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
//