ID   MPPA_BLAEM              Reviewed;         474 AA.
AC   P97997;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Mitochondrial-processing peptidase subunit alpha;
DE   AltName: Full=Alpha-MPP;
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000305};
DE   Flags: Precursor;
OS   Blastocladiella emersonii (Aquatic fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycota incertae sedis; Blastocladiomycetes; Blastocladiales;
OC   Blastocladiaceae; Blastocladiella.
OX   NCBI_TaxID=4808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX   PubMed=10400583; DOI=10.1128/jb.181.14.4257-4265.1999;
RA   Rocha C.R., Gomes S.L.;
RT   "Characterization and submitochondrial localization of the alpha subunit of
RT   the mitochondrial processing peptidase from the aquatic fungus
RT   Blastocladiella emersonii.";
RL   J. Bacteriol. 181:4257-4265(1999).
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:0000250|UniProtKB:P11914}.
CC   -!- SUBUNIT: Heterodimer of mas2 (alpha) and mas1 (beta) subunits, forming
CC       the mitochondrial processing protease (MPP) in which mas2 is involved
CC       in substrate recognition and binding and mas1 is the catalytic subunit.
CC       {ECO:0000250|UniProtKB:P11914}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:10400583}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
CC   -!- CAUTION: Does not seem to have a protease activity as it lack the zinc-
CC       binding site. {ECO:0000305}.
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DR   EMBL; U90568; AAB50243.1; -; Genomic_DNA.
DR   AlphaFoldDB; P97997; -.
DR   SMR; P97997; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; SSF63411; 2.
PE   3: Inferred from homology;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..474
FT                   /note="Mitochondrial-processing peptidase subunit alpha"
FT                   /id="PRO_0000026770"
SQ   SEQUENCE   474 AA;  50856 MW;  215D2252CC95D50E CRC64;
     MSPAAQLAKA AARSTCMTRL PSGIRVATAP SNSHFAAVGV YVDAGPIYET SIDRGVSHFV
     SSLAFKSTHG ATESQVLKTM AGLGGNLFCT ATRESILYQG SVLHHDLPRT VQLLADTTLR
     PALTEEEIAE RRATIAFEAE DLHSRPDAFI GEMMHAVAFG GRGLGNSIFC EPQRARNMTS
     DTIREYFATY LHPSRMVVAG TGVAHAELVD LVSKAFVPSS TRAPSSVTHS DIETAYVGGS
     HQLVIPKPPP THPNYEQTLT HVQVAFPVPP FTHPDMFPVS TLQVLMGGGG AFSAGGPGKG
     MYSRLYTNVL NRYRWMESCA AFQHAYSSTS LFGISASCVP SFNPHLCNVL AGEFVHMARN
     LSDEEVARAK NQLKSSLLMN LESQVITVED IGRQVLAQNQ RLEPLELVNN ISAVTRDDLV
     RVAEALVAKP PTMVAVGEDL TKLTDIKETL AAFNASGEAL QPVGSAGSFG RVTM