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Database: UniProt
Entry: A0A0D9MX05_ASPFA
LinkDB: A0A0D9MX05_ASPFA
Original site: A0A0D9MX05_ASPFA 
ID   A0A0D9MX05_ASPFA        Unreviewed;       510 AA.
AC   A0A0D9MX05;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   22-NOV-2017, entry version 11.
DE   SubName: Full=Aminopeptidase I zinc metalloprotease M18 {ECO:0000313|EMBL:KJJ32344.1};
GN   ORFNames=P034_07948219 {ECO:0000313|EMBL:KJJ32344.1};
OS   Aspergillus flavus (strain ATCC MYA-384 / AF70).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1392242 {ECO:0000313|EMBL:KJJ32344.1, ECO:0000313|Proteomes:UP000032444};
RN   [1] {ECO:0000313|EMBL:KJJ32344.1, ECO:0000313|Proteomes:UP000032444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-384 / AF70 {ECO:0000313|Proteomes:UP000032444};
RA   Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R.,
RA   Ehrlich K.C., Bhatnagar D., Cleveland T.E., Bennett J.W.,
RA   Nierman W.C.;
RT   "Draft genome sequence of Aspergillus flavus AF70.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KJJ32344.1}.
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DR   EMBL; JZDT01000524; KJJ32344.1; -; Genomic_DNA.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; KJJ32344; KJJ32344; P034_07948219.
DR   Proteomes; UP000032444; 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:KJJ32344.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032444};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KJJ32344.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KJJ32344.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032444};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   510 AA;  55456 MW;  8AB2D0402A626573 CRC64;
     MTKRSVLDLR DSAMAYRLSA QLPEPSPATI ATPVARSGPF APEDYTKPYC EFMTANPTIF
     HAVDGFTRQL ESQGYKRLPE RETWNSKLEK GGKYYVTRNG SAFISFSIGR DYKGGNGMAI
     VAGHIDALTA KLKPVSKLPN KAGFSQLGVA PYAGALSDTW WDRDLSIGGR VLVQDSNTGK
     VESKLVKLDW PIARIPTLAP HFGAPSQGPF NKETQMVPII GVDNSDLFQQ QAPSKIDQDN
     GIKPGTFAAT QPEKLVKVIS KELGITDYSS IISWELELYD SQPAQVGGLD KDLIFAGRID
     DKLCCYAAQE ALLASSDSTS TSSIKMVGMF DDEEIGSLLR QGARSNFMSS VIERITEAFS
     PNYGPNVLSQ TVANSFFVSS DVIHAVNPNF LGVYLENHAP RLNVGVAVSA DSNGHMTTDS
     VSYGFIKRVA DRCGSTLQVF QIRNDSRSGG TIGPMTSSRI GMRAIDVGIP QLSMHSIRAT
     TGSLDPGLGV KLFKGFFDYF EEVDKEFADF
//
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