ID   NM111_PHANO             Reviewed;        1017 AA.
AC   Q0UY70;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Pro-apoptotic serine protease NMA111;
DE            EC=3.4.21.-;
GN   Name=NMA111; ORFNames=SNOG_03294;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
CC   -!- FUNCTION: Nuclear serine protease which mediates apoptosis.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
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DR   EMBL; CH445328; EAT90025.2; -; Genomic_DNA.
DR   RefSeq; XP_001793864.1; XM_001793812.1.
DR   AlphaFoldDB; Q0UY70; -.
DR   SMR; Q0UY70; -.
DR   STRING; 13684.SNOT_03294; -.
DR   MEROPS; S01.434; -.
DR   EnsemblFungi; SNOT_03294; SNOT_03294; SNOG_03294.
DR   GeneID; 5970721; -.
DR   KEGG; pno:SNOG_03294; -.
DR   eggNOG; KOG1421; Eukaryota.
DR   HOGENOM; CLU_003212_0_0_1; -.
DR   InParanoid; Q0UY70; -.
DR   OrthoDB; 93889at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IEA:EnsemblFungi.
DR   GO; GO:0034605; P:cellular response to heat; IEA:EnsemblFungi.
DR   GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; IEA:EnsemblFungi.
DR   GO; GO:0120174; P:stress-induced homeostatically regulated protein degradation pathway; IEA:EnsemblFungi.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR025926; PDZ-like_dom.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF12812; PDZ_1; 2.
DR   Pfam; PF13180; PDZ_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 3.
DR   SUPFAM; SSF50494; SSF50494; 2.
PE   3: Inferred from homology;
KW   Apoptosis; Hydrolase; Nucleus; Protease; Reference proteome; Repeat;
KW   Serine protease.
FT   CHAIN           1..1017
FT                   /note="Pro-apoptotic serine protease NMA111"
FT                   /id="PRO_0000320358"
FT   DOMAIN          305..383
FT                   /note="PDZ 1"
FT   DOMAIN          879..960
FT                   /note="PDZ 2"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..278
FT                   /note="Serine protease"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        126
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        157
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        239
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1017 AA;  112679 MW;  3D50A49D183489A6 CRC64;
     MDQNGASTEA RSKRKQPPTS PSTDRPLKQI KPEVDAHTRN GVPKSPELEV VDDAHSVYSL
     EEPIAPVAGA VHDTAEWQKT IEGVVKSVVS IHFCQTCSFD TDPAISSEAT GFVVDAEKGY
     ILTNRHVVGA GPFIGYCIFD NHEECDVYPV YRDPVHDFGI LRFDPKAIKY MSVSALQLRP
     DFAKVGVEIR VVGNDAGEKL SILSGVISRL DRNAPEYGEG YSDFNTNYIQ AAAAASGGSS
     GSPVVNRDGF AVALQAGGRA DGAATDYFLP LDRPLRALEL VRRGEAVTRG TVQTQWILKP
     FDECRRLGLS TDLEKAVRTQ FPKETGMLVA EVVLPQGPAS TKVEEGDILI KVNGEFITQF
     VRLDSILDDN VGKTISVTIQ RAGENLEVEL DVGNLHDITP DRFVSVSGAS FHDLSYQQAR
     LYAISLKNAG VFVCEAAGSF RFADGYASGW LIQEVDNQPT PNLDTFIEVM KKIPDRKRIV
     IQYKHLRDLH TANTSITAVD RHWHAKIRIA TRNDKTGLWD FKPIADPVPA VPQVSRRANF
     VKMSSNYPNA VDIVRSFVRV HVSMPIKLDG FPKMNKQGYG LVVDAEQGLV LVSRAILPYD
     LCDISLIIAD SIFIDAKVVF MHPLQNYVIV KYDPALVNAP VKTPKFATEF IRKGDETIFF
     GLNQNFRPVV AKTVVTDITT VAIPASAITP RYRATNFDAI TVDTNQASHS GSGVLIAEDG
     TVQALWLSYL GERTSHSGKD VEYHLGLATP NLLPILNEIK SGKTPKLRIL NVEFQTVQMS
     QARVMGVSED WIEKTEQADP ERHQLFMVRK VDSGHGGDGM LEGDILLTLN GKLVTRSPDL
     DVMYNNEFLE AVIVRKREEK TIKVTTVATE EIETDRMVSF CGATLHRPHQ AVRQQISKIH
     SDVYISSRAR GSPAYMYGLA PTNFLTHVNN IPTPDLSTFL REVKKIGDNE YFRLKVMTFD
     NVPWVATMKK NEHYFPTIEY VKDDTEALGW KRIIHECEDG GAREEMAIDN EAGGDEE