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Database: UniProt
Entry: W7TV64_9STRA
LinkDB: W7TV64_9STRA
Original site: W7TV64_9STRA 
ID   W7TV64_9STRA            Unreviewed;       830 AA.
AC   W7TV64;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   08-NOV-2023, entry version 39.
DE   SubName: Full=Aspartyl protease family {ECO:0000313|EMBL:EWM27418.1};
GN   ORFNames=Naga_100138g2 {ECO:0000313|EMBL:EWM27418.1};
OS   Nannochloropsis gaditana.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC   Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX   NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM27418.1, ECO:0000313|Proteomes:UP000019335};
RN   [1] {ECO:0000313|EMBL:EWM27418.1, ECO:0000313|Proteomes:UP000019335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-31 {ECO:0000313|EMBL:EWM27418.1,
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:EWM27418.1}.
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DR   EMBL; AZIL01000462; EWM27418.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7TV64; -.
DR   EnsemblProtists; EWM27418; EWM27418; Naga_100138g2.
DR   OrthoDB; 3087283at2759; -.
DR   Proteomes; UP000019335; Chromosome 6.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EWM27418.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019335};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          172..559
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   REGION          125..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          623..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..830
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..649
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        736..751
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        752..774
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        803..817
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        440
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ   SEQUENCE   830 AA;  91839 MW;  293F28E7C68F53D2 CRC64;
     MRPPPHFIPD TPHRRRRSAV FTSVALCFIA PLFYIVCLIS YHMEGQDDVL KFSISNAFAS
     SKPKKESLII KAASSKGGIG IPLVQSKENH RTFSTIIRHA LKPLVPGLMI AASLDEESMS
     VPSSQRRALT RMQSSESPMP VKEEEERSSD DFRRLASGPG GIKLQSISDA QYVGMVGLGT
     PAQYFRVLFD TGSTDVWVPA ANCPSCGPGR RGFHPGASRT YRDVLEKDDD MEDDDGVLPR
     LFEAMYADGI VAGKKGEDTL RIGDVAVEGI KFGQAIYEDG ELTLASWDGV VGLGLGKAGE
     ISKPTVLEAL REQHPDLPFH FSVFLAADDR GLVEESSSEL RLGGYDLDKV GQNASWHFAP
     LILDEGGRAG KSWGWNGEEE ESISIMRQGR WSVGVNGVEV RARNHQQPGR GEILRLEEKK
     ELNGGGTNEA GWGHGIAIVD TGASLFIPPS TEYPRLISLI TQGLHCTVSS TYSSTKTPSS
     GWLPTCYGVS VSDFPDLVVR FQDGPSLPLR AEDYVSCSLS ICILLLQDVA DNPFWVLGEI
     WLEAYYTLFD VANQRLGFAC PREGCAGGSW HGERHAYGPF VWAKLAPFLA ILLGIVGWQC
     WGLIFEVVEF IFLEERRVRS VEGREEEGVE REEEEEEEEE EEEGEEEEGE ASRFWFNLLN
     RHDSRGTQHL EEESGDEEVS FAVLDSRAAR RAVSALTSVP QRGFRWMWGE RDSIWTTSFV
     NRWWPSARRS SQERRSRTMS LVTFQSDSGG ENGGSKDEDE LLRHDGEEGV IFKETMDKGG
     GNGCHGSQRR RGWSLEGLYP RPRGRTSSNS LTVIPASETP NGEEIGKGRS
//
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