NM111_ASPOR
ID NM111_ASPOR Reviewed; 1027 AA.
AC Q2TYB1;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Pro-apoptotic serine protease nma111;
DE EC=3.4.21.-;
GN Name=nma111; ORFNames=AO090103000320;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007174; BAE65762.1; -; Genomic_DNA.
DR RefSeq; XP_001826895.2; XM_001826843.2.
DR AlphaFoldDB; Q2TYB1; -.
DR SMR; Q2TYB1; -.
DR STRING; 510516.Q2TYB1; -.
DR EnsemblFungi; BAE65762; BAE65762; AO090103000320.
DR GeneID; 5999186; -.
DR KEGG; aor:AO090103000320; -.
DR HOGENOM; CLU_003212_0_0_1; -.
DR OMA; CVFDNHE; -.
DR Proteomes; UP000006564; Chromosome 8.
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..1027
FT /note="Pro-apoptotic serine protease nma111"
FT /id="PRO_0000320347"
FT DOMAIN 288..373
FT /note="PDZ 1"
FT DOMAIN 875..956
FT /note="PDZ 2"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..265
FT /note="Serine protease"
FT REGION 991..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1027 AA; 113315 MW; 119F18B7C8F87D3F CRC64;
MDLNGDAGAK RKRSSIVPAE RPAKHLKPES SALTPGDSTP ANGTVYDIED EDDASRLLPI
GPAQADSPEW QATIEEVVKS VVSIHFCQTC SFDTELSMSS QATGFVVDAE RGYILTNRHV
VCPGPFWGYC IFDNHEECDV RPVYRDPVHD FGILKFDPKA IRYMNLTELK LQPDAARVGS
EIRVVGNDAG EKLSILSGVI SRLDRNAPEY GEGYSDFNTN YIQAAAAASG GSSGSPVVNI
DGHAIALQAG GRADGAATDY FLPLDRPLRA LECIRRGEPV TRGTIQTQWI LKPFDECRRL
GLTPEWEATV RKAAPTETSM LVAEIILPEG PADGKLEEGD VLLQVNGELL TQFIRLDDIL
DSSVGQTVRL LVQRGGQDVE IECQVGDLHA ITPDRFVTVA GGTFHDLSYQ QSRLYAIATR
GVYVCEAAGS FKLENTLSGW LIDSVDKRPT RNLDEFVEVM KTIPDRSRVV ISYRHIRDLH
TRGTSIVYID RHWHPKMRLA VRNDETGLWD FSDLADALPA LPPVPRKADF IQLDGVSQPA
ASEIVRSFVR VSCTMPLKLD GYPQAKKTGF GLVVDAEKGL VVVSRAIVPY DLCDINITVA
DSIIVNAKVV FLHPLQNYTI IQYDPSLVQA PVQSAKLSTE YIKQGQDTIF VGFNQNFRIV
VAKTAVTDIT TVSIPANASA PRYRAINLDA VTVDTGLSGQ CSNGVLIGED GVVQALWLNY
LGERTPSSHK DVEYHLGFAT PSLLPVVSKI QQGVMPELRI LNMESYVVQM SQARIMGVSE
EWIEKVTQAN PSRHQLFMVR KVDCPPAGFD NMADTFQEGD ILLTLDGQLI TRVSELDVMY
DKEFLEALIV RNGQEMRIQV PTVPTADLET DRAVVFCGAV LQKPHHAVRQ QISKLHSEIY
VSARSRGSPS YQYGLSPTNF ITAVNGVPTP DLDRFVKEVS KIPDNTYFRL RAVTFDNVPW
VVTMKKNDHY FPMSEYLKDP SQPCGWRTVS HNKSKHKDGI APDAANLNPD AMEQGYDGAS
DIEPEAE