GenomeNet

Database: UniProt
Entry: L5LWS6_MYODS
LinkDB: L5LWS6_MYODS
Original site: L5LWS6_MYODS 
ID   L5LWS6_MYODS            Unreviewed;       472 AA.
AC   L5LWS6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   22-NOV-2017, entry version 12.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:ELK30546.1};
GN   ORFNames=MDA_GLEAN10022959 {ECO:0000313|EMBL:ELK30546.1};
OS   Myotis davidii (David's myotis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK30546.1, ECO:0000313|Proteomes:UP000010556};
RN   [1] {ECO:0000313|Proteomes:UP000010556}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y.,
RA   Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y.,
RA   Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G.,
RA   Wang L.F., Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the
RT   evolution of flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; KB106857; ELK30546.1; -; Genomic_DNA.
DR   MEROPS; M18.002; -.
DR   Proteomes; UP000010556; 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:ELK30546.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010556};
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:UP000010556};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   472 AA;  51757 MW;  F4E1D28E8E2627B5 CRC64;
     MNGWASKEAV QAAARELLKF VNRSPSPFHV VAECRSRLLQ AGFHELKETE SWDLKPESKY
     FLTRNSSTII AFAVGGQYVP GNGFSLIGAH TDSPCLRVKR RSRRSQVGFH QVGVETYGGG
     IWSTWFDRDL TLAGRVIVKC PTSDRLEQRL VHVDRPILRI PHLAIHLQRN VNESFGPNTE
     THLVPILATA VQEELEKENA EPGAFSAADD RHHSVLMSLL CGHLGLSPED ILEMELCLAD
     TQPAVLGGAY EEFIFAPRLD NLHSCFCALQ ALIESCAAPA SLAADPHVRM IALYDNEEVG
     SESAQGAQSL LTELVLRRIS ASPQHLTAFE EAIPKSYMIS ADMAHAVHPN YLGNFLLTAP
     RLSLAKGPVI KVNNKQRYAS NAVSEALIRR VANNVGVPLQ DIMVRNDSTC GTTIGPILAA
     RLGLRVLDLG SPQLAMHSIR ETACTTGVLQ TITLFKGFFE LYPSLSRNLL VD
//
DBGET integrated database retrieval system