ID A0A0N4WIL5_HAEPC Unreviewed; 128 AA.
AC A0A0N4WIL5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Mitochondrial inner membrane protease subunit 2 {ECO:0000256|ARBA:ARBA00013650};
GN ORFNames=HPLM_LOCUS10798 {ECO:0000313|EMBL:VDO41153.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0001080601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0001080601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO41153.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO41153.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. IMP2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007066}.
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DR EMBL; UZAF01017392; VDO41153.1; -; Genomic_DNA.
DR STRING; 6290.A0A0N4WIL5; -.
DR WBParaSite; HPLM_0001080601-mRNA-1; HPLM_0001080601-mRNA-1; HPLM_0001080601.
DR OMA; HTGHTLD; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; Unassembled WGS sequence.
DR GO; GO:0042720; C:mitochondrial inner membrane peptidase complex; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006627; P:protein processing involved in protein targeting to mitochondrion; 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; IPR037730; IMP2.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019533; Peptidase_S26.
DR PANTHER; PTHR46041; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 2; 1.
DR PANTHER; PTHR46041:SF2; MITOCHONDRIAL INNER MEMBRANE PROTEASE SUBUNIT 2; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000268014}.
FT DOMAIN 2..90
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 32
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 80
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 128 AA; 14361 MW; F9CE6FCF847DCB17 CRC64;
MLRFTVRVTS SVCVAMTAFD IVGHPAVVTG ASMSPTLEGS DSRWWHRDLV WLSPWGIRSP
NIGDVLTFIS PREPDMMHIK RVTGLEGDLV IDNPVNANDS NIYGPVSRGL VKNRATHIIW
PPSRWRRL
//