ID A0A178DRU3_9PLEO Unreviewed; 680 AA.
AC A0A178DRU3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 26.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:OAL46334.1};
GN ORFNames=IQ07DRAFT_146818 {ECO:0000313|EMBL:OAL46334.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL46334.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL46334.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL46334.1,
RC ECO:0000313|Proteomes:UP000077535};
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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; KV441654; OAL46334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178DRU3; -.
DR STRING; 765867.A0A178DRU3; -.
DR InParanoid; A0A178DRU3; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR PANTHER; PTHR47965:SF101; HYPOTHETICAL ASPARTYL PROTEASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OAL46334.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:OAL46334.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 484..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..445
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 515..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 73542 MW; 690AE566A698989E CRC64;
MRVFGSGGAS AFLLSMRHVR HVDGLVLGTH DTRESQATDV RVRGSEAVSI EKRQEIKKTP
KPISADVSQF WEGNDGPWSS FVLQIGNASQ EVRVLPSTAS TSTWVVIKDP YCDNIPIADC
GASRGKTFQK AASWTYQPVD IGQTSIFELG VEENLLGRTV YGDFGTDVMR LGWPGSGGAT
VAKSIIAGIG DTHFTWLGVI GLNPRPTNFS SANNAPQTSF IQSLKNQGDI PSLSWGYTAG
AQYILDSVFG SLVFGGYDSA RFTIPEKTNP GLTFRFHEDV ARDLLVGVTS ITTSKSTGSS
SESPLLEEGI FAFVDSTVPH MWLPASVCKS FEDAFGLTWD STKELYTLSG EQHSTLLGLN
PSITFTLSPS LTPASDEMTV PIVLPYSAFD LNVSWPFGGG EYSNESAYYF PLKRAANSSQ
YTLGRTFLQE AYLIADYERN NFSIWPAKWD DTTKTEKLVS ISPPTPVDAG GSDSTSKKGL
GTGVIAGIAV GGAAAVIICA LVIFFFVRRR RRVREDETEL QRAQTDTSRG SLPDYQQQHR
ASSEASPTIE LGGTEKHELH EDHRFEAPDG GKFEMDGEGI PHEADGMEKR GLYEMDAGGD
GIGGMHGVSI TVEPPTALSP RPESVMPSPI SEQSTLDSVA AEKAEHSRAE KEAVAANTDE
HDGVRSFFGF IKAFRRSGKS
//