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Database: UniProt
Entry: A0A0K9NQX2_ZOSMR
LinkDB: A0A0K9NQX2_ZOSMR
Original site: A0A0K9NQX2_ZOSMR 
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
//
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