ID A0A0K9NQX2_ZOSMR Unreviewed; 611 AA.
AC A0A0K9NQX2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Eukaryotic aspartyl protease family protein {ECO:0000313|EMBL:KMZ59159.1};
GN ORFNames=ZOSMA_6G00900 {ECO:0000313|EMBL:KMZ59159.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ59159.1, 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:KMZ59159.1}.
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DR EMBL; LFYR01001803; KMZ59159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NQX2; -.
DR STRING; 29655.A0A0K9NQX2; -.
DR OrthoDB; 335768at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
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; 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 PANTHER; PTHR13683; ASPARTYL PROTEASES; 1.
DR PANTHER; PTHR13683:SF817; EUKARYOTIC ASPARTYL PROTEASE FAMILY PROTEIN; 1.
DR Pfam; PF00026; Asp; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:KMZ59159.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..611
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005527153"
FT TRANSMEM 555..577
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..406
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 86
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 611 AA; 68657 MW; CA0FEA1694B2C872 CRC64;
MWSLIIVLLF LISEVLGYQT INPQPSPTIL PLFHSKPNSS RHRRHLDTNN QAQAQMKLSD
DLLTEGYYTT KLFIGTPPQE FALIVDTGST ITYVPCSTCY QCGHHQDPRF YPNNSTTYAG
VKCGNGCICN QKIDQCMYRV DYAEKSSSRG VLGEDVISFG SKTSLKPQRL IFGCENMESG
QLYTQHADGI IGLGSAKLGI MNQLVKKGAI DDSFSLCYGG MDQTGGMMVL GNVPPPKDMV
YSHYTPGRSR LYNVEIKDIL VSGNSLKLDP KMFDTQEGTI LDSGTTFAYL PHAAFTAIKS
AIVKELNSPT QIPGVDPAFQ DVCYSGFESD ASKLSNVFPN IHMVFGKKQE LLISPENYLF
RHSKVHGAYC LGIFASNNDK MTILGGILVR NTLVTYDRKN NRIGFWKTNC SELSTTLSSP
SSPSPVSNGF KDFDYDFTGN FQIGFIKFDM YLNISYLDFT PLVPEFTQFM KDKLQTRSHI
EIMSFIGGEG NNGTLIKWRI SPSPPSAHIS NSTAMAIFYL LTDHSFQIPK KFGSFQLLRW
KLEELPSRTW WKTSMTLVIG VSMIAIVAAL VYLIVYLRKH SHWFKNKFQP HFYQPVEARD
PTHEEQELQQ M
//