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Database: UniProt
Entry: D2VD00_NAEGR
LinkDB: D2VD00_NAEGR
Original site: D2VD00_NAEGR 
ID   D2VD00_NAEGR            Unreviewed;       476 AA.
AC   D2VD00;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   07-JUN-2017, entry version 40.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC45394.1};
GN   ORFNames=NAEGRDRAFT_66747 {ECO:0000313|EMBL:EFC45394.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Heterolobosea; Schizopyrenida; Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC45394.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC45394.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B.,
RA   Carpenter M.L., Field M.C., Kuo A., Paredez A., Chapman J., Pham J.,
RA   Shu S., Neupane R., Cipriano M., Mancuso J., Tu H., Salamov A.,
RA   Lindquist E., Shapiro H., Lucas S., Grigoriev I.V., Cande W.Z.,
RA   Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; GG738863; EFC45394.1; -; Genomic_DNA.
DR   ProteinModelPortal; D2VD00; -.
DR   STRING; 5762.XP_002678138.1; -.
DR   MEROPS; M18.002; -.
DR   EnsemblProtists; EFC45394; EFC45394; NAEGRDRAFT_66747.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   InParanoid; D2VD00; -.
DR   Proteomes; UP000006671; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006671};
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:UP000006671};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   476 AA;  52534 MW;  63FAD20D2447AB6E CRC64;
     MAPSLEELSN AQPITQKMVD FINESKSPYH AVGSIKKRLL DSGYEQLFER EANWEQKIKP
     CGKYFFTRNH STIVAFAVGG KFAAGTSGLK IIGAHTDSPH LVIKPISSQK SSGYLQVGVQ
     TYGGGLWYTW FDRDLTVAGR VILSDGQGKF KQHLVEVKRP ILRIPSLAIH LQREVSTDGF
     KPNTELHLLP IIGTELGELS DDPNTKGFIA NHHSVLLKAI AEELKCNVAD IRDFDMSIAD
     VQPGVIGGVN NEFVFAPRLD NLASCFVSLE ALLNSENTLA TEKDIRMICL FDHEEVGSTS
     SYGADSSLIN DTINRVIQCT HASFDKNAPV DSYGACIANS FIISCDMAHA VHPNYSEKHQ
     AKHRPQIHQG LVIKTNANQR YATNGHTSFL FGELAKRHNI PIQQFVVRND SACGSTIGPI
     TSSNTSIRTI DVGIPQLSMH SIREQCGCVD IKSTIDLFTE YFNEFSEIDS TLHIDE
//
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