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Database: UniProt
Entry: I0Z2J1_COCSC
LinkDB: I0Z2J1_COCSC
Original site: I0Z2J1_COCSC 
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
//
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