ID   NM111_VANPO             Reviewed;         990 AA.
AC   A7TGI3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Pro-apoptotic serine protease NMA111;
DE            EC=3.4.21.-;
GN   Name=NMA111; ORFNames=Kpol_1048p20;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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}.
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DR   EMBL; DS480387; EDO18590.1; -; Genomic_DNA.
DR   RefSeq; XP_001646448.1; XM_001646398.1.
DR   AlphaFoldDB; A7TGI3; -.
DR   SMR; A7TGI3; -.
DR   STRING; 436907.A7TGI3; -.
DR   GeneID; 5546890; -.
DR   KEGG; vpo:Kpol_1048p20; -.
DR   eggNOG; KOG1421; Eukaryota.
DR   HOGENOM; CLU_003212_0_0_1; -.
DR   InParanoid; A7TGI3; -.
DR   OMA; FWGHCVF; -.
DR   OrthoDB; 1779375at2759; -.
DR   PhylomeDB; A7TGI3; -.
DR   Proteomes; UP000000267; 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   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 2.
DR   Gene3D; 2.40.10.120; -; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR025926; PDZ-like_dom.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR46366; PRO-APOPTOTIC SERINE PROTEASE NMA111; 1.
DR   PANTHER; PTHR46366:SF8; PRO-APOPTOTIC SERINE PROTEASE NMA111; 1.
DR   Pfam; PF12812; PDZ_1; 2.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 3.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
PE   3: Inferred from homology;
KW   Apoptosis; Hydrolase; Nucleus; Protease; Reference proteome; Repeat;
KW   Serine protease.
FT   CHAIN           1..990
FT                   /note="Pro-apoptotic serine protease NMA111"
FT                   /id="PRO_0000320361"
FT   DOMAIN          290..368
FT                   /note="PDZ 1"
FT   DOMAIN          758..843
FT                   /note="PDZ 2"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          73..263
FT                   /note="Serine protease"
FT   ACT_SITE        111
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        142
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        225
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   990 AA;  110302 MW;  02E7FD66B2BF865F CRC64;
     MSVTNSNRKR SLSEVSEGSD PEAPAKTRNS YTTDEIVMVE EVDSEIPVNI SSYGDAETYL
     KWQNTIAKVV KSVVSIHFSQ VAPFDSDNAV VSQATGFVVD ASLGIILTNR HVVGPGPFVG
     YAVFDNHEEC DVTPIYRDPV HDFGFLKFDP TKIKYMNIQA LELKPSLAKV GSEIRVVGND
     AGEKLSILSG FISRLDRNAP DYGELTYNDF NTEYIQAAAA ASGGSSGSPV VNSDGYAVAL
     QAGGSTEAST DFFLPLDRIL RALKCLQSNK PITRGTIQLQ WLLKPFDECR RLGLTADRES
     QARAQFPDKI GLLVAETILR EGPSDIKIKE GDTLISINGE LISSFIQVDD ILDESIGKEI
     EIIIQRGGIE HTVKCEVGDL HSITPDRYVE VCGATFHELS YQMARFYGMP VRGVFISSAS
     GSFNIDANER VGWIVDSIDN KETPNLDTFI EVMKTIPDRQ RVTLRYHHLT DQHTIHVTSI
     YIDRHWCSEF RLYKRNDVTG IWDYENVAEP IKAEELKPHA AKFIDIPIDI PEIATLSHSL
     CMVSTVSAIP LDSLPVENVK TSGLVIDAEQ GYIIVSRRAV PHDCLDVFVT FADSVMIPAS
     IVFLHPTKNY AIIKYDINLV NANIITPKLS NTPMKRGDRT RFIGFTHNNR LVTSETSVTD
     ISSISIPSNI IPRYRATNLE AISIDCNVST KCNSGILTDN DGTIRALWLS FLGERQDNKD
     KIYLMSLDIT DCKEVIELLK EGKKPKVSII DAGFGAISIL TARIRGVPEE WIKKMELQSE
     NRLQFISVSR VSFTEEPVKL QTGDVILAVN DKLVTEMSQL DGVVSTADDE ESQTLRFKVV
     REGKIIDLNI KTIYVKETSQ IAVFSGSILQ PPHHAVWQSM MNIPSGVYCT FRGESSPALQ
     FGISATNFIT HVNETETPDL DTFLKVIKQI PDNTYCKMRL MTFDNVPFAI SLKTNYHYFP
     TTELKKNIES GKWIENELNK TEEKKIIKSD
//