ID A0A1F7ZKZ8_9EURO Unreviewed; 282 AA.
AC A0A1F7ZKZ8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Mitochondrial inner membrane protease subunit 2 {ECO:0000256|ARBA:ARBA00013650};
GN ORFNames=ABOM_011813 {ECO:0000313|EMBL:OGM40137.1};
OS Aspergillus bombycis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=109264 {ECO:0000313|EMBL:OGM40137.1, ECO:0000313|Proteomes:UP000179179};
RN [1] {ECO:0000313|EMBL:OGM40137.1, ECO:0000313|Proteomes:UP000179179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 26010 {ECO:0000313|Proteomes:UP000179179};
RX PubMed=27664179;
RA Moore G.G., Mack B.M., Beltz S.B., Gilbert M.K.;
RT "Draft genome sequence of an aflatoxigenic Aspergillus species, A.
RT bombycis.";
RL Genome Biol. Evol. 0:0-0(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGM40137.1}.
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DR EMBL; LYCR01000158; OGM40137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7ZKZ8; -.
DR STRING; 109264.A0A1F7ZKZ8; -.
DR OrthoDB; 447775at2759; -.
DR Proteomes; UP000179179; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OGM40137.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OGM40137.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000179179}.
FT DOMAIN 83..184
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 24..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 170
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 282 AA; 31888 MW; 5DBE73EA956257ED CRC64;
MPNSSQKPPG SRFQVLTLEA AKLRSQHRLS PSPTPSLSST APSTAPRAAQ PAPEPPRKPS
SLFSHFRSRY AAQPVSVRTG FRVLRILAPI VPIGLFFSEH VLGVMWVSGP SMTPYLNEDY
EQMHTKRDMV LVNMWPWGGA GWPWERTRRL ERGMVVTFRS PANQGHIAIK RVVGLPGDRI
TTRDPCMKPS QIVPFNHVWL EGDAADPKRS LDSNTYGPVS ISLITGRVMA VMYPRFRMLK
WTDWEQGLVE GDDERRLGDN YRHEVRDRVS KEAVKLERPV LS
//