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
//