ID A0A0M0JFK2_9EUKA Unreviewed; 420 AA.
AC A0A0M0JFK2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE SubName: Full=Aspartic proteinase-like protein 2-like protein {ECO:0000313|EMBL:KOO25369.1};
DE Flags: Fragment;
GN ORFNames=Ctob_007712 {ECO:0000313|EMBL:KOO25369.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO25369.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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:KOO25369.1}.
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DR EMBL; JWZX01002984; KOO25369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0JFK2; -.
DR OrthoDB; 335768at2759; -.
DR Proteomes; UP000037460; 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 Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR13683; ASPARTYL PROTEASES; 1.
DR PANTHER; PTHR13683:SF375; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 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 Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000037460}.
FT DOMAIN 59..402
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 77
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 283
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT NON_TER 420
FT /evidence="ECO:0000313|EMBL:KOO25369.1"
SQ SEQUENCE 420 AA; 45527 MW; E0EA126DBAD4699F CRC64;
MGVILISAPV LELNTTVTPL RFLHADPSGL RGRRQAAHKR RLNPAGLELE GNLNTLGYFS
AEVCVGTPAR SFDLIVDTGS ALTAFPCSDC PHCGEHKHSS VPGARFDPAH STSARTVDCS
QPPPGMHCRS CGSGGTCEYG VSYTEGSSIR GRLVEDSFWF GQAETPSPRN VRATFGCQTY
ESGLFYSQVA DGISGFSQAD TYGPTLFDYM RLATDAPDVF SMCLDETHGA LVLGASVPAA
LHASALWIPY TGGGSYTVPL TDLKIDGRSV GAPASRYFST IVDSGTTFMY LPPDAYRPVR
DHFRSECPWG TCTARVAKGE YPDDYCYTMS AQELDQMSPM TLHFEGGVTL DFGPRQYAYE
LRQGIWCLGV FDNEHNGAVI GAANMRHHEV VFDRGSRRVG FFPSDCAEMH ANRRSSILSG
//
