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Database: UniProt
Entry: A0A0B3VI07_9FIRM
LinkDB: A0A0B3VI07_9FIRM
Original site: A0A0B3VI07_9FIRM 
ID   A0A0B3VI07_9FIRM        Unreviewed;       430 AA.
AC   A0A0B3VI07;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=QX51_13480 {ECO:0000313|EMBL:KHS56451.1};
OS   Terrisporobacter othiniensis.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae; Terrisporobacter.
OX   NCBI_TaxID=1577792 {ECO:0000313|EMBL:KHS56451.1, ECO:0000313|Proteomes:UP000031189};
RN   [1] {ECO:0000313|EMBL:KHS56451.1, ECO:0000313|Proteomes:UP000031189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=08-306576 {ECO:0000313|EMBL:KHS56451.1,
RC   ECO:0000313|Proteomes:UP000031189};
RA   Lund L.C., Sydenham T.V., Hogh S.V., Skov M.N., Kemp M.,
RA   Justesen U.S.;
RT   "Draft genome sequence of Terrisporobacter sp. 08-306576, isolated
RT   from the blood culture of a bacteremia patient.";
RL   Submitted (DEC-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:KHS56451.1}.
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DR   EMBL; JWHR01000112; KHS56451.1; -; Genomic_DNA.
DR   RefSeq; WP_039680419.1; NZ_JWHR01000112.1.
DR   EnsemblBacteria; KHS56451; KHS56451; QX51_13480.
DR   Proteomes; UP000031189; 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:KHS56451.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031189};
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:UP000031189};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   430 AA;  48155 MW;  DE66957F67E804D1 CRC64;
     MKKQFAENLI DYIYNSPTAF NAVKTSKDLL MKNGFKELKM NEKWQLKVGG KYFITKNASS
     LTAFVVNSDN MQEGFRIIGS HSDSPTFRIK PDAEMTVENT YLKLNTEGYG GSILSTWFDR
     PLSIAGRVVL KSEDILCPRE EIININRPIC IIPNLAIHMN RTVNDGYKFN KQKDTLPLVG
     LLNETLEKDE FLLKEISKAL NINKEDILDF DLYLYEYEKG SIIGPNEEFI SSSRLDNLSM
     AHASLYALID SKGKKGINVV AIFDNEEVGS STKQGADSNM LLNLLERICI SLKKDREDFI
     SAIYSSFMIS ADLAHALHPN IVEKHDPTNR PVMGGGPVIK ISANQSYTSD AFSAGIYKSI
     CEKCGVKYQQ FVNRSDERGG STIGPISSTH LDINSVDIGS PILSMHSVRE LGSVEDHYNI
     YKTFVGFYQI
//
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