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Database: UniProt
Entry: A0A0L0DGY4_THETB
LinkDB: A0A0L0DGY4_THETB
Original site: A0A0L0DGY4_THETB 
ID   A0A0L0DGY4_THETB        Unreviewed;       497 AA.
AC   A0A0L0DGY4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 11.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:KNC51599.1};
GN   ORFNames=AMSG_07507 {ECO:0000313|EMBL:KNC51599.1};
OS   Thecamonas trahens ATCC 50062.
OC   Eukaryota; Apusozoa; Apusomonadidae; Thecamonas.
OX   NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC51599.1, ECO:0000313|Proteomes:UP000054408};
RN   [1] {ECO:0000313|EMBL:KNC51599.1, ECO:0000313|Proteomes:UP000054408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC51599.1,
RC   ECO:0000313|Proteomes:UP000054408};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA   Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA   Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T.,
RA   Howarth C., Jen D., Larson L., Mehta T., Park D., Pearson M.,
RA   Roberts A., Saif S., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   Thomson T., Walk T., White J., Yandava C., Burger G., Gray M.W.,
RA   Holland P.W.H., King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I.,
RA   Lander E., Nusbaum C.;
RT   "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL   Submitted (MAY-2010) 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; GL349468; KNC51599.1; -; Genomic_DNA.
DR   RefSeq; XP_013755997.1; XM_013900543.1.
DR   EnsemblProtists; KNC51599; KNC51599; AMSG_07507.
DR   GeneID; 25566411; -.
DR   Proteomes; UP000054408; 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   PANTHER; PTHR28570; PTHR28570; 1.
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:KNC51599.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054408};
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:UP000054408};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   497 AA;  52367 MW;  644A0E2A00C7953C CRC64;
     MSSSSPTLAT ASAAVDFINA SPSAFHAVAT TRETLLGAGF VELAEGEVWT LETGGKYFVT
     RNQSAVMAFA VGGGYTPGAG FTMLGAHTDS PCLKVKPISH KASEGLLTVG VEVYGGPILH
     SWFDRDLGLA GRVVVRKADG SLGSHLVRVH RPLLRVPTLA IHLDRKVNSG FSFNAETELL
     PVLGSAFQLA FATDDAPAGA AATSDTEFEV SLGHSTVLLD VLLEALAAED GCAGLARDAI
     VDFDLVMYDV QDGTLGGAQN EFIFASQLDN LMMSFCGLRG LLGSLDSLAD DTNVRLVALF
     DNEEVGSQSE HGANSNLLQR LVERIIHGLA EAAAAAGSPD VQLSSLYDRT IRKSFFVSAD
     MAHAAHPNYR SKHPDTSRPA MNKGPVIKYN ARERYATTGV SAAILKEVAA RADVPLQAFA
     CRNDIPCGST IGPMTSAHLG VRTVDMGNPQ LSMHSAREMC GSRDPALAIA LFEAYFTHFA
     AIDATLHESF PAAAASS
//
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