ID A0A0K9Q0R6_ZOSMR Unreviewed; 515 AA.
AC A0A0K9Q0R6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative Aspartic proteinase {ECO:0000313|EMBL:KMZ74749.1};
GN ORFNames=ZOSMA_122G00190 {ECO:0000313|EMBL:KMZ74749.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ74749.1, 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:KMZ74749.1}.
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DR EMBL; LFYR01000244; KMZ74749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9Q0R6; -.
DR STRING; 29655.A0A0K9Q0R6; -.
DR OMA; HDEMCRV; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd06098; phytepsin; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR Gene3D; 1.10.225.10; Saposin-like; 1.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033869; Phytepsin.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF47862; Saposin; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS50015; SAP_B; 2.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..515
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005528448"
FT DOMAIN 96..512
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 326..366
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DOMAIN 385..426
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT ACT_SITE 114
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 301
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 127..133
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 515 AA; 56262 MW; 10E51157949F7DF9 CRC64;
MPIMYEMNRM TLVASFVLSL VLLALVLPVS AEGLFKIKLK KKPLEQNNQV SMRFLPKNRH
SQWPYARNYG LNGILRGDGE GEVDIVSLKN YLNAQYFGEI GIGTPPQNFT VIFDTGSSNL
WVPSTKCYLS LACYFHSRYK SSKSSTYNKN GTSAAIKYGT GAISGFFSKD SVEIGDLIVK
NQDFIEATRE PSLTFLLAKF DGILGLGFQE ISIGKAVPVW YNMVDQNLVK EPIFSFWFNR
NANEGIGGEI VFGGVDPDHY KGEHTYVPVS HKGYWQFDMG DVLIGKQSSG FCSEVCSAIA
DSGTSLIAGP TATVTEINYA IGAAGVVSEE CKTIVAEYGE MIFQFLVSET QPSKICSEIG
LCEFNGIQGV GIGIESVVDG TGLRSDVMCN VCEMSVVWIR NQLIQNRTQE SILNYVNELC
ERLPSPMGES AVDCSNLASM PTVSFTIGGK IFPLKPEEYV LKIGEGGAAQ CISGFTAMDV
PPPLGPLWIL GDVFMGPYHT VFDYGNLKVG FAEAM
//
