ID D7KIE3_ARALL Unreviewed; 774 AA.
AC D7KIE3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Subtilase family protein {ECO:0000313|EMBL:EFH67279.1};
GN ORFNames=ARALYDRAFT_473476 {ECO:0000313|EMBL:EFH67279.1};
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; GL348713; EFH67279.1; -; Genomic_DNA.
DR RefSeq; XP_002891020.1; XM_002890974.1.
DR AlphaFoldDB; D7KIE3; -.
DR STRING; 81972.D7KIE3; -.
DR EnsemblPlants; fgenesh2_kg.1__3430__AT1G32940.1; fgenesh2_kg.1__3430__AT1G32940.1; fgenesh2_kg.1__3430__AT1G32940.1.
DR Gramene; fgenesh2_kg.1__3430__AT1G32940.1; fgenesh2_kg.1__3430__AT1G32940.1; fgenesh2_kg.1__3430__AT1G32940.1.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_4_2_1; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR GO; GO:0009505; C:plant-type cell wall; IEA:EnsemblPlants.
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:SF671; SUBTILISIN-LIKE PROTEASE; 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; 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..774
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003101041"
FT DOMAIN 29..107
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 133..590
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 408..472
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 667..762
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 552
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 774 AA; 82720 MW; 437059E20BE101A5 CRC64;
MRNYRLLLVL VLSLVIALNV VRASDESKVH IVYLGEKQHD DPEFVTESHH QMLSSLLGSK
VDAHDSMVYS YRHGFSGFAA KLTESQAKKL ADSPEVVHVM ADSLYELATT RTWDYLGLSA
ANPNNLLNDT NMGDQVIIGF IDTGVWPESE SFNDNGVGPL PSHWKGGCES GEKFISTNCN
RKLIGAKYFI NGFLAENEGF NTTKSRDYIS ARDFIGHGTH TASIAGGSFV PNISYKGLAG
GNLRGGAPRA RIAIYKACWY VDQLGIVACS SSDILKAMDE AMHDGVDVLS LSLGAQIPLY
PETDLRDRIA TGAFHAVAKG IIVVCAGGNS GPAAQTVLNT APWILTVAAT TLDRSFPTPI
TLGNRKVILG QALYTGQELG FTSLGYPENP GNTNETFSGV CESLNLNPNR TMAGKVVLCF
TTNTLFTAVS RAASYVKAAG GLGVIIARNP GYNLTPCRDN FPCVAIDYEL GTDVLLYIRS
TRSPVVKIQP SRTLVGQPVG TKVATFSSRG PNSISPAILK PDIGAPGVSI LSATSPDSNS
SVGGFDILSG TSMAAPVVAG VVALLKALHP NWSPAAFRSA IVTTAWRTDP FGEQIFAEGS
SRKVADPFDY GGGVVNAEKA AEPGLIYDMG TQDYILYLCS AGYNDSSITQ LVGNVTVCSN
PKPSVLDVNL PSITIPNLKD EVTLTRTVTN VGPVDSVYKV VLDPPLGIRV VVTPETLVFN
SKTKSVSFTV GVSTTHKINT GFYFGNLIWT DSMHNVTIPV SVRTQILQNY YDEN
//
