ID G4V115_NEUT9 Unreviewed; 537 AA.
AC G4V115;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:EGZ68602.1};
GN ORFNames=NEUTE2DRAFT_118593 {ECO:0000313|EMBL:EGZ68602.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ68602.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ68602.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; GL891269; EGZ68602.1; -; Genomic_DNA.
DR AlphaFoldDB; G4V115; -.
DR MEROPS; A01.082; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_4_1; -.
DR OMA; ANCGEQI; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05474; SAP_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033876; SAP-like.
DR PANTHER; PTHR47966:SF65; ASPARTIC-TYPE ENDOPEPTIDASE; 1.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EGZ68602.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..537
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003469966"
FT DOMAIN 88..408
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 537 AA; 55405 MW; B7EE170D8AA397CC CRC64;
MLPLTTLSLY VSLLSPAAAG VLASPNLPIK LPISPAQGHR SSPSLTSRSS NGNGFVRASV
HAAHGAPPKL RRRQEDEGLK NQNLGTTYTI DIDIGTPPQT VTLILDTGSP DLWVNPQCET
SGQEKYCNSF RQFDYTKSKT IQDTGAADIL KYGKGNVTIE YVTDDVIIGS AKIKSQILGI
GFESIDIPLG ILGLSPSVSP DGQSPYPYLL DSMASQGIIS SRAFSLDLRS IDNPSGAIIF
GGVDLGKFSG SLAKLPMLDP SQTPSGVDRY WIVLSGVGMT YPDGEEVESE EIGVPVFLDS
GGTLSRLPET IFQAIGDSFP GSQYDTESGF YIVDCAVAEQ AGSVDFIFGS STSAKKIRVP
YGDFIWEVQT GVCVVGVLPT DDEPVFGDSF LRAAYVVFDQ DNRNLHLAQA ANCGEQIVEI
GSGQDAVLSS TGKCKDGSAG STKTAGGGGL DVTATRAPTR TAGGSGPAVT NSDFGPGPAG
TRVSTGGIGL PTGTGGGGGS GDGNGNDDDD SAASGLDVGV TAAAVLAGLN MLAVWLL
//