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Database: UniProt
Entry: A0A0N1HTZ6_LEPSE
LinkDB: A0A0N1HTZ6_LEPSE
Original site: A0A0N1HTZ6_LEPSE 
ID   A0A0N1HTZ6_LEPSE        Unreviewed;       451 AA.
AC   A0A0N1HTZ6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   25-OCT-2017, entry version 7.
DE   SubName: Full=Putative Aspartyl aminopeptidase {ECO:0000313|EMBL:KPI84694.1};
GN   ORFNames=ABL78_6263 {ECO:0000313|EMBL:KPI84694.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae;
OC   Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI84694.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI84694.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI84694.1,
RC   ECO:0000313|Proteomes:UP000038009};
RX   PubMed=26317207;
RA   Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J.,
RA   Grybchuk D., Lestinova T., Votypka J., Volf P., Opperdoes F.,
RA   Flegontov P., Lukes J., Yurchenko V.;
RT   "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed
RT   by Genome Sequencing, Transcriptome Profiling and Co-infection with
RT   Leishmania donovani.";
RL   PLoS Pathog. 11:E1005127-E1005127(2015).
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:KPI84694.1}.
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DR   EMBL; LJSK01000239; KPI84694.1; -; Genomic_DNA.
DR   EnsemblProtists; KPI84694; KPI84694; ABL78_6263.
DR   Proteomes; UP000038009; 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:KPI84694.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000038009};
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:UP000038009};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   451 AA;  49289 MW;  373A79B451327794 CRC64;
     MATLKSEHAV SMAKEFVNFM NEAITPFHAV QTVATMLQKA GFSRLDEGKA WPDMTPGGKY
     YLTRNGSSIV AFAVGGKFDP ANGVKIVGAH TDSPTFLLKP HTKSSSTNYH RVAVQCYGGG
     LWHSWFDRDL TVAGRVVISR DRLEEKIIKI DKPIMRIPNL AIHLTSAKER EGFAPNKESH
     LIPVICTEIA KKIAAREGEE TTSATQCTAL MNAIADEAGC KPEEILDFDL SVVDTQPATF
     GGIYDEFIFS ARLDNLISCY CAIKAIIDAE ALENDTMVRM VCLFDHEECG SSSPHGAAGS
     LVPDVIEHLT SNKTLRATLV ANSFLLSVDG AHGCHPNYTD KHENAHRPEL HEGPVIKYNA
     NVRYATNGVT AAVVKHLAKK VNVPVQEFVV RNDSPCGSTI GPILSTLTGI KTADIGNPMI
     SMHSVREMCG TLDIYYMTKL IESFFVNYEN P
//
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