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Database: UniProt
Entry: A1CP42_ASPCL
LinkDB: A1CP42_ASPCL
Original site: A1CP42_ASPCL 
ID   A1CP42_ASPCL            Unreviewed;       479 AA.
AC   A1CP42;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
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=ACLA_021220 {ECO:0000313|EMBL:EAW07413.1};
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW07413.1, ECO:0000313|Proteomes:UP000006701};
RN   [1] {ECO:0000313|EMBL:EAW07413.1, ECO:0000313|Proteomes:UP000006701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC   {ECO:0000313|Proteomes:UP000006701};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR   EMBL; DS027059; EAW07413.1; -; Genomic_DNA.
DR   RefSeq; XP_001268839.1; XM_001268838.1.
DR   AlphaFoldDB; A1CP42; -.
DR   STRING; 344612.A1CP42; -.
DR   MEROPS; M16.980; -.
DR   EnsemblFungi; EAW07413; EAW07413; ACLA_021220.
DR   GeneID; 4700589; -.
DR   KEGG; act:ACLA_021220; -.
DR   VEuPathDB; FungiDB:ACLA_021220; -.
DR   eggNOG; KOG0960; Eukaryota.
DR   HOGENOM; CLU_009902_4_2_1; -.
DR   OMA; IDVVCDM; -.
DR   OrthoDB; 167798at2759; -.
DR   Proteomes; UP000006701; Unassembled WGS sequence.
DR   GO; GO:0017087; C:mitochondrial processing peptidase complex; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IEA:EnsemblFungi.
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: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:UP000006701}.
FT   DOMAIN          51..198
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          204..394
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   479 AA;  53353 MW;  96AB1B611AF98B11 CRC64;
     MASRRLAFNF NQALRSRAAL KAVQPVKRGF ASPVTLPTTT QSTTLSNGFT IATEYSPWAQ
     TSTVGVWIDA GSRAETDKTN GTAHFLEHLA FKGTNKRTQH QLELEIENMG AHLNAYTSRE
     NTVYYAKSFN NDVPKAVDIL ADILQNSKLE PAAIERERDV ILREQEEVDK QLEEVVFDHL
     HATAFQHQPL GRTILGPKEN IQTISRDNLT DYIKTNYTAD RMVLVGAGGI PHEQLVKLAE
     QHFGSLPSKP PTSAALALTA EQKRTPEFIG SEVRIRDDTL PTAHIAVAVE GVSWKDDDYF
     TALVAQAIVG NWDRAMGNSP YLGSRLSSFI NHHNLANSFM SFSTSYSDTG LWGIYMVSEN
     LTNLNDLVHF ALREWSRMCY NVTPAEVERA KAQLKASILL SLDGTTAVAE DIGRQIITTG
     RRLSPEDVER IIGRITEKDV MDFANRKLWD QDIALSAVGS IEGILDYQRI RSDMSRNSL
//
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