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Database: UniProt
Entry: S7NLZ7_MYOBR
LinkDB: S7NLZ7_MYOBR
Original site: S7NLZ7_MYOBR 
ID   S7NLZ7_MYOBR            Unreviewed;       471 AA.
AC   S7NLZ7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-NOV-2017, entry version 19.
DE   SubName: Full=Aspartyl aminopeptidase {ECO:0000313|EMBL:EPQ18461.1};
GN   ORFNames=D623_10032940 {ECO:0000313|EMBL:EPQ18461.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
OC   Vespertilionidae; Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ18461.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D.,
RA   Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N.,
RA   Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A.,
RA   Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; KE164532; EPQ18461.1; -; Genomic_DNA.
DR   RefSeq; XP_005883532.1; XM_005883470.2.
DR   RefSeq; XP_014386630.1; XM_014531144.1.
DR   MEROPS; M18.002; -.
DR   GeneID; 102263892; -.
DR   CTD; 23549; -.
DR   Proteomes; UP000052978; 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:EPQ18461.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000052978};
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:UP000052978};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   471 AA;  51993 MW;  2F72592425C82683 CRC64;
     MNGWASKEAV QAAARELLKF VNRSPSPFHV VAECRSRLLQ AGFHELKETE SWDLKPESKY
     FLTRNSSTII AFAVGGQYVP GNGFSLIGAH TDSPCLRVKR RSRRSQVGFH QVGVETYGGG
     IWSTWFDRDL TLAGRVIVKC PTSDRLEQRL VHVDRPILRI PHLAIHLQRN VNENFGPNTE
     THLVPILATA VQEELEKENA EPGPFNAADD RHHSVLVSLL CGHLGLSPED ILEMELCLAD
     TQPAVLGGAY EEFIFAPRLD NLHSCFCALQ ALIESCAAPA SLAADPHVRM IALYDNEEVG
     SESAQGAQSL LTELVLRRIS ASSQHLTAFE EAIPKSYMIS ADMAHAVHPN YLDKHEENHR
     PLFHKGPVIK VNNKQRYASN AVSEALIRRV ANNVGVPLQD LMVRNDSPCG TTIGPILASR
     LGLRVLDLGS PQLAMHSIRE TACTTGVLQT ITLFKGFFEL YPSLSRNLLV D
//
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