NM111_LODEL
ID NM111_LODEL Reviewed; 979 AA.
AC A5DVI0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Pro-apoptotic serine protease NMA111;
DE EC=3.4.21.-;
GN Name=NMA111; ORFNames=LELG_01366;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981525; EDK43188.1; -; Genomic_DNA.
DR RefSeq; XP_001526538.1; XM_001526488.1.
DR AlphaFoldDB; A5DVI0; -.
DR SMR; A5DVI0; -.
DR STRING; 379508.A5DVI0; -.
DR MEROPS; S01.434; -.
DR EnsemblFungi; EDK43188; EDK43188; LELG_01366.
DR GeneID; 5234307; -.
DR KEGG; lel:LELG_01366; -.
DR VEuPathDB; FungiDB:LELG_01366; -.
DR eggNOG; KOG1421; Eukaryota.
DR HOGENOM; CLU_003212_0_0_1; -.
DR InParanoid; A5DVI0; -.
DR OMA; CVFDNHE; -.
DR OrthoDB; 93889at2759; -.
DR Proteomes; UP000001996; 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; IPR025926; PDZ-like_dom.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR Pfam; PF12812; PDZ_1; 2.
DR PRINTS; PR00834; PROTEASES2C.
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..979
FT /note="Pro-apoptotic serine protease NMA111"
FT /id="PRO_0000320354"
FT DOMAIN 277..362
FT /note="PDZ 1"
FT DOMAIN 871..943
FT /note="PDZ 2"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..260
FT /note="Serine protease"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
SQ SEQUENCE 979 AA; 109304 MW; 8753B9F5BCB69A8A CRC64;
MKRNGESHLN GEAKKSRTEQ NQEQQDYQDE YYSSSDEELL PSSQTSPVFD IAHSNSDKWQ
STIRKVVNSV VSIQFSHVAA FDTETALVSE ATGFVVDAER GLILTNRHVV GPGPFTGYVV
FDNHESVDVK PIYRDPVHDF GFLQFDTKDV KYLKLTQLDL DPSLAKIGTE IRVVGNDNGE
KLSILAGIIS RIDRNAPDYG ALTYNDFNTE YIQAAASATG GSSGSPVVNE DGKCVALQAG
GSTEASTDFF LPVSRPKRAL QCIQKGLPIT RGDIQVEWQL KPFDECARLG FTAEAEAEAR
KMFPDKIGML VAELVLPEGP ADGLIKEGDT LISIQGEYIS TFVRVDEILD ENVGKELEFV
FQRSGREIKQ MIKIGNLHAI TPDRFVHVAG ASFNNLSYQV ARCYCLPVRG LYVCDGSGSF
EFSNQDTLGF IVETVDDKPV ANLDEFVEVM KQLPDCSRVP VVYRHVSDMH AEYVQTIYID
RHWYTSFKLA VRNDTTGLWD FTTLQKEALP PAALVPQNAK YVDIPFSDPS RAECSKLVRS
FVQVRTLCPS GVDSHPFKKD IGYGVVVDST NGYVLVSRRY VPHYMCDIFV VFAESIDVAG
EVVFLHPHLN YAIIKYDPKL VLADVQSPKF SETPLKRGDD LFFIGYNYNL RVVTDDVKVS
SISSLNVTAN SIAPRYRGTN LECILLDSKL THECNTGVLV DNDGTLRAFW LSYLGESNEL
SFKMGLDVTD VLSILKSLQA NHIPKSLRML DAEFASLTVL QGRTRGVPQT WIKRFEDEAQ
DLIKFLSVDR VSAPTFEAKP SPLKVGDIVL SVNGKLVKNM RDFASMYDET SLTFNIIRQK
QEMTLEVPTI DTTSMETSHV VSWSGALLQK PHYGVRQLMT KIPSEVYIVD KSSCGPAHQY
GIVPISFITH VNDQETKDLD SFIQVVKLIP DKTYVKLRLV SFDNIPAAIS LKTDYHYFPT
TTLKRDAVSG KWNTEKINE