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Database: UniProt
Entry: A0A0L1IW10_ASPNO
LinkDB: A0A0L1IW10_ASPNO
Original site: A0A0L1IW10_ASPNO 
ID   A0A0L1IW10_ASPNO        Unreviewed;       624 AA.
AC   A0A0L1IW10;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN   ORFNames=ANOM_008208 {ECO:0000313|EMBL:KNG83677.1};
OS   Aspergillus nomiae NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG83677.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG83677.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG83677.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Substrate recognition and binding subunit of the essential
CC       mitochondrial processing protease (MPP), which cleaves the
CC       mitochondrial sequence off newly imported precursors proteins.
CC       {ECO:0000256|ARBA:ARBA00002123}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNG83677.1}.
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DR   EMBL; JNOM01000253; KNG83677.1; -; Genomic_DNA.
DR   RefSeq; XP_015404600.1; XM_015553464.1.
DR   AlphaFoldDB; A0A0L1IW10; -.
DR   STRING; 1509407.A0A0L1IW10; -.
DR   GeneID; 26810012; -.
DR   OrthoDB; 7099at2759; -.
DR   Proteomes; UP000037505; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000037505}.
FT   DOMAIN          91..238
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          244..294
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          401..521
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          602..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        287..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..624
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   624 AA;  67702 MW;  F93067939ECEA92C CRC64;
     MGSRLSSKSL RWSPENSSLR QHKEHLNSIA SEPIEFKIDN MRRSVLRAVE SAKPLSRASR
     SVSRSFATVN EAGSKDPAEL DQITTLPNGI RVATESLPGP FSGVGVYVDA GSRYEDESLR
     GVSHIMDRLA FKSTNKRSGD EMLEVLEGLG GNIQCASSRE SLMYQSASFN SAVPTTLGLL
     AETIRDPLIT EEEVLQQLGT AEYEIGEIWA KPELILPELV HMAAYKDNTL GNPLLCPEER
     LGEINKAVVD KYREVFFNPD RMVVAFAGVP HDVAVKLTEQ YFGDMQGQKS NKGPVLSGTG
     IETTLSNSSS AVEEGQVPTI PQFTPSSTTS TTPASPKSGS GLLSKLPFLK NLSGSQNGSV
     SPLDPSLVEP STFNLTRPSH YTGGFLSLPP IPPPANPMLP RLSHIHLAFE ALPISNPDIY
     ALATLQTLLG GGGSFSAGGP GKGMYSRLYT NVLNQHGWVE SCIAFNHSYT DSGIFGISAS
     CSPTRTPEML EVMCRELQAL TLDNGYSALQ AQEVNRAKNQ LRSSLLMNLE SRMVELEDLG
     RQVQVHGRKV GVKEMCDHID ALTVEDLRRV ARQVFGGNVQ NKGQGTGRPT VVLQEGELEG
     YNFVPSHGRR SKKGSPDGSW EEDE
//
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