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Database: UniProt
Entry: A0A090CD18_PODAN
LinkDB: A0A090CD18_PODAN
Original site: A0A090CD18_PODAN 
ID   A0A090CD18_PODAN        Unreviewed;       280 AA.
AC   A0A090CD18;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Mitochondrial inner membrane protease subunit {ECO:0000256|RuleBase:RU362041};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU362041};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP25500.1, ECO:0000313|Proteomes:UP000001197};
RN   [1] {ECO:0000313|EMBL:CDP25500.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
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; FO904937; CDP25500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090CD18; -.
DR   STRING; 515849.A0A090CD18; -.
DR   InParanoid; A0A090CD18; -.
DR   Proteomes; UP000001197; Chromosome 2.
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; 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; 2.
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|RuleBase:RU362041};
KW   Mitochondrion inner membrane {ECO:0000256|RuleBase:RU362041};
KW   Protease {ECO:0000256|RuleBase:RU362041, ECO:0000313|EMBL:CDP25500.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197}.
FT   DOMAIN          97..180
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          198..241
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   REGION          27..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        169
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   280 AA;  31119 MW;  DA05535FF02F2C08 CRC64;
     MSSLYRLRAI TRPHNLSPHR SLTRLSLTQP HPFRPSPISP AQTNLSPPQQ SYSTTTTSPE
     NTQPQHQHRQ QNNHHDQNQQ SQNEPTPPFP PLHPLRLLLS YLKLLALAHL IWNNLLSLAP
     AQGPSMLATY PITGTWHLTS RLSRLGRNLS IGDIVTFTLP DRPSAIGVKR VIGLPGDYVL
     IGTPGPAADD ALMLQSSITY QHKQQVPEGH VYLVGDNLPA SNDSRIFGPV PLGLIRGKVI
     ASMEPSFTRG PFANFEWVRN PMKKTEPPTR EEVLAARDLE
//
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