ID G4U7H9_NEUT9 Unreviewed; 529 AA.
AC G4U7H9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:EGZ77475.1};
GN ORFNames=NEUTE2DRAFT_146994 {ECO:0000313|EMBL:EGZ77475.1};
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:EGZ77475.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ77475.1, 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; GL890999; EGZ77475.1; -; Genomic_DNA.
DR AlphaFoldDB; G4U7H9; -.
DR MEROPS; A01.015; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_9_3_1; -.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EGZ77475.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..529
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003469373"
FT TRANSMEM 506..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..415
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 437..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 285
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 321..371
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 529 AA; 55948 MW; 675CFABD782F0542 CRC64;
MKSTLATLLA LASVAVAENG VVNFPLNRGV PHFRVGNVRQ NVKRDTYSQA LINNITGGAY
YAEVTVGTPG QKVSVVLDTG SSDLWVVSYK ADLCTDPSIQ RQWGDSCDKT YNPTKSSSYK
VLEEDSFEIR YLDNSTAAGD YITDDLNIGG TTIKSLQMGY ATKTVRGAGI LGVGYSSNVA
STQRYPNLID QFVAQKLITT KAYSLYLNDR RSDTGSILFG GIDKDKFIGD LSILPIYLAK
GQAEPIHFEV EMQSVSLALT KNGKTTKIIS TDPSLSQTST IAILDSGTTL SYLPSKITDQ
IHTKLSVYVD EIWTGLTFID CKYLTSNPDL RLSFTFGANA TISVPVWELV LDLLGETQSE
LPFKMPFKNA CIFGIQSTAG FQEDNFDEDW ALLGETFLRS AYVVYDLTHH QIGIAQANLN
STTTDMVELS GADGGLPSGL TGVKEQQTSN DPSGNAGSGS GSSTDKDGAK ETETVTAGST
AATGTAASGA KETDSAAAGL SARGGAVGAL AVASLTGFLA LVGGAVVAL
//