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Database: UniProt
Entry: L1MHD0_9CORY
LinkDB: L1MHD0_9CORY
Original site: L1MHD0_9CORY 
ID   L1MHD0_9CORY            Unreviewed;       419 AA.
AC   L1MHD0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-2017, entry version 19.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF9997_01189 {ECO:0000313|EMBL:EKX90693.1};
OS   Corynebacterium durum F0235.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1035195 {ECO:0000313|EMBL:EKX90693.1, ECO:0000313|Proteomes:UP000010445};
RN   [1] {ECO:0000313|EMBL:EKX90693.1, ECO:0000313|Proteomes:UP000010445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0235 {ECO:0000313|EMBL:EKX90693.1,
RC   ECO:0000313|Proteomes:UP000010445};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R.,
RA   Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M.,
RA   Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C.,
RA   Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S.,
RA   Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (MAY-2012) 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:EKX90693.1}.
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DR   EMBL; AMEM01000017; EKX90693.1; -; Genomic_DNA.
DR   RefSeq; WP_006063426.1; NZ_KB290831.1.
DR   EnsemblBacteria; EKX90693; EKX90693; HMPREF9997_01189.
DR   PATRIC; fig|1035195.3.peg.1069; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000010445; 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:EKX90693.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010445};
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:UP000010445};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   419 AA;  44621 MW;  104B003EE0AD55AD CRC64;
     MRSFLDFIAS SPSSFHAAHQ VARRLDQAGF AEQDEAEPWD ASPGGHYVVR GGAIMAWWVP
     ENASPESGFR IVGSHTDSPG FKVKPGTDFT TVGWQQVAVE VYGGPILTSW FDRELVLAGR
     VILSDGSEKM VATGPLLRIP NLAIHLSRDK AQDASVLSRQ VHLQPVMGVG DPEASVLDVV
     AASAGVDKHD IVAHDLITCD AQRGEMFGAN MDLVAAGRLD NLSSVYASLE AFIAALQSGD
     AGNDVLVLAA FDHEEVGSAT ISGAAGPLLE NVLVRTAQAL EADTEDLHRM FARSWCVSAD
     AAHSVHPNYV GKHDPVTQPL VNHGPVVKMN ANQRYASDAV TWALWERACR DAGVPSQVFV
     GNNDSPCGST IGPITATRLG IRTVDVGIAL LSMHSARELC GAHDMGWFPQ ALEAFFVGD
//
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