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Database: UniProt
Entry: K2N0L5_TRYCR
LinkDB: K2N0L5_TRYCR
Original site: K2N0L5_TRYCR 
ID   K2N0L5_TRYCR            Unreviewed;       450 AA.
AC   K2N0L5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   25-OCT-2017, entry version 11.
DE   SubName: Full=Aspartyl aminopeptidase, putative,metallo-peptidase, clan MH, family M20, putative {ECO:0000313|EMBL:EKF32950.1};
GN   ORFNames=MOQ_003191 {ECO:0000313|EMBL:EKF32950.1};
OS   Trypanosoma cruzi marinkellei.
OC   Eukaryota; Euglenozoa; Kinetoplastida; Trypanosomatidae; Trypanosoma;
OC   Schizotrypanum.
OX   NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF32950.1, ECO:0000313|Proteomes:UP000007350};
RN   [1] {ECO:0000313|EMBL:EKF32950.1, ECO:0000313|Proteomes:UP000007350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B7 {ECO:0000313|EMBL:EKF32950.1,
RC   ECO:0000313|Proteomes:UP000007350};
RX   PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA   Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA   Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA   Andersson B.;
RT   "Comparative genomic analysis of human infective Trypanosoma cruzi
RT   lineages with the bat-restricted subspecies T. cruzi marinkellei.";
RL   BMC Genomics 13:531-531(2012).
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:EKF32950.1}.
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DR   EMBL; AHKC01009511; EKF32950.1; -; Genomic_DNA.
DR   EnsemblProtists; EKF32950; EKF32950; MOQ_003191.
DR   Proteomes; UP000007350; 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:EKF32950.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007350};
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:UP000007350};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   450 AA;  49589 MW;  BE8A5396E35329E3 CRC64;
     MSFGSPFSME LAKEFVEFIN KACTPFHAVE VISSWLLEAG YKRLNEGEPW PSISVGDRYF
     VTRNDSSLVA FSVGGKFEPA NGVKIVGAHT DSPNLALKPR TRVDKGEYQG IAVQCYGGGL
     WHTWFDRDLT VAGRVFLSRT KLEKRLVNLK RPIVRIPSLA IHLQTAQERE GFAPNKEKHL
     VPIIATEISG ALNGDDDKRH SFHLMKLISE ALGCLPEEIV DYDLSVIDTQ PATIGGAFDE
     FIFAPRLDNL ISCFCGIKAL LQTDKSLDTE NMIRMVCLFD NEEIGSETSQ GAGGTLVPDL
     IEHIIASKTL RATLVANSFL LSVDGAHALH PNYKDKHEEN HRPLLHRGPV IKYNANMRYA
     TNGATASIVK SIAKEALVPV QEFCVRNDSS CGSTIGPILS SLSGIRTVDI GNPMLSMHSV
     REMCGTTDIS YLTNFIEAFF TNYDKHVISS
//
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