ID A0A177CQ62_9PLEO Unreviewed; 534 AA.
AC A0A177CQ62;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:OAG09082.1};
GN ORFNames=CC84DRAFT_1142289 {ECO:0000313|EMBL:OAG09082.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG09082.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG09082.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG09082.1,
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; KV441550; OAG09082.1; -; Genomic_DNA.
DR RefSeq; XP_018039447.1; XM_018176359.1.
DR AlphaFoldDB; A0A177CQ62; -.
DR STRING; 1460663.A0A177CQ62; -.
DR GeneID; 28759845; -.
DR InParanoid; A0A177CQ62; -.
DR OrthoDB; 1831139at2759; -.
DR Proteomes; UP000077069; 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; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OAG09082.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:OAG09082.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 412..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..374
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
SQ SEQUENCE 534 AA; 58720 MW; CEB0A40A221DD15D CRC64;
MSSPQPLVFS PSGSWDGNNG NWSTVVVRIG TPEQDFRVLP APITGEILVP DSEACQMSKG
DLPNCGALRG VVNASHSAGF SFNASETWDP LGKFMTNIHC ELGYASGATF GTDNVGLMVQ
NSGGPTLQDQ VVGLLGKSPF FTGFFGLSPK AANFTNYNDP HPSYITTLKN TRRIPSLSYG
YTAGAFYTPG HAFASLTLGG YDESRFEPNL NITFPFHGDD ERPTSIYLQQ IMAENTPNGT
VSILRDKIFV NLDFTLPFLW LPTDACDRIA SLFKLRYDTV HNLYLAEDNV NAELMEKNAQ
FTFDLGDSVH PAERVSIVIP YSAFNHGLSW PIYNSTTKYF PMRRTNGTHY TLGRAFMQEA
YIIVDYERDS FSVHQASQSI SQEQKLVAIS AKDQQEIAQS QRERKTLSSA SIGGITTACI
LGTAAFLALA ILLFRRRSRS HGTSRMSIDG TYTQNEHEGH GGLDRQLMST EVVEIQGPVA
QMLQARHNAE LQETARELPG SGITLNHCGT VFKNEETDGR FELSADREPR GGGR
//