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Database: UniProt
Entry: U4L6F2_PYROM
LinkDB: U4L6F2_PYROM
Original site: U4L6F2_PYROM 
ID   U4L6F2_PYROM            Unreviewed;       158 AA.
AC   U4L6F2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Similar to Mitochondrial inner membrane protease subunit 1 acc. no. O74800 {ECO:0000313|EMBL:CCX12055.1};
GN   ORFNames=PCON_11649 {ECO:0000313|EMBL:CCX12055.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX12055.1};
RN   [1] {ECO:0000313|EMBL:CCX12055.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX12055.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX12055.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(2013).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family. IMP1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00038445}.
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DR   EMBL; HF935675; CCX12055.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4L6F2; -.
DR   STRING; 1076935.U4L6F2; -.
DR   eggNOG; KOG0171; Eukaryota.
DR   OMA; CKGPSME; -.
DR   OrthoDB; 447775at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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   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|ARBA:ARBA00022670, ECO:0000313|EMBL:CCX12055.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CCX12055.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..158
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004651956"
FT   DOMAIN          20..91
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          104..139
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        36
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        81
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   158 AA;  17453 MW;  D60C69DB398CC93F CRC64;
     MASLLHRQLR ILPLTFLWTH LFWTKCYSVG DTLGASMLPT INVSGDWIVI SKFHSRGRGI
     IVGDLVSYAH PIDGPDVNVV KRVIGLEGDF VVKDPSDGSG DMLQVPKGHI WTTGDNLPHS
     LDSRIYGPVP MALVRGKVIA KGLPWGWIKN PFTEEVNQ
//
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