ID A0A167CIC9_9HYPO Unreviewed; 1010 AA.
AC A0A167CIC9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BBO_05767 {ECO:0000313|EMBL:OAA41231.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA41231.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA41231.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA41231.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
CC -!- FUNCTION: Nuclear serine protease which mediates apoptosis.
CC {ECO:0000256|ARBA:ARBA00002558}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA41231.1}.
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DR EMBL; AZHA01000017; OAA41231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167CIC9; -.
DR OrthoDB; 1779375at2759; -.
DR Proteomes; UP000076863; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; -; 1.
DR InterPro; IPR025926; PDZ-like_dom.
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; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 388..464
FT /note="PDZ-like"
FT /evidence="ECO:0000259|Pfam:PF12812"
FT DOMAIN 863..940
FT /note="PDZ-like"
FT /evidence="ECO:0000259|Pfam:PF12812"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1010 AA; 111632 MW; B49F51F7A68F6185 CRC64;
MNGHSMAGAK RKSSGSPDRA PAPKRVPNGN HSHDENTSDT DSIHYDDEFD LVDEGDMYSG
TPVSLGEWQD TIQKVVRNVV AIRFCQTCSF DTDPALTSEA TGFVVDSERG YILTNRHVVG
SGPFWGHCVF DNHEEVDCYP VYRDPVHDFG ILRYDPKALK YMQVDGLDLT PDQAKVGVEI
RVVGNDAGEK LSILSGVISR LDRNAPEYGE GYSDFNTCYY QANAAASGGS SGSPVVCKDG
TAVALQAGGR SDGASTDYFL PLDRPLRALQ CIQQGKPVTR GDIQCQFLLK PFDECRRLGL
SPHWEAAIRQ EFPDETNMLV GEIILPDGPS HKKIEEGDVL IKVNGQLITQ FLRLDDILDS
SVGQPIKLQL QRGGQDIEVE IEVGDLHKIT PDRFVSVAGA SFHDISYQQA RLYAVAVKGV
YVCESAGSFR FDNTDNGWII QSVDNKKVPD LDTFIQVMKG IPDKARVVVK YKHLRDLHTL
NTTVIYVDRH WSAKMKLAVR NDITGLWDFS DLGDPLPPVA PVRRSAAFIE LDHMPDPSIA
KLIRSFVHIN CTMPVKLDGF PKNRRWGMGL VIDAEKGIVL ISRAVVPYDL CDITITIADS
IIVEGKVLFL HPLQNYTIVK YDPSLVDAPV VSARLSSEPL TQGAKTHFLG YNRIGRVVHG
STTVTEITAV AIPANSAAPR YRAVNVDAIT IDSNLGSSCN SGVLVAPDGT VQALWLSYLG
ERSSCSQRDE EYYLGLGTPT LLPVISAIQR GEMPKLRLLS VEFRSIQMSQ ASVMGVSDEW
IKKVTQANRS HHQLFMVSKR TFERGSMPVS LLEGDIILTL NGKICTTITD FDIMYSNTVL
DAVIMRENEE IQLQLPTVPA EDLETDHAVA FCGAILHRPH QAVRQQISKL HSEVYVSSRI
RGSPAYQYGV APTNFITHVN AEPTPDLDSF IAATRKIPDN TYFRLKAVTF DCVPWVITMK
KNDHYFPTME WIKDNSEPCG WRRVTYEGAA VTNGEAVDGV PLPADDAEME
//