ID   NM111_CANGA             Reviewed;         979 AA.
AC   Q6FLE2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Pro-apoptotic serine protease NMA111;
DE            EC=3.4.21.-;
GN   Name=NMA111; OrderedLocusNames=CAGL0L04092g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380958; CAG61922.1; -; Genomic_DNA.
DR   RefSeq; XP_448952.1; XM_448952.1.
DR   AlphaFoldDB; Q6FLE2; -.
DR   SMR; Q6FLE2; -.
DR   STRING; 5478.XP_448952.1; -.
DR   EnsemblFungi; CAG61922; CAG61922; CAGL0L04092g.
DR   GeneID; 2890766; -.
DR   KEGG; cgr:CAGL0L04092g; -.
DR   CGD; CAL0135960; CAGL0L04092g.
DR   VEuPathDB; FungiDB:CAGL0L04092g; -.
DR   eggNOG; KOG1421; Eukaryota.
DR   HOGENOM; CLU_003212_0_0_1; -.
DR   InParanoid; Q6FLE2; -.
DR   OMA; CVFDNHE; -.
DR   Proteomes; UP000002428; Chromosome L.
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; 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..979
FT                   /note="Pro-apoptotic serine protease NMA111"
FT                   /id="PRO_0000320349"
FT   DOMAIN          273..361
FT                   /note="PDZ 1"
FT   DOMAIN          750..836
FT                   /note="PDZ 2"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..255
FT                   /note="Serine protease"
FT   ACT_SITE        103
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        134
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        217
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   979 AA;  109126 MW;  0E9FE49198108455 CRC64;
     MTIMNEGKKR SHSSSSDDHL AKRQYVEHGN ECIMADEDID TAIFEDGIKN NMQWQDTISK
     VVKAVVSIHF AQVAPFDCDP ALVSEATGFV VDSELGIILT NRHVVGAGPF VGYVVFDNHE
     ECDVIPIYRD PVHDFGFLKF DPKKIKYTKI HALELKPSLA KVGSEIRVVG NDAGEKLSIL
     AGFISRIDRN APDYGELTYN DFNTEYIQAA ASASGGSSGS PVVNVDGYAV ALQAGGSTEA
     STDFFLPLDR ILRALKCIQA DQPITRGTIQ TQWLLKPYDE CKRLGLTPEH ESTSRALFPD
     RIGLLVAETI LREGPSDGKI KEGDILIAIN GQRISTFIQV DDILDSNVGN NVEFTVQRGG
     TDINVTCTIG DLHAITPSKY VEVCGATFNE LSYQMARFYA LPIRGVFLSS ASGSFNFDNK
     EKIGWIVDSV NYQDTPNLDA FVEVMKTIPD KSRVTVRYHH LTDQHSPNVT SIYIDRHWCS
     EFRIYERNDK TGIWDYTNVA DPISEEPLKP HTAKFIPIPS TNPEIAKLSS SLCMVHTVAA
     IPIDSLSAET LKTSGLIIDA EQGYVIVSRR AVPHDCLDVF VTIADSIVIP ATIEFLHPMQ
     NYAIVKYDPN LVKAPVVTPK LSNRRMKRGE SAQFIGYTHN NRLITSETSV TDISSVSIPS
     NLIPRYRATN LEAISIDSNI SPRCNFGIMT DQDGTVRALW LSFLGERQEN KEKVYLMGLD
     IMDCKNVINI LKSGKKPQVH IIDAGFGSIS ILHARIRGVP EEWIQKMEAE SNNRLQFITV
     SRVSYTEETV KLQTGDVILS VNDKLVTEMD QLSGIVHASD ENIDSHVLHF KVVRDGKIVD
     LDMKTVQVDE TDQIVIFAGC ILQKPHHAVR QAMSDIPKGV YCTFRGESSP AIQYGISATN
     FITHVNEIPT PDLDKFLEVV RQIPDNTYCK IRMMTFDNVP FAISLKTNYH YFPTAELKKN
     KDTGKWIEKE YNNSQEIPK