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Database: UniProt
Entry: A0A436ZP67_9PEZI
LinkDB: A0A436ZP67_9PEZI
Original site: A0A436ZP67_9PEZI 
ID   A0A436ZP67_9PEZI        Unreviewed;       227 AA.
AC   A0A436ZP67;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Peptidase S26 domain-containing protein {ECO:0000259|Pfam:PF10502};
GN   ORFNames=DFL_008591 {ECO:0000313|EMBL:RVD80697.1};
OS   Arthrobotrys flagrans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Arthrobotrys.
OX   NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD80697.1, ECO:0000313|Proteomes:UP000283090};
RN   [1] {ECO:0000313|EMBL:RVD80697.1, ECO:0000313|Proteomes:UP000283090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD80697.1,
RC   ECO:0000313|Proteomes:UP000283090};
RA   Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT   "Intercellular communication is required for trap formation in the
RT   nematode-trapping fungus Duddingtonia flagrans.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:RVD80697.1}.
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DR   EMBL; SAEB01000012; RVD80697.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A436ZP67; -.
DR   STRING; 97331.A0A436ZP67; -.
DR   VEuPathDB; FungiDB:DFL_008591; -.
DR   Proteomes; UP000283090; Unassembled WGS sequence.
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   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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283090}.
FT   DOMAIN          80..155
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          167..207
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        144
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   227 AA;  24617 MW;  09E7C6A08D20F7CA CRC64;
     MYRLFSRRHG RLLPLPSRSH IPTTIPHYKP QLLIRRNGTA ATSPNGGTAG GGGATPEGDL
     PWYHPRWRRA LTSLVIGIKL LAFTHLVVSK VFIISQCEGP SMLPTLPTSG SVVVNNLYSR
     GRGIKVGDLI AAHRPDDMDV MLLKRVIGMP GDYVVTDPMA AGSGEETVMV RVPEGHCWIA
     GDNLSHSIDS RFYGPVPLAL IMGKVVAQVA GGRKWFSGPF TEVSKDE
//
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