBL:ERJ00331.1};
OS   Clostridium sp. (strain ATCC 29733 / VPI C48-50).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1507 {ECO:0000313|EMBL:ERJ00331.1, ECO:0000313|Proteomes:UP000016486};
RN   [1] {ECO:0000313|EMBL:ERJ00331.1, ECO:0000313|Proteomes:UP000016486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29733 {ECO:0000313|EMBL:ERJ00331.1,
RC   ECO:0000313|Proteomes:UP000016486};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R.,
RA   Fronick C., O'Laughlin M., Godfrey J., Miner T., Herter B.,
RA   Appelbaum E., Cordes M., Lek S., Wollam A., Pepin K.H., Palsikar V.B.,
RA   Mitreva M., Wilson R.K.;
RL   Submitted (JUL-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:ERJ00331.1}.
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DR   EMBL; AWTA01000031; ERJ00331.1; -; Genomic_DNA.
DR   RefSeq; WP_021659753.1; NZ_KE993576.1.
DR   EnsemblBacteria; ERJ00331; ERJ00331; HMPREF0262_00982.
DR   PATRIC; fig|1507.3.peg.870; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000016486; 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:ERJ00331.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016486};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ERJ00331.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:ERJ00331.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016486};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   465 AA;  50955 MW;  562E92F0B972412D CRC64;
     MNELSQGQEL AKQLLMDDRN GVEKVGAEEI YQADLFCENY KQFLDCGKTE REVAAQVTAM
     LQQNGYRPFV PQTAYQPGDK VFLNNRGKAI IACTIGRQPV SAGVHIAAAH IDSPRLDLKQ
     RPLYEEKDLA LFKTHYYGGI KKYQWTAIPL ALHGVIVKQS GEVVPVCVGE SADDPVFCVT
     DLLPHLAAEQ MKRTLGDGVK GEELNILIGS RPFLDDKVSE KVKLNIMQIL AQKYGITERD
     FLSAELEMVP AFKAQDVGFD RSMIGAYGHD DRVCAYTALM AEMAAQSPEY TTVTILADKE
     ETGSDGNTGL NSSYLKYFVA DLAACFGANG RDVLSHSRCL SADVNAAYDP TFPDVTEPMN
     TAYLNRGVVV TKFTGSRGKG GTSDASAEYV GYVRRLLEQE NVLWQTGELG KVDAGGGGTV
     ALYIANLNVD VIDVGVPVLS MHAPFEVVSK LDVYMAYRAF RAFYK
//
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