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Database: UniProt
Entry: W5MXA5_LEPOC
LinkDB: W5MXA5_LEPOC
Original site: W5MXA5_LEPOC 
ID   W5MXA5_LEPOC            Unreviewed;       474 AA.
AC   W5MXA5;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   25-OCT-2017, entry version 15.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|Ensembl:ENSLOCP00000013014};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000013014, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Ensembl:ENSLOCP00000013014, ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000013014}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2014) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSLOCP00000013014}.
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DR   EMBL; AHAT01034388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01034389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSLOCT00000013042; ENSLOCP00000013014; ENSLOCG00000010615.
DR   GeneTree; ENSGT00390000003164; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; EOG091G06FO; -.
DR   Proteomes; UP000018468; 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   Complete proteome {ECO:0000313|Proteomes:UP000018468};
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:UP000018468};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   474 AA;  51618 MW;  31A31E3F5373BA64 CRC64;
     MQSAIMKSSK EAVQTAAKEF LQFVNRGVSP YHVVQECKAM LLGAGFKELK ETEHWSIEPD
     TKYFVTRNYS TIIAFAVGAL YKPGNGFSII GAHTDSPCLR VKPRSKKTSQ GCLQVGVECY
     GGGIWSTWFD RDLTVAGRVM LKTGQLLSQK LVHIPRPVLR IPHLAIHLQR DVNDSFGPNK
     ESHLVPILAT AVQEELETGS ASTGDASSAT TTSEKHHLAL INLLCTELEV EKESLLDFEL
     CLVDTQPAVL GGVFEEFIFS PRLDNLHSCF CALKALIDSN SLAKDPNIRV VTLYDNEEVG
     SESAQGAMSS LTEIILRRLA SSKENLTAFE EAMPRSFVIS ADMAHAVHPN YQEKHEENHR
     PAFHKGPVIK FNSNQRYATT AVTASILREI ATKVDVPLQD VMVRNDSPCG TTIGPILSAK
     LGIPVLDLGS PQLAMHSIRE MCCTSSILQT TTLFQSTLAG TQAGASTGAA VPIL
//
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