ID   NM111_ASHGO             Reviewed;         977 AA.
AC   Q75D90;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Pro-apoptotic serine protease NMA111;
DE            EC=3.4.21.-;
GN   Name=NMA111; OrderedLocusNames=ABR134C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 37-47 AND 50.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016815; AAS50905.2; -; Genomic_DNA.
DR   RefSeq; NP_983081.2; NM_208434.2.
DR   AlphaFoldDB; Q75D90; -.
DR   SMR; Q75D90; -.
DR   STRING; 33169.AAS50905; -.
DR   PRIDE; Q75D90; -.
DR   EnsemblFungi; AAS50905; AAS50905; AGOS_ABR134C.
DR   GeneID; 4619191; -.
DR   KEGG; ago:AGOS_ABR134C; -.
DR   eggNOG; KOG1421; Eukaryota.
DR   HOGENOM; CLU_003212_0_0_1; -.
DR   InParanoid; Q75D90; -.
DR   OMA; CVFDNHE; -.
DR   Proteomes; UP000000591; Chromosome II.
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; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR025926; PDZ-like_dom.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF12812; PDZ_1; 2.
DR   Pfam; PF17820; PDZ_6; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   SUPFAM; SSF50494; SSF50494; 2.
PE   3: Inferred from homology;
KW   Apoptosis; Hydrolase; Nucleus; Protease; Reference proteome; Repeat;
KW   Serine protease.
FT   CHAIN           1..977
FT                   /note="Pro-apoptotic serine protease NMA111"
FT                   /id="PRO_0000320344"
FT   DOMAIN          271..356
FT                   /note="PDZ 1"
FT   DOMAIN          749..835
FT                   /note="PDZ 2"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..254
FT                   /note="Serine protease"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        102
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        133
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        216
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   977 AA;  108313 MW;  D299524CB8CF88AC CRC64;
     MTIQAHKRTL SEVSTSSVGQ LKRREGYTED YTDEGSDIDM PEYVTDSANN QQWQDTISRV
     VQSVVSVHFA QVAPFDCESA LVSEATGFVV DAKLGIILTN RHVVGAGPFS GYAVFDNHEE
     CDVIPIYRDP VHDFGFLKFD PSTIKYMNVQ ALELKPALAK VGSEIRVVGN DAGEKLSILA
     GFISRVDRNA PDYGELTYND FNTEYIQAAA AASGGSSGSP VVNIDGYAVA LQAGGSTEAS
     TDFFLPLDRI LRALRCIQGS QPITRGTIQT QWLLKPYDEC RRMGLSPESE AKAREQFPGK
     IGLLVAETIL REGPADKSIK EGDILISING QMICSFIQVD AILDENVGKP ITLVVQRSGI
     DITVECTVGD LHAITPSRYV EVCGATFNEL SYQMARYYAI PVRAVFLSSA TGSFCFDTKE
     KLGWIVDEVN NQPTPTLDTF IEVMSTIPDC SRVTVQYHHL VDQHSPHVTT VYIDRHWCNE
     FRIFERNDET GIWDYKNLAD PIPALPLKPQ TAKFIDLPIS NPKLARLARM LVMVSTIGPV
     PLDSVDPEPR KAAGLVLDAK QGYVIVSRRI VPHDCMDVFV TIAESVLVPA SVVFLHPTQN
     YVIVKYDPAQ VQAAVETPIL STERLKRGDK VQFVGYTHNF RSVSSETTVT DISSLSIPSN
     MVPRYRATNL EAISIESSVG SRCHSGILAD DDGTVRALWL SFLGEKQDEK DKIYLMGLDL
     VDIGEVVEVL KKGKIPRVNI VDSGFGSISV LQARLRGVPE EWIKRMESES ENRLQFITVT
     RVSYTDEEQK LVSGDIILSV NDQLVKQMRD LEGIVTTTDV PAVQQVLRFK IVRKGSIMDL
     DIKTIEVEET SKIVIFAGCI LQAPHHAVRQ AMLNIPSGVY CTFRGQSSPA IQYGISSTNF
     ITHVNEIETP DLDRFLEVVR TIPDNTYCKI RLVTFDNVPF AISLKTNYHY FPTSELSRNS
     DTGRWIEHLC NATPAKN