ID A0A0K9NRE6_ZOSMR Unreviewed; 425 AA.
AC A0A0K9NRE6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Eukaryotic aspartyl protease family protein {ECO:0000313|EMBL:KMZ59163.1};
GN ORFNames=ZOSMA_6G00940 {ECO:0000313|EMBL:KMZ59163.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ59163.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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:KMZ59163.1}.
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DR EMBL; LFYR01001803; KMZ59163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NRE6; -.
DR STRING; 29655.A0A0K9NRE6; -.
DR OrthoDB; 335768at2759; -.
DR Proteomes; UP000036987; 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 CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034161; Pepsin-like_plant.
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:SF817; OS07G0592200 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|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454}; Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KMZ59163.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..425
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005526996"
FT DOMAIN 79..416
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 97
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 425 AA; 46703 MW; 0932F05765DF7B15 CRC64;
MMLTVVFFLF LAFPQWEAMS GVEALLNSTA YPSSVTQVLK LPLVLSEKKS LIDRRIRGRV
DVETSSMRLY DDLVTTGYYS TKVYIGTPLQ EFTLIVDTGS AVTYVPCSSC QSCGHHQNPR
FEPKLSATYQ RVPCTGECER CNPGRTQCAY DNQYAEKSSS RGVLGRDVIS FDPDIVGNEV
VFGCGNEESG AIYDQDADGI LGLGRGKVGV MDQLVRMGVV DESFSLCYGG IDVGGGAMFL
GEFPPPASMV FSSSDPQRSP YYNVDLKKIL VSGVALEVDP NVFDGNLGTF IDSGTTLAYL
PQQAFLALRD SVRKELGNPN EIPGLDPNIE EVCFAGYDTE ISGLSSSFPQ LHLVFGNEEK
ISLNPENYLY RHYNIQGAYC LGVLPNGNDK TTLLGEIMFR NTLVKYDLKN SRIGFWKTNC
SKLSI
//
