ID A0A078A2X4_STYLE Unreviewed; 508 AA.
AC A0A078A2X4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Eukaryotic aspartyl protease family protein {ECO:0000313|EMBL:CDW76633.1};
GN Name=Contig12589.g13429 {ECO:0000313|EMBL:CDW76633.1};
GN ORFNames=STYLEM_5594 {ECO:0000313|EMBL:CDW76633.1};
OS Stylonychia lemnae (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW76633.1, ECO:0000313|Proteomes:UP000039865};
RN [1] {ECO:0000313|EMBL:CDW76633.1, ECO:0000313|Proteomes:UP000039865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=130c {ECO:0000313|EMBL:CDW76633.1,
RC ECO:0000313|Proteomes:UP000039865};
RA Swart Estienne;
RL Submitted (JUN-2014) 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; CCKQ01005409; CDW76633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078A2X4; -.
DR EnsemblProtists; CDW76633; CDW76633; STYLEM_5594.
DR InParanoid; A0A078A2X4; -.
DR OMA; NARISNH; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000039865; 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 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 SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:CDW76633.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000039865};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..508
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001729133"
FT TRANSMEM 436..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..419
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 107
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 301
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 508 AA; 58679 MW; 2FFC59CF83F65CAC CRC64;
MSSNTLISNK FLIFFAIQIC LGQSQFSFYG IDEELVQQSK IYLKQQQIFS FQIKVIRVRG
TSKSKQLFIL IDIERSFVFD LSYSSQNEYL SQIVIGSENI QNQISFDTTL QNYLYVKSKD
CLNCTYNNPE EPQYDPIAST SHDSEDEHQH IKSSGKYRFN SKTFIDDVSI DQGLQLQAKQ
IKFEVVDTFN DLVLQQFHTN SILGLAPSRL HDENQFIYQL KQKQLIDQKI VSLLIGNDSI
KSTIEIGGYN QSLLLQGDQQ KGYGLHWIKT ISDNQWQFEI QEIYYGGFSF YNSFLTLSIL
DSAQPYIIMP NKTFQVFLGM IKKIDENVKC LDEICKIHRP CESFAKRLDP IRLQLDDFNM
FGIPAQEYLI QDRENSSQCI LGLTTNQYVT QQNTFILGHV FMRLFYTVLD FENNKIGLGL
HLNSGGYVEP VKSYRIYMII LIIIVVLLMV LAALLGFKMY KQRQIKRLAE NEARILKSNS
MNAAAASELS HIHRQSLLEG RSSNLNKY
//
