NM111_CHAGB
ID NM111_CHAGB Reviewed; 1030 AA.
AC Q2H334;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Pro-apoptotic serine protease NMA111;
DE EC=3.4.21.-;
GN Name=NMA111; ORFNames=CHGG_03812;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408032; EAQ87193.1; -; Genomic_DNA.
DR RefSeq; XP_001223026.1; XM_001223025.1.
DR AlphaFoldDB; Q2H334; -.
DR SMR; Q2H334; -.
DR STRING; 38033.XP_001223026.1; -.
DR EnsemblFungi; EAQ87193; EAQ87193; CHGG_03812.
DR GeneID; 4392816; -.
DR eggNOG; KOG1421; Eukaryota.
DR HOGENOM; CLU_003212_0_0_1; -.
DR InParanoid; Q2H334; -.
DR OMA; CVFDNHE; -.
DR OrthoDB; 93889at2759; -.
DR Proteomes; UP000001056; 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; -; 1.
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..1030
FT /note="Pro-apoptotic serine protease NMA111"
FT /id="PRO_0000320350"
FT DOMAIN 312..384
FT /note="PDZ 1"
FT DOMAIN 880..960
FT /note="PDZ 2"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..279
FT /note="Serine protease"
FT COMPBIAS 12..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 158
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 240
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1030 AA; 113704 MW; 8FAA33C19804222C CRC64;
MNGTTSPIAA RSKRKEPPHT VDGRHPKHHR TNGEVAPAAD NTPDNQDEFE GEFGVELEEY
EDARLPAVLP TGPDTAEWQA TIQRVVRNVV SIRFCQTCSF DTDPALTSEA TGFVVDAERG
YILTNRHVVG SGPFWGYCIF DNHEEVDAYP VYRDPVHDFG ILKFDPKAIK YMPVDALPLR
PDLAKVGIEI RVVGNDAGEK LSILSGVISR LDRNAPEYGE GYSDFNTCYY QASAAASGGS
SGSPVVNMDG YAVALQAGGR ADGAATDYFL PLDRPLRALK CLQEGNPITR GDIQCQFVLK
PFDECRRLGL TPEWEAQIRK AFPKETNMLV AEIVLPEGPS HKKAEEGDVL IKVNGELLTQ
FIRLDDILDS SVGKPVKLLL LRGGEEIEVE IEVGDLHSIT PDRFVSVAGG SFHSLSYQQA
RLYGVACKGV FVCEAGGSFR FDNAENGWLI QTVDHKKTPD LETFIEVMKG IHDKARVVVT
YKHLRDLHTL NTTILHIDRH WSKKMKLAVR NDETGLWDFT NLADPLPPVA PIPRKADFIQ
LEHTSHPAVA DLVRSFVHVS CVMPVKLDGF PKNRKWGMGL VIDADKGLVV ISRAIVPYDL
CDITVTIADS IVVEGKVVFL HPLQNYAIIQ YDPKLVDAPV LSARLSSQEI TQGASTYFIG
YNRIGRIVHA ATTVTEIFAV TIPANSGAPR YRAVNVDAIT VDTSLSGQCG SGVLVAQDGT
VQALWLTYLG ERNPSTHRDE EYHLGLATPT LLPVVEQIQR GVDPKLRMLS VEFRAIQMSQ
ARLMGVSEEW IQKVSVANTA HHQLFMVTKR TFERNEQEEA AALLEGDVVL SLNGKIITKI
SDLDIMYSNE QLDAVLVRNC EELSLKLDTV AADDVETTRA VSFCGAIFHA PHHAVRQQIS
KLFSEVYVSA RTRGSPSYQY GLAPTNFITH VNGKPTPDLE AFLAEVVKIP DNTYFRLRAM
SFDSVPWVVT MKKNDHYFPT MELIKDPKEE CGWRRITYEG GKVIQGEGPD GVVGSAGEIT
DMDVDADVCG