ID A0A177CXR9_9PLEO Unreviewed; 455 AA.
AC A0A177CXR9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 25.
DE SubName: Full=Aspergillopepsin A {ECO:0000313|EMBL:OAG12364.1};
GN ORFNames=CC84DRAFT_1078835 {ECO:0000313|EMBL:OAG12364.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG12364.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG12364.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG12364.1,
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; KV441548; OAG12364.1; -; Genomic_DNA.
DR RefSeq; XP_018042729.1; XM_018173813.1.
DR AlphaFoldDB; A0A177CXR9; -.
DR STRING; 1460663.A0A177CXR9; -.
DR GeneID; 28757299; -.
DR InParanoid; A0A177CXR9; -.
DR OrthoDB; 2900143at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 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; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077069}.
FT DOMAIN 107..441
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 67..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 330
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 455 AA; 48779 MW; DF256C8B0107BFB1 CRC64;
MSSFQRIALP RNPVYKANGT KSYLHAMRKY GFHPTKPGPY FQAKQFQPQG KFGRVGGRMR
SHYVLAKRHH HPSSSQGATG GATQPTSGSD GDVGEVPAED IQNDSLYLCE VGIGSPVQKL
YLDFDTGSSD LWVWSTELPS NILSQANKDN QQVAFDSSKS STFKKLSGET WKISYGDSSS
ASGDVGTDTV DLGGLKVEGQ AVELAKELSQ QFAQGNGSGL LGLAFSSINT VSPKPQKTPV
DNIIAQKGAG EQVFTAYLGS WRDSDEADKG ESFYTFGYID SATLTAAGAT ESSINYADVD
NSQGFWQIAS ASATINGKTL SRTSNTSIMD TGTTLCLVDD SLVEEVYAAI PGAKYDQSNQ
GYIFPSSTSA DDLPTITLAI GDAQVEFQKE DLGFADAGNG MLYGSIQSRG SMDMDIYGDA
VLKAMYAVFD MNNGSPRFGF VQRKEETQNT TVPPQ
//
