ID   MPPA1_DICDI             Reviewed;         654 AA.
AC   Q86A84; Q1ZXL4; Q3LG19;
DT   19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Mitochondrial-processing peptidase subunit alpha-1;
DE   AltName: Full=Alpha-MPP;
DE            Short=Ddalpha-MPP;
DE   AltName: Full=Inactive zinc metalloprotease alpha-1 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=mppA1; Synonyms=mppA; ORFNames=DDB_G0274809;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18603769; DOI=10.1271/bbb.80106;
RA   Nagayama K., Itono S., Yoshida T., Ishiguro S., Ochiai H., Ohmachi T.;
RT   "Antisense RNA inhibition of the beta subunit of the Dictyostelium
RT   discoideum mitochondrial processing peptidase induces the expression of
RT   mitochondrial proteins.";
RL   Biosci. Biotechnol. Biochem. 72:1836-1846(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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:0000269|PubMed:18603769}.
CC   -!- SUBUNIT: Heterodimer of alpha and beta subunits, forming the
CC       mitochondrial processing protease (MPP) in which subunit alpha is
CC       involved in substrate recognition and binding and subunit beta is the
CC       catalytic subunit. {ECO:0000250|UniProtKB:P10507}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:18603769}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; AB213513; BAE45920.1; -; mRNA.
DR   EMBL; AAFI02000012; EAS66919.1; -; Genomic_DNA.
DR   RefSeq; XP_001134603.1; XM_001134603.1.
DR   AlphaFoldDB; Q86A84; -.
DR   SMR; Q86A84; -.
DR   STRING; 44689.DDB0232199; -.
DR   PaxDb; Q86A84; -.
DR   EnsemblProtists; EAS66919; EAS66919; DDB_G0274809.
DR   GeneID; 8619373; -.
DR   KEGG; ddi:DDB_G0274809; -.
DR   dictyBase; DDB_G0274809; mppA1.
DR   eggNOG; KOG2067; Eukaryota.
DR   HOGENOM; CLU_419463_0_0_1; -.
DR   InParanoid; Q86A84; -.
DR   OMA; LKYHHSP; -.
DR   PhylomeDB; Q86A84; -.
DR   BRENDA; 3.4.24.64; 1939.
DR   Reactome; R-DDI-611105; Respiratory electron transport.
DR   PRO; PR:Q86A84; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:dictyBase.
DR   GO; GO:0017087; C:mitochondrial processing peptidase complex; ISS:dictyBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:dictyBase.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:dictyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; ISS:dictyBase.
DR   GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; IDA:dictyBase.
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   2: Evidence at transcript level;
KW   Coiled coil; Mitochondrion; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           ?..654
FT                   /note="Mitochondrial-processing peptidase subunit alpha-1"
FT                   /id="PRO_0000390659"
FT   REGION          73..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          381..446
FT                   /evidence="ECO:0000255"
FT   CONFLICT        3..5
FT                   /note="IIF -> NNI (in Ref. 1; BAE45920)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        9
FT                   /note="P -> H (in Ref. 1; BAE45920)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   654 AA;  73262 MW;  9BAE7EB8E355236B CRC64;
     MNIIFLKVPS IFKKLNVGNI KILNVNQNSP SIIVNSNNTK SIKNHNYSSF TNNNNNNNKN
     QVNLVQNKSI LSSSSSYKGN NNNNNKLSYT TSSNNNNNNK IEEIVKSTTV SPFTPLNILH
     PKLVGEKLYS NDNEANNNQK EFKAEISTLP NGIRVVSKQT HEGVCAIGLY INAGTKYESP
     QDRGVFNLLE KMTFKETKNN STSEIIKELE EISMNAMASS SREMINVSLE VLRKDLEFVL
     SILSDQIKSP TYSEEELREQ IEVCIRNYEM ITNSSSDQLM TEILMGVAFG DAGLGNLVIA
     TPEQYQNITR EKLFDALRKY YVGKNIVISV TGAEHSQVIE LVDKYFGDIP FTQKDTPSED
     SIDSTITYKG GTDACVAGLI HKNHLKSQLQ FLIEKQQKLK QQQQQQQPQP QNSNIDDNDN
     EEELLNLEIE QTKISIEQLE LQQVKESSWI IAFPHSGLST VAENKDIING LVLQSLLGGG
     SSYSTGGPGK GMQSRLNLNV VYSSHRVKNC HAFLFVFNKV SLFGISLTTQ SGFLQDGIEL
     VLQELLMLRS SMTQQELERA KRSQKSQILQ NLEMRSVQCD DMARHILSFG SYKSPEQICK
     LIDSVTLDDI KKLISKLAQS NPSVVSIVAN ENEPILTAEQ YNQIVKQNSS TLFK