ID   NM111_AJECN             Reviewed;        1028 AA.
AC   A6RG85;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Pro-apoptotic serine protease NMA111;
DE            EC=3.4.21.-;
GN   Name=NMA111; ORFNames=HCAG_08651;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDN04997.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CH476666; EDN04997.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001536330.1; XM_001536280.1.
DR   AlphaFoldDB; A6RG85; -.
DR   SMR; A6RG85; -.
DR   STRING; 339724.A6RG85; -.
DR   EnsemblFungi; EDN04997; EDN04997; HCAG_08651.
DR   GeneID; 5442702; -.
DR   KEGG; aje:HCAG_08651; -.
DR   HOGENOM; CLU_003212_0_0_1; -.
DR   OrthoDB; 93889at2759; -.
DR   Proteomes; UP000009297; 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; 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   Pfam; PF12812; PDZ_1; 2.
DR   Pfam; PF17820; PDZ_6; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
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..1028
FT                   /note="Pro-apoptotic serine protease NMA111"
FT                   /id="PRO_0000320343"
FT   DOMAIN          292..377
FT                   /note="PDZ 1"
FT   DOMAIN          878..959
FT                   /note="PDZ 2"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..269
FT                   /note="Serine protease"
FT   REGION          1003..1028
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1017
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        123
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        154
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        236
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1028 AA;  113146 MW;  F76995066B0E9CC2 CRC64;
     MEMSSKRKHS SGPISLRSTK HLRSDTAASP QPLTPDDQTL GEEAVYVLDN EDEDLSHVLP
     LAPAAAAQTD SPEWQATIET VVKSVVSIHF CQTASFDTDL SMSSQATGFV VDAEKGYILT
     NRHVVCAGPF WGYCIFDNHE ECDVRPVYRD PVHDFGILKF DPAAIKYMPV TELKLSPDAA
     KVGVEIRVVG NDAGEKLSIL SGVISRLDRN APEYGEGYSD FNTNYIQAAA AASGGSSGSP
     VVNIDGHAIA LQAGGRADGA ATDYFLPLDR PLRALECIRK GVPVTRGTIQ TQWIIKPFDE
     CRRLGLSPEW EAAVRKGSPK ETGMLVAEIV LPEGPGDGKL QEGDVLIKVN GELLTQFVKL
     DAILDSSVGK DVHLLVQRGG EDLEVSCTVG DLHAITPARY VTVAGATFHD LSYQQARLYA
     IACKGVYVCE AAGSFKLENT FSGWIVDTVD KRPTKNLDEF IEVMKTIPDR ARVALSYRHI
     RDLHTRGTSI VHIDRHWHPH IREAIRNDET GLWDFTNIAD PLPAEPPVPR KADFIQLDGA
     NHPAAADIVR SFVRVSCTMP VKLDGYPQAR KAGFGLVVDA EAGLVLVSRA IVPFDLCDIN
     VTVADSIIVM AKVIFLHPLQ NYTIIQYDPS LVQAPVKTAR LSTNYIKQGA DTIFVGFNQN
     FRIVVAKTAV TDITTVAIPP NAAAPRYRAL NLDAITVDTG LSSQCSNGVL IGEDGIVQAL
     WLNYLGERTA SSHKDVEYHL GLATPSLLPI INQIESGSLP KLRIMDMESY VIQMSQARIM
     GVSEEWIEKV AIANPARHEL FMVRKVDCAS PLTEDTHQLE EGDIILTLND KLITRVSEFD
     IMYHHETLDA LIVRNGQEMR VNIKTVPTED LETDRALIFC GAVLQKPHHA VRQQISKLHS
     EVYVSARSRG SPAYQYGLSP TNFITAVNGV KTPDLDSFIK QVNVIPNNTY FRLRAVTFDN
     VPWVVTMKKN DHYFPMSEYI KDPSAPEGWR SISHDKELLR LDSDNLNADA MDEGRDDGIS
     DMEPDGEK