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Database: UniProt
Entry: A0A0V0WM66_9BILA
LinkDB: A0A0V0WM66_9BILA
Original site: A0A0V0WM66_9BILA 
ID   A0A0V0WM66_9BILA        Unreviewed;       467 AA.
AC   A0A0V0WM66;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   25-OCT-2017, entry version 6.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KRX76744.1};
GN   Name=DNPEP {ECO:0000313|EMBL:KRX76744.1};
GN   ORFNames=T06_13107 {ECO:0000313|EMBL:KRX76744.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichocephalida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX76744.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX76744.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX76744.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX76744.1}.
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DR   EMBL; JYDK01000094; KRX76744.1; -; Genomic_DNA.
DR   Proteomes; UP000054673; 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   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:KRX76744.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054673};
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:UP000054673};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   467 AA;  51858 MW;  505BCFA0F1F6DF4C CRC64;
     MNGKCCSITN NAYVGEFVKF LNKAVTPYHV INYCRSSFAD ANFVELNDGD QWQITPGRSY
     FVVKNESSVI AFAVGGKFKP GNAANIIATH TDSPCLKVKP IATAGYANWK QVSVTTYGGG
     IWRTWFDREL TVAGRLFVKE NESVHMKLFN LEHPLLFLPN LAIHLDRDSN TTFTFNAEEH
     LKPIFTFTSN TTNDKSKVMS IIDIIGRRLE INPENILSSD VFLVPVQEAT TGGLVGEFIF
     GARLDNLMST YNGLTSILTI SQDQAWMNSS ESISMFAAFD NEECGSMSAQ GAMSSWTEWV
     LRRLQNDAFE RSIAKSFLIS ADVAHAIHPN YKSKHDTNHC PEFGKGIVIK LNANQRYATS
     GSSLAKMIRL ADMTCTPHQF YTNRNDIGCG STVGPILASK LAIETVDVGA PLLAMHSVRE
     MGCTFGLVCG DTFFKGFFYR MHEVEKEFNK NVTSIEQKSA TEVDKHL
//
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