ID A0A177CKQ2_9PLEO Unreviewed; 411 AA.
AC A0A177CKQ2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:OAG07419.1};
GN ORFNames=CC84DRAFT_1087845 {ECO:0000313|EMBL:OAG07419.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG07419.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG07419.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG07419.1,
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 -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; KV441551; OAG07419.1; -; Genomic_DNA.
DR RefSeq; XP_018037784.1; XM_018174220.1.
DR AlphaFoldDB; A0A177CKQ2; -.
DR STRING; 1460663.A0A177CKQ2; -.
DR GeneID; 28757706; -.
DR InParanoid; A0A177CKQ2; -.
DR OrthoDB; 3087283at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:OAG07419.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 1..308
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 311..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 18
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 203
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 31..36
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 237..269
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 411 AA; 41817 MW; 63FEB3AEB46EE65A CRC64;
MAAVTIGSSN EEYHLLLDSA ASNTWVMGQE CTAEACGKHN TFGEGDSGSL KTTTKSFSIT
YGTGSVSGTT ASDTLHIASL STALTFGLAT NVSSEFNAYP MDGILGLGRG TAAELDDSQT
LIEALAAADL IPAKLYGIHL SRAADGTNDG ELNLGEVNSE RFDGDLDWLD GVPNDTGFWE
ISVGDAGVGT SLAGLKGKSA IIDSGTSYVF MPEADALAVH KLIDGYTQSG ETFSVPCSTT
TNLSIKFGDK TYAISSKDWV GGTTSEGMCR SNVFGRQTFG DDQWLLGDVF LKNVYAAFDL
DSGKVGFGTK KDGGSLSSTS TSASTSASSS KTASGSYSTG ASSSGGEETT SAAPILPPGA
SATPTPDPSS SPSSSSVDTS AASNDHTGGS STLAASSLLC IAVIIFTMNV L
//
