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Database: UniProt
Entry: U6KI52_EIMTE
LinkDB: U6KI52_EIMTE
Original site: U6KI52_EIMTE 
ID   U6KI52_EIMTE            Unreviewed;       484 AA.
AC   U6KI52;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   25-OCT-2017, entry version 15.
DE   SubName: Full=Aspartyl aminopeptidase, putative {ECO:0000313|EMBL:CDJ37715.1};
GN   ORFNames=ETH_00026985 {ECO:0000313|EMBL:CDJ37715.1};
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ37715.1, ECO:0000313|Proteomes:UP000030747};
RN   [1] {ECO:0000313|EMBL:CDJ37715.1, ECO:0000313|Proteomes:UP000030747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ37715.1,
RC   ECO:0000313|Proteomes:UP000030747};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in
RT   chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDJ37715.1, ECO:0000313|Proteomes:UP000030747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ37715.1,
RC   ECO:0000313|Proteomes:UP000030747};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; HG673774; CDJ37715.1; -; Genomic_DNA.
DR   RefSeq; XP_013228553.1; XM_013373099.1.
DR   MEROPS; M18.002; -.
DR   EnsemblProtists; CDJ37715; CDJ37715; ETH_00026985.
DR   GeneID; 25254493; -.
DR   Proteomes; UP000030747; 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:CDJ37715.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030747};
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:UP000030747};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   484 AA;  53679 MW;  B880BC7B1A83EC19 CRC64;
     MALEEATPLA RRFIKFVNRT GSPYHSVQAV KDFIAGYGFE ELHERTSWKM TQGGRYFVMR
     NGSCIAAFVV GRNFQKEFPG GFCVTATHSD SPCLRLRPRA FAEKEGYQMG SVECYGGGLW
     HTWFDRGLGV AGKVVLRTGN KVEERLVHIP KPLFYVPSLA IHLKTSEEIG ALKINKEQHL
     QPVLCSVIAE HLNQGNGSSI HEGESEVQRL PPALERLVMQ EIGMPGATLL DWDLCLMDAT
     PGRLAGIHLE FIESPRLDNL ASTFAAFEAL VETSIRQRRG EQDCGETEIL MAVAFDHEEV
     GSESLAGANS SLLETWMRRS LKAIGCEDAL HEILAKSFIV SSDMAHAVHP NYSEKHQAQH
     KPSLHKESSE SARSFKYILS LIGVVIKENA NQSYASSATT MSFIRVIAGE ANIPLQDFVV
     RNDSRCGGTV GAMLSARLGI RTVDVGIAQW AMHSCREICG VTDLMYLKNL LEAVYCNFRR
     WDSN
//
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