ID I0Z2J1_COCSC Unreviewed; 860 AA.
AC I0Z2J1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 08-NOV-2023, entry version 47.
DE SubName: Full=Acid protease {ECO:0000313|EMBL:EIE24860.1};
GN ORFNames=COCSUDRAFT_46982 {ECO:0000313|EMBL:EIE24860.1};
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:EIE24860.1, ECO:0000313|Proteomes:UP000007264};
RN [1] {ECO:0000313|EMBL:EIE24860.1, ECO:0000313|Proteomes:UP000007264}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-169 {ECO:0000313|EMBL:EIE24860.1,
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}.
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:EIE24860.1}.
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DR EMBL; AGSI01000005; EIE24860.1; -; Genomic_DNA.
DR RefSeq; XP_005649404.1; XM_005649347.1.
DR AlphaFoldDB; I0Z2J1; -.
DR STRING; 574566.I0Z2J1; -.
DR GeneID; 17042861; -.
DR KEGG; csl:COCSUDRAFT_46982; -.
DR eggNOG; KOG1339; Eukaryota.
DR OrthoDB; 641254at2759; -.
DR Proteomes; UP000007264; 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; NAPSIN-A; 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:0000313|EMBL:EIE24860.1};
KW Protease {ECO:0000313|EMBL:EIE24860.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007264};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..860
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003637515"
FT DOMAIN 46..370
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT REGION 457..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 64
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 254
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 77..82
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 292..329
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 860 AA; 84703 MW; 67F806DB96C40811 CRC64;
MGMGSIWALL LCCCALAQAR QATVKLYRNS GTLDRNEGRR QTNQLLYGQI QLGTPGQDFT
VCFDTGSADL WLPSVSCTTP SCLSHSRFNG QTSTTFRGSG DRFSIDYSQG MVAGQVAIDS
LTLGVPNMTI ADQAFGLTTN STADFHSNTC DGVFGLAFPG LGRLKSGARI RVPAFYNLIK
LGFLDQPLFS IWLASDETKD FTGELNFGGI QSRYFSGPLN QIPVNSRKYW SVGLKGLSVG
NNALSINATS AVFDSGTHFI IASDADARII NGAVQGLQYA QDSNSWKVAG GCSNLDGLPT
INLRMGEFLV PLAPRQYITQ AVGTVNIGCT SVIVGGGPAG KIVLGDVFMR SYYTVYTHNQ
DADQAFVSLA PSSGDATGNG LPQRSIPIGS LEKTPGAATN ITTLIAPATA GGAVPATGSQ
SAPAVPAGSL GARPAAGGAG AAAPAATAGG TPAVVGGTPA TAGGTPPAAT NLNSLPQGAG
SGAPPPAPAD AAPAAAAGDL SALPTASNTS APAQNSTINA LAEAATAGTN ATIPAGAYLV
TKTPTGTILT PIYTNDTATA ANTTALAEGL SSAPRAAVPQ QPPQSPGQVA ASSVASGTAV
PAAQQAPVQQ TPGTGAPAAI SGTGNAQNDY RPAGVTAAPG LMATSPQPSA MAAGTQQQQP
SMTTAQPQSQ TAQSSGLTAV PAPPSPTLYY AVQTANGTQY RPVTQPATTT VPAATAQQSG
PAGPAAVRPV ITSPLVIGSS TAPAPQSAAA AASGPATASS LPAGAAAPAQ AAAADAPSEA
AAAAAAGPAA EGPAGALTRA MADALAPAVA LAQADAVAAG VAAPAAADAA EGAEQPAAAP
TVETPVAAPA LSILQRDVLP
//