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Database: UniProt
Entry: A0A101WTF9_9FIRM
LinkDB: A0A101WTF9_9FIRM
Original site: A0A101WTF9_9FIRM 
ID   A0A101WTF9_9FIRM        Unreviewed;       440 AA.
AC   A0A101WTF9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   22-NOV-2017, entry version 6.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=APF81_18310 {ECO:0000313|EMBL:KUO78865.1};
OS   Desulfosporosinus sp. BRH_c37.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfosporosinus.
OX   NCBI_TaxID=1734396 {ECO:0000313|EMBL:KUO78865.1, ECO:0000313|Proteomes:UP000053148};
RN   [1] {ECO:0000313|EMBL:KUO78865.1, ECO:0000313|Proteomes:UP000053148}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c37 {ECO:0000313|EMBL:KUO78865.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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:KUO78865.1}.
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DR   EMBL; LOEW01000020; KUO78865.1; -; Genomic_DNA.
DR   Proteomes; UP000053148; 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:KUO78865.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053148};
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:UP000053148};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   440 AA;  48812 MW;  414027536E443D10 CRC64;
     MRKSVITTEE LQFALELLDF INQSPSSFHA VESVKRILDL EGFRELPLEE KWSLSQGGKY
     FVIRNSSALI AFIVGQGEPD LNGFHLIGAH TDSPSFRVKP LSEIPIEGHY LKLNVETYGG
     PILNTWLDRP LSLAGRIVLR GESPFAPHIK LFRSDRPLLV IPNLAIHMNR KVNEGVELNK
     QKDMLPLLAQ ITEDLRKEGI LLHHLAEILN CPPEDILDFD LFLYEYEKGC LVGLQQEFIS
     SGRLDDLAMI HAGTWALAKA KPALMTQVLA CFDHEECGST SKQGAASPFL AHVLERILLA
     QNKDREAYFQ ALAHSFFISA DMAHALHPNA GEKHDPVNRP ILNGGPVIKI SANQSYTTDA
     ESSAVFAALC QRAGVQFQKF VNRSDERGGS TIGPISSTHL DIRSVDIGNP ILAMHSVREL
     GGVKDHLAIA NVFSEFYKTR
//
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