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Database: UniProt
Entry: A0A177CAG5_9PLEO
LinkDB: A0A177CAG5_9PLEO
Original site: A0A177CAG5_9PLEO 
ID   A0A177CAG5_9PLEO        Unreviewed;      1262 AA.
AC   A0A177CAG5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=CC84DRAFT_1219041 {ECO:0000313|EMBL:OAG03768.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG03768.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG03768.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG03768.1,
RC   ECO:0000313|Proteomes:UP000077069};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KV441554; OAG03768.1; -; Genomic_DNA.
DR   RefSeq; XP_018034133.1; XM_018183050.1.
DR   AlphaFoldDB; A0A177CAG5; -.
DR   STRING; 1460663.A0A177CAG5; -.
DR   GeneID; 28766536; -.
DR   InParanoid; A0A177CAG5; -.
DR   OrthoDB; 1779375at2759; -.
DR   Proteomes; UP000077069; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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; PF00595; PDZ; 1.
DR   Pfam; PF12812; PDZ_1; 2.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
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:0000313|EMBL:OAG03768.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT   DOMAIN          474..552
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   DOMAIN          1047..1128
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
FT   REGION          76..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..187
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1262 AA;  139240 MW;  B9F6A30B65CE312C CRC64;
     MSDTEKNSGA GKANSGWTDK ERLVYLIGLL ENSGTKLDFK NAPRPNGRSE IACERMVGRL
     KTAYKAELDA LKAGQHLDGG DAATPKKRGS KAKGTGGDDE GTPKTPKRKG KTAVEDGGSP
     KKKGKKTDAT AEVKDELAMS SLAGAFRHLH LAPHLVTQRR RFTTDPMPAE HHGEHDTRSK
     RKQPPTPSSE RPMKQIKPEA THARNGTYAA AESEPLARDQ SPTPSMDIDE FVPPQIAAAV
     HDTAEWQRTI ETVVKSVVSI HFCQTCSFDT DPAVASEATG FVVDAERGYI LTNRHVVGAG
     PFIGYCIFDN HEECDVFPVY RDPVHDFGIL RFDPKEIKYM PVTALELHPK KAQVGVEIRV
     VGNDAGEKLS ILSGVISRLD RNAPEYGEGY SDFNTNYIQA AAAASGGSSG SPVVNVNGHA
     VALQAGGRAD GAATDYFLPL DRPLRALELI REGKPVSRGT IQTQWILKPF DECRRLGLSP
     DVEKAVRTQF PKETGMLVAE VVLKNGPASK HVEEGDVLVK VNGELLTQFV RLDAVLDDSV
     GGKVSLTIQR AGEDLEVELD VTDLHAITPD RFISVAGASF HDLSYQQARL YAISLENAGV
     YVCEAAGSFR FAEGFTSGWL VQEVDNQPTP NLEAFIEVMR KIPDRKRVVM VYKHLRDLHT
     ANTSITTIDR HWHAKMRVAK RNDETGLWDF TTIADAIPAV PNVPRKANFI KLTSNFPAAV
     DIIRSFVRVH VHMPIKLDGF PKSNKQGYGV VVDAEQGLVL VSRALLPYDL CDISLIIADS
     IFVDAKVVFM HPLQNYAIIK YDTSLVNAPV KTPKFATEFI KKGDETIFFG MNQNFRPVVT
     KTSVTDISTV AIPASAVTPR YRATNFDAIT VDTNQASHSH SGVLVAEDGT VQALWLSYLG
     ERTSQSGKDV EYHLGLAVPM ILPVLEQIRS GKTPKLRILN VEFQTVQMSQ ARVMGVPEEW
     IEKTEHEDPE RHQLFMVRKV DSGHEGGLME GDVLLTLNGK LITRAPDLDV MYDHDFLDAA
     IVRKRQEVTL KVPTVATEDL ETARVVNFCG ATLHRPHQAV RQQISRIHSD VYISSRSRGS
     PAYMYGLAPT NFLTHVNNVP TPDLDSFLRE AKKIADNEYF RLKVVTFDNV PWVATMKKNE
     HYFPTIEYLK DSEEELGWKK IIHEADAGGA REEIAPAEVE GGGEEMPFLA GLETAALISG
     LALSSGIAIP WITTVERREL RDENAALRAQ GRREISYGKY LWRKIWHGEK LSRVTGGDVE
     SE
//
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