ID A0A0L1J991_ASPNO Unreviewed; 460 AA.
AC A0A0L1J991;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=mitochondrial processing peptidase {ECO:0000256|ARBA:ARBA00012299};
DE EC=3.4.24.64 {ECO:0000256|ARBA:ARBA00012299};
DE AltName: Full=Beta-MPP {ECO:0000256|ARBA:ARBA00031018};
GN ORFNames=ANOM_002516 {ECO:0000313|EMBL:KNG88314.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG88314.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG88314.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG88314.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal transit peptides from precursor proteins
CC imported into the mitochondrion, typically with Arg in position P2.;
CC EC=3.4.24.64; Evidence={ECO:0000256|ARBA:ARBA00001098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {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:KNG88314.1}.
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DR EMBL; JNOM01000056; KNG88314.1; -; Genomic_DNA.
DR RefSeq; XP_015409237.1; XM_015547773.1.
DR AlphaFoldDB; A0A0L1J991; -.
DR STRING; 1509407.A0A0L1J991; -.
DR GeneID; 26804320; -.
DR OrthoDB; 167798at2759; -.
DR Proteomes; UP000037505; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
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; 3.
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:SF149; GH01077P; 1.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
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 51..198
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 204..375
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 460 AA; 50945 MW; EFFB3140D614DABF CRC64;
MASRRLAFNF NQALRSRAAL KSIQPVKRGF SSPVTLPSTT QSTTLSNGFT IATEYSPWAQ
TSTVGVWIDA GSRAETDKTN GTAHFLEHLA FKGTNKRSQH QLELEIENMG AHLNAYTSRE
NTVYYAKAFN NDVPKAVDIL ADILQNSKLE PGAIERERDV ILREQEEVDK QFEEVVFDHL
HATAYQNQPL GRTILGPKEN IQTISRDNLV DYIKTNYTAD RMVLVGAGGI PHEQLVRLAE
EHFGTLPSKP PTSAALALTA EQKRTPEFIG SEVRLRDDTI PTAHIALAVE GVSWKDDDYF
TALVAQAIVG NWDRAMGNSP YLGSKLSSLV EHHGLANSFM SFSTSYSDTG LWGIYLVSEN
LTALDDLTHF AMPQLKASIL LSLDGTTAVA EDIGRQIITT GRRLSPEDIE RTIGQISEKD
VMDFANRRIW DQDVAVSAFG SVEGLLDYNR IRADTTRNTL
//
