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Database: UniProt
Entry: A0A0D1YY83_9PEZI
LinkDB: A0A0D1YY83_9PEZI
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ID   A0A0D1YY83_9PEZI        Unreviewed;      1171 AA.
AC   A0A0D1YY83;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Pro-apoptotic serine protease NMA111 {ECO:0000256|ARBA:ARBA00020338};
DE   AltName: Full=Pro-apoptotic serine protease nma111 {ECO:0000256|ARBA:ARBA00021524};
GN   ORFNames=PV09_03523 {ECO:0000313|EMBL:KIW05657.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW05657.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIW05657.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW05657.1,
RC   ECO:0000313|Proteomes:UP000053259};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Nuclear serine protease which mediates apoptosis.
CC       {ECO:0000256|ARBA:ARBA00002558}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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DR   EMBL; KN847537; KIW05657.1; -; Genomic_DNA.
DR   RefSeq; XP_016215526.1; XM_016356733.1.
DR   AlphaFoldDB; A0A0D1YY83; -.
DR   STRING; 253628.A0A0D1YY83; -.
DR   GeneID; 27311496; -.
DR   VEuPathDB; FungiDB:PV09_03523; -.
DR   HOGENOM; CLU_003212_0_0_1; -.
DR   InParanoid; A0A0D1YY83; -.
DR   OrthoDB; 1779375at2759; -.
DR   Proteomes; UP000053259; 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:InterPro.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.120; -; 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; 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; PF17820; PDZ_6; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 3.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
PE   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053259};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          452..524
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   REGION          126..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1171 AA;  129158 MW;  D6C18C218606F056 CRC64;
     MHAGLRTAFR RATSASIFET SATTRRLSSC SNNSSILRHI SGSLPPLHPR LSVRPQPTNL
     PGRIHRFLVH PGQASVHTGR LRQVVRTTKE LAPSAAAHHP VALSPLLGEP ARSREAPVLV
     YRRALSTSSS LQNMSSTSEQ RLSKRKQPPN PSNDRPMKQF KHQDAGGYAN GVDNTFSNGG
     SPELARGSSN ANDMPLDIDE GRALSRVPTT TAAETAEWQA TVEKVIKNVV SIHFCQTHSF
     DTDGAIASEA TGFVVDAENG YILTNRHVVG AGPFWGYCIF DNHEECDVFP VYRDPVHDFG
     ILRFDPKKIK YMPVTALKLR PDLAKVGSEI RVVGNDAGEK LSILSGVISR LDRNAPEYGD
     GYCDFNTNYI QAAASASGGS SGSPVVNQDG YAVALQAGGR CDGAATDYFL PLDRPLRALQ
     CIQRGIPVSR GTIQTQWLLK PYDECRRLGL TANWEAAMRA RFPNETGLLV AETVLPKGPA
     HEKLEEGDVL LKVNGELVSQ FIRLDDILDS SVSKKVTLLV QRGGRDIEVE LEVGDLHAIT
     PDRFVQVAGA TFHDLSYQQA RLYAISIKGN GVYVCETGGT FRLDGSESGW MIQSVNNEET
     PDLDTFIKVM AAIPDRSRVV IAYKHLRDLH TRNTAIINVD RHWHKKMRLA VRNDKTGLWD
     FSDLAEPLPA EPRSPQRANF ITMTNEQYPQ AVDIVRSFVR VTCLLPVKLD GFPRGRKTGH
     GLVVDAEKGL VVISRAIVPY DMCDIHVTIA DSIQVPGKVL FMHPLQNFTV LQYDAKLVHA
     PVQSAKLSKE YVKQGQEVVF FGFNQNYRPV TAKTTITDIT TVAIPASAAT PRYRAVNIDA
     ITVDTNLAAQ CGSGVLMSED GTVQALWLTY LGDRSGHSGK DVEYHLGLQT PMVQPVIDQI
     QAGVIPDLRI LNAELHTCPM DHARILGVTE EWIERVERDD PERHQLFMVR KVDSGHNGEG
     LQESDVLLTL NGKLITRVSD LDIQYNNEVL DAVIVRRREI INIKVSTTAT SNIETSRVVV
     FCGALLHRPH HAVRQQISKI HSDVYISGRT RGSPAYMYGL APTNFITHLN GIPTPDLETF
     LREAEKIPDN TYFRLKVMTF DNVPWVVTMK KNDHYFPTVD MVKDSSEELG WRITVREGEK
     GGEAEVPGTG NVEVEAGGNV TEAPDGVKAR L
//
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