ID   HETQ2_PODAS             Reviewed;         366 AA.
AC   P0DW09;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 1.
DT   03-AUG-2022, entry version 1.
DE   RecName: Full=Subtilisin-like protease het-Q2 {ECO:0000305};
DE            EC=3.4.21.- {ECO:0000269|PubMed:35135876};
DE   AltName: Full=Heterokaryon incompatibility protein Q2 {ECO:0000303|PubMed:35135876};
GN   Name=het-Q2 {ECO:0000303|PubMed:35135876};
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF HIS-105 AND SER-266.
RX   PubMed=35135876; DOI=10.1073/pnas.2109418119;
RA   Clave C., Dyrka W., Turcotte E.A., Granger-Farbos A., Ibarlosa L.,
RA   Pinson B., Vance R.E., Saupe S.J., Daskalov A.;
RT   "Fungal gasdermin-like proteins are controlled by proteolytic cleavage.";
RL   Proc. Natl. Acad. Sci. U.S.A. 119:0-0(2022).
CC   -!- FUNCTION: Serine protease involved in heterokaryon incompatibility, a
CC       process that ensures that during spontaneous vegetative cell fusion,
CC       only compatible cells from the same colony survive (non-self-
CC       recognition) (PubMed:35135876). In P.anserina, the het-q locus exists
CC       as 2 incompatible alleles, het-Q1 (AC B2AXJ5) and het-Q2 (this entry)
CC       (PubMed:35135876). Prevents cell fusion with strains containing the
CC       gasdermin-like protein het-Q1 by mediating proteolytic cleavage and
CC       maturation of het-Q1 during the allorecognition process, thereby
CC       triggering cell death (PubMed:35135876). {ECO:0000269|PubMed:35135876}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; MZ576188; UJY53792.1; -; Genomic_DNA.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Membrane; Protease; Serine protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..366
FT                   /note="Subtilisin-like protease het-Q2"
FT                   /id="PRO_0000455985"
FT   TRANSMEM        261..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1..321
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        35
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        105
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT                   ECO:0000305|PubMed:35135876"
FT   ACT_SITE        266
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT                   ECO:0000305|PubMed:35135876"
FT   MUTAGEN         105
FT                   /note="H->A: Abolished ability to trigger cell death during
FT                   the allorecognition process."
FT                   /evidence="ECO:0000269|PubMed:35135876"
FT   MUTAGEN         266
FT                   /note="S->A: Abolished ability to trigger cell death during
FT                   the allorecognition process."
FT                   /evidence="ECO:0000269|PubMed:35135876"
SQ   SEQUENCE   366 AA;  39643 MW;  62FBF96D720A087D CRC64;
     MSAISHHSLS HLNSTVSKRL MPTYSDPVVR IAVLDTGFDG SHPDFSHPRT AYFTGPFSDL
     PQPEKDEEPQ LTRIKAYHDF CQPSPPGDRQ GPPPQPHSMV DLAGHGTAIA GLILRLAPRA
     ELVIGRVCHG VDSNELSAPD PSRVAAAIRW AITQKVHIIN LSLGYRNQPL KELLPLRAAL
     LEAQRSNILV FASTSNQGSH EPAAWPASDA RFAIGVHSCN DMGSAPSGSS CKASENGYNF
     MAVGENLLVH RLAQKGGGFE LVSGSSFATP VVVSVAALVL AFVWQEECKR ERDEVGREVM
     LEDLGSLGGM GRVLMALGEK TAGSYWAVGM KLFWAGYREG DGRDPEKEEK EARRWAWGVL
     RGAVAY