ID   NM111_ASPTN             Reviewed;        1038 AA.
AC   Q0CSC0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Pro-apoptotic serine protease nma111;
DE            EC=3.4.21.-;
GN   Name=nma111; ORFNames=ATEG_03414;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAU36688.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CH476597; EAU36688.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001212592.1; XM_001212592.1.
DR   AlphaFoldDB; Q0CSC0; -.
DR   SMR; Q0CSC0; -.
DR   STRING; 341663.Q0CSC0; -.
DR   MEROPS; S01.434; -.
DR   PRIDE; Q0CSC0; -.
DR   EnsemblFungi; EAU36688; EAU36688; ATEG_03414.
DR   GeneID; 4317596; -.
DR   eggNOG; KOG1421; Eukaryota.
DR   OrthoDB; 93889at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..1038
FT                   /note="Pro-apoptotic serine protease nma111"
FT                   /id="PRO_0000320348"
FT   DOMAIN          289..374
FT                   /note="PDZ 1"
FT   DOMAIN          877..958
FT                   /note="PDZ 2"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..275
FT                   /note="Serine protease"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        120
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        151
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        233
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1038 AA;  114370 MW;  A334433F97915FE1 CRC64;
     MDLNGDSNAK RKRSSISAAA ERPAKHLRPE NSSLTPGDTT PANGTVYDVE DDAESSHLIP
     IAAAPADSPE WQATIEEVVK SVVSIHFCQT CSFDTELSMS SQATGFVVDA ERGYILTNRH
     VVCPGPFWGY VIFDNHEECD VRPVYRDPVH DFGILKFDPK AIRYLKLTEL KLQPDAARVG
     SEIRVVGNDA GEKLSILSGV ISRLDRNAPE YGEGYSDFNT NYIQAAAAAS GGSSGSPVVN
     IDGHAIALQA GGRADGAATD YFLPLDRPLR ALNCIRRGEP VTRGTIQTQW ILKPFDECRR
     LGLTPEWEAK VRKAAPTETS MLVAEIILPE GPADGKLEEG DVLLQVNGEL LTQFIRLDDI
     LDSSVGKTVR LLVQRGGQNV ELECEVGDLH AITPDRFVTV AGGTFHDLSY QQARLYAIAT
     RGVYVCEAAG SFKLENTLSG WLIDSVDKRP TRNLEEFVEV MKSIPDRSRV VISYRHIRDL
     HTRGTSIVYI DRHWHPKMRL AVRNDETGLW DFSDLADPIP ALPPVPRKAN FIQLDGVSQP
     AAAEIVRSFV RVSCTMPLKL DGYPQAKKTG FGLVIDAEKG LVVVSRAIVP YDLCDINVTV
     ADSIIVSAKV VFLHPLQNYT IVQYDPSLVQ APVQSARLST EYIKQGQSTI FVGFNQNFRI
     VVAKTAVTDI TTVSIPANAS APRYRAINLD AITVDTGLSG QCSNGVLVGE DGVVQALWLN
     YLGERTPSSH KDVEYHLGFA TPALLPVASK VQAGEMPKLR ILNMESYVVQ MSQARIMGVS
     EEWIQRVTQA NPSRHQLFMV RKVDCPPAGF STTAHDSFQE GDIILTLDGQ LITRVSELDI
     MYDKDVLEAL IVRNGQEMKI QVPTVPTEDL ETDRAVVFCG AVLQKPHHAV RQQISKLHSE
     VYVSARSRGS PAYQYGLSPT NFITAVNGVP TPNLDTFVQE VSKIPDNTYF RLRAVTFDNV
     PWVVTMKKND HYFPMSEYIK DPAHPAGWKT VSHDKAKHKD GIAPDAANLN PDAMDEGFDD
     VSELEPEVRL EVGHWTVR