ID D7L2E3_ARALL Unreviewed; 776 AA.
AC D7L2E3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 78.
DE RecName: Full=Subtilase family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARALYDRAFT_478841 {ECO:0000313|EMBL:EFH61284.1};
OS Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN [1] {ECO:0000313|Proteomes:UP000008694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX PubMed=21478890; DOI=10.1038/ng.807;
RA Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT change.";
RL Nat. Genet. 43:476-481(2011).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; GL348715; EFH61284.1; -; Genomic_DNA.
DR RefSeq; XP_002885025.1; XM_002884979.1.
DR AlphaFoldDB; D7L2E3; -.
DR STRING; 81972.D7L2E3; -.
DR MEROPS; S08.A44; -.
DR EnsemblPlants; fgenesh2_kg.3__1542__AT3G14240.1; fgenesh2_kg.3__1542__AT3G14240.1; fgenesh2_kg.3__1542__AT3G14240.1.
DR Gramene; fgenesh2_kg.3__1542__AT3G14240.1; fgenesh2_kg.3__1542__AT3G14240.1; fgenesh2_kg.3__1542__AT3G14240.1.
DR eggNOG; ENOG502QTK5; Eukaryota.
DR HOGENOM; CLU_000625_4_3_1; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02120; PA_subtilisin_like; 1.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR PANTHER; PTHR10795:SF542; SUBTILISIN-LIKE PROTEASE SBT1.5; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000008694};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..776
FT /note="Subtilase family protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003101795"
FT DOMAIN 28..104
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 129..600
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 369..459
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 666..770
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 138
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 211
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 550
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 776 AA; 82824 MW; 88605F5B2D202D9C CRC64;
MAFFFFYFFF LLTLSSPSSS SSSSNSLTYI VHVDHEAKPS IFPTHRHWYT SSLASLTSSP
PSIIHTYDTV FHGFSARLTS QDASHLLDHP HVISVIPEQV RHLHTTRSPE FLGLRSTDKA
GLLEESDFGS DLVIGVIDTG IWPERPSFDD RGLGPVPLKW KGQCIASQDF PESACNRKLV
GARFFCGGYE ATNGKMNETT EFRSPRDSDG HGTHTASISA GRYVFPASTL GYARGVAAGM
APKARLAAYK VCWNSGCYDS DILAAFDTAV ADGVDVISLS VGGVVVPYYL DAIAIGAFGA
IDRGIFVSAS AGNGGPGALT VTNVAPWMTT VGAGTIDRDF PANVKLGNGK MIAGVSVYGG
PGLNPGRMYP LVYGGSLIGG DGYSSSLCLE GSLDPNLVKG KIVLCDRGIN SRATKGEIVR
KNGGLGMIIA NGVFDGEGLV ADCHVLPATS VGASGGDEIR RYISESSKAR SSKHPTATIV
FKGTRLGIRP APVVASFSAR GPNPETPEIL KPDVIAPGLN ILAAWPDRIG PSGVPSDNRR
TEFNILSGTS MACPHVSGLA ALLKAAHPDW SPAAIRSALM TTAYRVDNRG DPMMDESTGN
TSSVMDYGSG HVHPTKAMDP GLVYDITPYD YINFLCNSNY TGTNIVTITR RQADCDGARR
AGHVGNLNYP SFSVVFQQYG ESKMSTHFIR TVTNVGDPDS VYEIKIRPPR GTTVTVEPEK
LSFRRVGQKL SFVVRVKTTE VKLSPGATNV QTGHIIWSDG KRNVTSPLVV TLQQPL
//
