ID   T2MDW9_HYDVU            Unreviewed;       512 AA.
AC   T2MDW9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Mitochondrial-processing peptidase subunit alpha {ECO:0000256|ARBA:ARBA00016741};
DE   AltName: Full=Alpha-MPP {ECO:0000256|ARBA:ARBA00030006};
DE   AltName: Full=Inactive zinc metalloprotease alpha {ECO:0000256|ARBA:ARBA00032315};
GN   Name=PMPCA {ECO:0000313|EMBL:CDG70286.1};
OS   Hydra vulgaris (Hydra) (Hydra attenuata).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Aplanulata; Hydridae; Hydra.
OX   NCBI_TaxID=6087 {ECO:0000313|EMBL:CDG70286.1};
RN   [1] {ECO:0000313|EMBL:CDG70286.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole animals {ECO:0000313|EMBL:CDG70286.1};
RX   PubMed=24065732; DOI=10.1093/gbe/evt142;
RA   Wenger Y., Galliot B.;
RT   "Punctuated emergences of genetic and phenotypic innovations in eumetazoan,
RT   bilaterian, euteleostome, and hominidae ancestors.";
RL   Genome Biol. Evol. 5:1949-1968(2013).
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|RuleBase:RU004447}.
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DR   EMBL; HAAD01004054; CDG70286.1; -; mRNA.
DR   AlphaFoldDB; T2MDW9; -.
DR   MEROPS; M16.971; -.
DR   EnsemblMetazoa; XM_012705269.1; XP_012560723.1; LOC101240630.
DR   EnsemblMetazoa; XM_047278729.1; XP_047134685.1; LOC101240630.
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; 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; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   2: Evidence at transcript level;
FT   DOMAIN          67..216
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          228..419
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   512 AA;  57319 MW;  B065B7C09874B932 CRC64;
     MAAKVLKSKS NPLQFISLIF SCKRSVSFDK IPPLTVPFFN ENVFSKNVLS AQKIKNVKFT
     TLQNGLKVAS EDSFGQFCTI GALIDAGSRY EIDYEGGVSH ILEKLAFHST ANYESNEVIV
     KELEKLGGHA DCQIFRDCSI YAASAFKYNV EGVVNILSET VLRPTLKDSE VEEQKQSILF
     ELDSLNYRPD LEPQLTDLIH AAAFNGNTLG LPKLCPQNSI SKLSSCILKD YMNRYYRPER
     ITISGVNVNH EELVKYCKKF FVDNAPIIKH RIDPDRSIAQ YTGGILKDHR PEPRLQPGIT
     QLPELVHVAI AFEGANYADK DMFSFAVLNT LLGGGGSFSA GGPGKGMYSR LYTNVLNRKH
     WMFSSAAFNH SYADAGLFAI HSSAHPSEAK DLVKVITNEY TRLISEPFHE VEVARAKKQT
     QSMLMMNLES RVVRFEDIGR QILGLGFHKS AQELYESIEA VTSDDLRRIS EKMLSSKLSV
     AAIGNLENFP SYEEIQKLLI KKSFTSKFFA RS
//