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Database: UniProt
Entry: W7U1R7_9STRA
LinkDB: W7U1R7_9STRA
Original site: W7U1R7_9STRA 
ID   W7U1R7_9STRA            Unreviewed;       759 AA.
AC   W7U1R7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   08-NOV-2023, entry version 40.
DE   SubName: Full=Aspartic proteinase {ECO:0000313|EMBL:EWM26574.1};
GN   ORFNames=Naga_100001g8 {ECO:0000313|EMBL:EWM26574.1};
OS   Nannochloropsis gaditana.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC   Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX   NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM26574.1, ECO:0000313|Proteomes:UP000019335};
RN   [1] {ECO:0000313|EMBL:EWM26574.1, ECO:0000313|Proteomes:UP000019335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-31 {ECO:0000313|EMBL:EWM26574.1,
RC   ECO:0000313|Proteomes:UP000019335};
RX   PubMed=23966634; DOI=10.1093/mp/sst120;
RA   Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA   Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT   "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT   Nannochloropsis gaditana in Nitrogen Depletion.";
RL   Mol. Plant 7:323-335(2014).
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:EWM26574.1}.
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DR   EMBL; AZIL01000609; EWM26574.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7U1R7; -.
DR   EnsemblProtists; EWM26574; EWM26574; Naga_100001g8.
DR   OrthoDB; 3087283at2759; -.
DR   Proteomes; UP000019335; Chromosome 8.
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; 2.
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:UP000019335}.
FT   DOMAIN          41..454
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          500..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          661..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        509..524
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        525..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..560
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        608..622
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..699
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        59
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        308
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   759 AA;  82537 MW;  BF3975BDC156B377 CRC64;
     MKMDVTNVTS RLRSLTALSP TLEPVLPRGH VPLENIQEAE FVGRVYIGSP PRPYTVVFDT
     GSANLWVLSK AGSHVASGKG LYVHDRSSTY QPNGRNMSIK YGSGFVQGFY SNDCIRAGGL
     VVPQMAFGEA TLAMDNEHGT LFSGMQGEGI LGLAFQGISE HAVPTFIDLL YQQKQIEHKI
     FSFYLTRNVR RHGSRMILGG VDMSFAREKE FQYVPLVEEG FWAVGMAGME LKKGEYKGLR
     EAGLGSVRRK GERDNEAIVA EPMRMMTTGA SSRNVSLGNP TQVHTAARAD NGSLVLCGGG
     ASCLAIVDTG TSFLGVPAKT LPVMLEYITQ GQRNCKVQKG KLTVCDCDRS MSGFPDIEIR
     LHADPPVSFS RRQGFKEGRR KGGKEGGEVV TLRLAPEDYL LQFYSDFRYR CAIGLQAVHS
     SLMGKDDDVY ILGTTVLKTY YTVFDGEAMR VGFAYTAEEK QPLSWTGPAF ATLYRLVTLA
     LYMVILVCLV QIFQSSREED VDGPEVGVQD KEEGEEEEGQ VDEEGDKTEA GKVETEERST
     PRSSFLSRVW RPSASSRWSW VGNGEGGRDG AHGTGCMSRP LMQGAPEIAP PNGTTPRGHA
     PHGDSSRTAT AGRERSGEGE GGRDGRGYPG GWAVSPSLSP WKGGDRRSIG QETGQLLRWW
     WSGSAEGESD PTGGWQVGRQ RQEKARPTDR QERHGHVSPF LEGRSSPTCG SHVGGMAGWR
     AGAVDEGVLM GESGHGYSHL ASPHNSPTRR KRGGGTKTL
//
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