ID   NM111_ASPNC             Reviewed;        1028 AA.
AC   A5AB13;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Pro-apoptotic serine protease nma111;
DE            EC=3.4.21.-;
GN   Name=nma111; ORFNames=An08g08670;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAK96647.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM270178; CAK96647.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001392979.2; XM_001392942.2.
DR   AlphaFoldDB; A5AB13; -.
DR   SMR; A5AB13; -.
DR   MEROPS; S01.434; -.
DR   PaxDb; A5AB13; -.
DR   EnsemblFungi; CAK96647; CAK96647; An08g08670.
DR   GeneID; 4983185; -.
DR   KEGG; ang:ANI_1_1198074; -.
DR   Proteomes; UP000006706; Chromosome 8R.
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; -; 1.
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..1028
FT                   /note="Pro-apoptotic serine protease nma111"
FT                   /id="PRO_5000242372"
FT   DOMAIN          289..374
FT                   /note="PDZ 1"
FT   DOMAIN          876..957
FT                   /note="PDZ 2"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..266
FT                   /note="Serine protease"
FT   REGION          983..1028
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   1028 AA;  113400 MW;  65729E729CD12EB2 CRC64;
     MDLNGDAGAK RKRSSITTPA ERPVKHLRPE SSALTPGDST PANGTVYDVE DDEDASRLLP
     VGPAQADSPE WQATIEEVVK SVVSIHFCQT CSFDTELSMS SQATGFVVDA ENGYILTNRH
     VVCPGPFWGY CIFDNHEECD VRPVYRDPVH DFGILKFDPK AIRYMKLREL KLQPDAAKVG
     SEIRVVGNDA GEKLSILSGV ISRLDRNAPE YGDGYSDFNT NYIQAAAAAS GGSSGSPVVN
     IDGHAIALQA GGRADGAATD YFLPLDRPLR ALECIRRGEP VTRGTIQTQW ILKPFDECRR
     LGLTPEWEAT VRKAAPTETS MLVAEIILPE GPADGKLEEG DVLLQVNGVL LTQFIRLDDI
     LDSSVGQTVR LLVQRGGQNV EIECQVGDLH AITPDRFVTV AGGTFHNLSY QQSRLYAIAT
     RGVYVCEAAG SFKLENTLSG WIIDSVDKRP TRNLDEFVEV MRTIPDRSRV VISYRHIRDL
     HTRGTSIVYI DRHWHPKMRL AVRNDDTGLW DFSDLADPIP ALPPVPRKAD FIQLDGVSQP
     AAADIVRSFV RVSCTMPLKL DGYPQAKKTG FGLVVDAEKG LVVVSRAIVP YDLCDINVTV
     ADSIIVNAKV VFLHPLQNYS IIQYDPSLVQ APVQSAKLAT DYIKQGQDTI FVGFNQNFRI
     VVAKTAVTDI TTVSIPANAS APRYRAINLD AITVDTGLSG QCSNGVLIGE DGVVQALWLN
     YLGERTSNSH KDVEYHLGFA TPSLLPVLSK VQQGEMPELR ILNMESYVVQ MSQARIMGVS
     EEWIEKVTQA NPSRHQLFMV RKVDCPPPGF NSAADTFEEG DIILTLDGQL ITRVSELDIM
     YEKDTLEALI VRNGQEMRIQ VPTVPTEDLE TDRAVVFCGA VLQKPHHAVR QQISKLHSEV
     YVSARSRGSP SYQYGLAPTN FITAVNGVPT PNLDRFSEEV SKIPDNTYFR LRAVTFDNVP
     WVVTVKKNDH YFPMSEYIKD QSQPSGWRTV SHDKDKYKDG IAPDAANLNP DAMDEGFDGV
     SDIEPDLE