NM111_DEBHA
ID NM111_DEBHA Reviewed; 987 AA.
AC Q6BKM0; B5RUK4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Pro-apoptotic serine protease NMA111;
DE EC=3.4.21.-;
GN Name=NMA111; OrderedLocusNames=DEHA2F20768g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAR66382.1; -; Genomic_DNA.
DR RefSeq; XP_002770862.1; XM_002770816.1.
DR AlphaFoldDB; Q6BKM0; -.
DR SMR; Q6BKM0; -.
DR STRING; 4959.XP_002770862.1; -.
DR EnsemblFungi; CAR66382; CAR66382; DEHA2F20768g.
DR GeneID; 8999024; -.
DR KEGG; dha:DEHA2F20768g; -.
DR VEuPathDB; FungiDB:DEHA2F20768g; -.
DR eggNOG; KOG1421; Eukaryota.
DR HOGENOM; CLU_003212_0_0_1; -.
DR InParanoid; Q6BKM0; -.
DR OMA; CVFDNHE; -.
DR OrthoDB; 93889at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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 Gene3D; 2.40.10.10; -; 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; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; 3.
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..987
FT /note="Pro-apoptotic serine protease NMA111"
FT /id="PRO_0000320352"
FT DOMAIN 279..364
FT /note="PDZ 1"
FT DOMAIN 878..950
FT /note="PDZ 2"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..262
FT /note="Serine protease"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
SQ SEQUENCE 987 AA; 110741 MW; 4269B20729DA6C35 CRC64;
MPDIPTKRRL SNGSVIDNTN KRQMQSSFVP EVEQESDGYL SEDSSDQPIF DMAVAANSNQ
WQETITKVVK SVVSIQFTHV SNFDTESSIV SEATGFVVDA KRGLILTNRH VVGPGPFCGY
VVFDNHEEAV VKPIYRDPVH DFGFLQFDAK SIKYMDVTQL ELKPDLAKVG TEIRVVGNDA
GEKLSILAGF ISRLDRNAPD YGALTYNDFN TEYIQAAASA SGGSSGSPVV NEDGHAVAIQ
AGGSSEASTD FFLPVYRPLR ALRCIQESQP ITRGDIQVEW SLKPFDECRR LGLTSEAERI
ARERFPDKIG LLVAELVLPE GPADELIKEG DTLISINDEP ISTFIKVDEI LDESVGKELK
VVIQRGGEEI TQTIKIGDLH SITPDRYVDV AGASFNQMSY QVARCYCIPV KGVYINDASG
SFEFSTFEKT GWLLETVDDK QTPDLDTFIE VMKQIPDRQK VTITYRHVSD LHTESIQVIY
IERHWQSTFR LAVRNDKSGL WDFTDIQDKP LPPLKLEPQN AKYINIPFEN EEKQGCASLV
KSFVQVRTVA PVPMDSYPYR KEIGYGVVVD ATNGYVLVSR RFVPHDMCDI FVIFAESVDI
PGKVVFLHPN QNYAIIKYDP KLVLADVQAP KFSDKPLKRG EKSFFVGYNY NLRLVTEDVK
VSGISSLNVP AASLSPRYRG TNLECVLLDS KLCQECDSGV LADEDGTLRS FWLSYLGESN
CDQTTDRMYR MGLDVTDVLD VINKLKDNEI PVDLRILDAE FSSITILQGR TRGVPQKWIN
EFEKVCHDEL KFLSVERVAA AKLNQTPNPL KIGDILLSVN GSIVKTMRDL KIMYNKPSLD
FKIIRSKKEM DITVPTVETT SLNTSHVVFW CGAILQAPHH GVRQLMEKIP SEVYVTRKNS
GGPAHQYGIV TNSFITHVND KETKNLESFM DAITDIADNT YIKLRLVSFD NVPVAISVKT
NYHYFPTAEL KKNKETGEWK EIEHKEK