ID I0YSU0_COCSC Unreviewed; 347 AA.
AC I0YSU0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 08-NOV-2023, entry version 49.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:EIE21459.1};
GN ORFNames=COCSUDRAFT_66898 {ECO:0000313|EMBL:EIE21459.1};
OS Coccomyxa subellipsoidea (strain C-169) (Green microalga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Trebouxiophyceae incertae sedis; Elliptochloris clade; Coccomyxa;
OC Coccomyxa subellipsoidea.
OX NCBI_TaxID=574566 {ECO:0000313|EMBL:EIE21459.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE21459.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE21459.1,
RC ECO:0000313|Proteomes:UP000007264};
RX PubMed=22630137; DOI=10.1186/gb-2012-13-5-r39;
RA Blanc G., Agarkova I., Grimwood J., Kuo A., Brueggeman A., Dunigan D.,
RA Gurnon J., Ladunga I., Lindquist E., Lucas S., Pangilinan J., Proschold T.,
RA Salamov A., Schmutz J., Weeks D., Yamada T., Claverie J.M., Grigoriev I.,
RA Van Etten J., Lomsadze A., Borodovsky M.;
RT "The genome of the polar eukaryotic microalga coccomyxa subellipsoidea
RT reveals traits of cold adaptation.";
RL Genome Biol. 13:R39-R39(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EIE21459.1}.
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DR EMBL; AGSI01000012; EIE21459.1; -; Genomic_DNA.
DR RefSeq; XP_005646003.1; XM_005645946.1.
DR AlphaFoldDB; I0YSU0; -.
DR STRING; 574566.I0YSU0; -.
DR GeneID; 17039443; -.
DR KEGG; csl:COCSUDRAFT_66898; -.
DR eggNOG; KOG1339; Eukaryota.
DR OrthoDB; 641254at2759; -.
DR Proteomes; UP000007264; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
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; IPR001969; Aspartic_peptidase_AS.
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; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EIE21459.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007264}.
FT DOMAIN 3..340
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 21
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 220
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 34..39
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 258..299
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 347 AA; 36750 MW; 10D0EB753017F715 CRC64;
MLYYGEFYLG SPPKQFTGCF DTGSSDTWVP SVACLDPSCQ THDRFNPLQS STFKSSANTD
TPAEAVLQRT SSWGPFMITY GTGQVAGTVA ADTLTVGNIT VKNQGFGLVL RASTDFLDIS
CDGLFGLGFP QISNLQTTPA FFNMLSDGQL DQPLFSLYLN PDVTKEPAGE LEFGSIDTSR
YVGKLTYTPV VEKKYWTVGL SGVTVSGVDV GMEATRVVID SGTSAILLGA NDAASIHKAI
PGMYLDRQSG YWVVKGGCAA VADLPPVTFV IGGTPYAMPP QLWTRPAASE SSTDFSGQCV
SVLIGAGMAS NTILGAPFLR AFYSVYTYDM ASKVAQIGFA QAADGSK
//