ID A0A0U1LU50_TALIS Unreviewed; 292 AA.
AC A0A0U1LU50;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Mitochondrial inner membrane protease subunit {ECO:0000256|RuleBase:RU362041};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU362041};
GN ORFNames=PISL3812_03154 {ECO:0000313|EMBL:CRG86151.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG86151.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG86151.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG86151.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CVMT01000002; CRG86151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1LU50; -.
DR STRING; 28573.A0A0U1LU50; -.
DR OMA; VNMWPWG; -.
DR OrthoDB; 447775at2759; -.
DR Proteomes; UP000054383; 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 NCBIfam; TIGR02227; sigpep_I_bact; 1.
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|RuleBase:RU362041};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW ECO:0000256|RuleBase:RU362041};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|RuleBase:RU362041};
KW Protease {ECO:0000256|RuleBase:RU362041, ECO:0000313|EMBL:CRG86151.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054383}.
FT DOMAIN 92..190
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 177
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 292 AA; 32765 MW; C7B0AB8CCB7A90ED CRC64;
MANSKANSNP RPANAAQANN NRPRVISPRE LQRRLARGNP KSSGVSDPST YISESFATPH
VKRPSVLSSF ISRFRKRYAA LPAPIRGAAR AFRFLAPAIP IGMFFSEHVL QVMWVRGPSM
TPYLNENYAN TQTESDMVLV NMLPWGSGWP WSRTKTLERG MVVTFRSPSN PSHIAIKRVI
GLPGDRIMTR EPCPQPSQTV PFNHVWLEGD AEDPRKSLDS NTYGPVSISM ITGSVVAVLY
PRMRQLKWWD WDKPFDNQAG SDTQKDLGGG YRDSVRNRVI KEAVKVETPL FN
//
