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Database: UniProt
Entry: A0A0M4ET38_DROBS
LinkDB: A0A0M4ET38_DROBS
Original site: A0A0M4ET38_DROBS 
ID   A0A0M4ET38_DROBS        Unreviewed;       167 AA.
AC   A0A0M4ET38;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Mitochondrial inner membrane protease subunit {ECO:0000256|RuleBase:RU362041};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU362041};
DE   Flags: Fragment;
GN   ORFNames=Dbus_chrXg1446 {ECO:0000313|EMBL:ALC49590.1};
OS   Drosophila busckii (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC49590.1, ECO:0000313|Proteomes:UP000494163};
RN   [1] {ECO:0000313|EMBL:ALC49590.1, ECO:0000313|Proteomes:UP000494163}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole larvae {ECO:0000313|EMBL:ALC49590.1};
RA   Zhou Q., Bachtrog D.;
RT   "Ancestral chromatin configuration constrains chromatin evolution on
RT   differentiating sex chromosomes in Drosophila.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Heterodimer of 2 subunits, IMMPL1 and IMMPL2.
CC       {ECO:0000256|ARBA:ARBA00011805}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273,
CC       ECO:0000256|RuleBase:RU362041}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038445}.
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DR   EMBL; CP012528; ALC49590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M4ET38; -.
DR   STRING; 30019.A0A0M4ET38; -.
DR   OMA; CKGPSME; -.
DR   Proteomes; UP000494163; Chromosome x sequence.
DR   GO; GO:0098796; C:membrane protein complex; IEA:UniProt.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   CDD; cd06530; S26_SPase_I; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR   InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR   InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR   InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR   InterPro; IPR019533; Peptidase_S26.
DR   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR12383:SF16; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 1; 1.
DR   PANTHER; PTHR12383; PROTEASE FAMILY S26 MITOCHONDRIAL INNER MEMBRANE PROTEASE-RELATED; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU362041};
KW   Membrane {ECO:0000256|RuleBase:RU362041};
KW   Mitochondrion {ECO:0000256|RuleBase:RU362041};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU362041};
KW   Protease {ECO:0000256|RuleBase:RU362041};
KW   Reference proteome {ECO:0000313|Proteomes:UP000494163}.
FT   DOMAIN          22..159
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ALC49590.1"
SQ   SEQUENCE   167 AA;  18625 MW;  6644F738994E11FB CRC64;
     YTVLSRLGTL ARYTIAYASI THCTFEYVGD FVLCKGPSME PTLFSDNVLL TERLSKHWRS
     YQSGDIIIAV SPVNANQFIC KRIVAVSGEK INTLKPHPLE AESTSTSTKQ PMEMSMVTDY
     VPRGCVWIEG DNKGNSSDSR YYGPIPLGLI RSRVVCRIWP LSELTGL
//
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