ID D7MEV0_ARALL Unreviewed; 1745 AA.
AC D7MEV0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Subtilase family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ARALYDRAFT_329472 {ECO:0000313|EMBL:EFH46153.1};
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}.
CC -!- SIMILARITY: Belongs to the phosphosulfolactate synthase family.
CC {ECO:0000256|ARBA:ARBA00010424}.
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DR EMBL; GL348719; EFH46153.1; -; Genomic_DNA.
DR RefSeq; XP_002869894.1; XM_002869848.1.
DR STRING; 81972.D7MEV0; -.
DR MEROPS; S08.A32; -.
DR EnsemblPlants; fgenesh1_pm.C_scaffold_7001699; fgenesh1_pm.C_scaffold_7001699; fgenesh1_pm.C_scaffold_7001699.
DR Gramene; fgenesh1_pm.C_scaffold_7001699; fgenesh1_pm.C_scaffold_7001699; fgenesh1_pm.C_scaffold_7001699.
DR eggNOG; ENOG502QSF0; Eukaryota.
DR HOGENOM; CLU_000625_8_2_1; -.
DR Proteomes; UP000008694; Unassembled WGS sequence.
DR ExpressionAtlas; D7MEV0; baseline.
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; 2.
DR CDD; cd04852; Peptidases_S8_3; 2.
DR Gene3D; 2.60.40.2310; -; 1.
DR Gene3D; 3.50.30.30; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 2.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR003830; ComA_synth.
DR InterPro; IPR036112; ComA_synth_sf.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
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:SF729; (RAPE) HYPOTHETICAL PROTEIN; 1.
DR PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR Pfam; PF02679; ComA; 1.
DR Pfam; PF17766; fn3_6; 2.
DR Pfam; PF05922; Inhibitor_I9; 2.
DR Pfam; PF00082; Peptidase_S8; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF102110; (2r)-phospho-3-sulfolactate synthase ComA; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 2.
DR PROSITE; PS51892; SUBTILASE; 2.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 2.
PE 3: Inferred from homology;
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}.
FT DOMAIN 365..440
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 470..902
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 981..1048
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT DOMAIN 1045..1123
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 1148..1566
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 1643..1738
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 317..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 479
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 553
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 864
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1157
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1232
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1528
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1745 AA; 189665 MW; 0B6870669AA803D8 CRC64;
MAAYYRWKSF EENEDRPEKP RRYGVTEMRG PHYSVLSQNL LQEIFESMGQ FVDGLKFSGG
SNSLIPKSFI KQAIEMAHEH GVYVSTGDWA EHMLRSGPSA FKDYVEECKQ LGFDTIELNA
NSLEVPEETL LRYVRLIKNG GLRAKPMFAV KFNKSDIPGR NRAFGSYVVP EPRSSEFVED
IDLLIRKAER CLEAGADTIM IDADDVCKYP DSLRADIIAK VIGRLGIEKT MFEASDGKLA
EWFIKRYGPN VFADTPLYYF YLLFEWSPSQ DSCLFVLVFQ VNLYVDHSQI MDLECLRGRH
LAFGFVFIMN GKLSSGTTPH EADPPQASNL AFSPEAAPPD TSAMDDDSDI NYEPVPPFVP
EFPVFIFYLG ERKHDDPNLV TQSHLEILKS VLGSEEAANK SLVYSYHHGF SGFAAKLKPA
EAEKLKKHPE VIILLENRKL GLQTTRTWDY LGQFSTPTSS KGLLHETNMG SGAIIGVIDS
GIWSESGAFD DDGYGPIPKQ WKGQCVSADQ FSPADCNKKL IGAKYYIDGL NADLETSINS
TIEYLSPRDR NGHGTQVSST VAGSFVSNVT LPGLSSGSIM RGGAPKAHIA MYKACWDVEG
GMCSVADVWK AFDEAIHDGV DILSVSIGGS ALKSLDVEID IAIPALHAVN KGIPVVSPAG
NGGSRYSSVI NISPWILTVA ATTLDRSFPT LITLENNKTF LGQSLYTGPE ISFTVLICTA
DHSNLDQITK GKVIMHFSMG PTPPMTPDIV QKNGGIGLID VTSPSDSRVE CPANFPCIYL
DLEVGSELYT YIQTTSSLKI KISPYKTIIG ERVASKVAKS SARGPSSFSP AILKPDIAAP
GVTLLTPRIP TDEDTSEFTY SGTSMATPVI AGIVALLKIS HPNWSPAAIK SALVTTAMKT
DPYGERLTVD GGNYKVADAF DYGGGLVNLE KATDPGLVYD MDINDYIHYL CSQALYTDKK
VSALTGNITS KCPSSCSSIL DLNVPSITIP DLKRDVTVTR TVTNVGPVKS VYKPVIETPL
GFKVVVSPKK LKFNKRRNKV AFKIYIVHLG VRQHDDSELV SESHQRMLES VFESEEAARD
SIVYNYHHGF SGFAARLTDS QAKQLSDRPD VFSVTPNRKV QLQSTRVYDY LGLPPSFPSG
ILHESNMGSD LVIGFLDSGV WPESPAFNDE GLGPIPKHWK GKCVAGEGFD PAKHCNKKLV
GAKYFTDDWD EKNPGNPITD DEFMSPRGLI GHGTMVSSIA ASSFVPNASY GGLAPGLMRG
GAPKARIAMY KVVWDSVTMG STTANMVKAF DEAINDGVDV LSISLASVAP FRPIDAITED
LELGSFHAVT KGIPVIAGAS NTGPDAYTVA NGAPWLLTVA ATNVDRTFYA DMTFGNNITI
MGQAQHTGKE VSAGLVYIED YKNDISSVPG KVVLTFVKED WEMTSALAAT STNNAAGLIV
ARSGDHQSDI VYSQPFIYVD YEVGAKILRY IRSSSSPTVK ISTGKTLVGR PIATQVCGFS
SRGPNIISPA ILKVLSLNNV SKSCTGTSYA TPVVAGLVVL LKALHPDWSP AALKSAIMTT
AWKTDPSGEP IFAEGEPRKL ADPFDYGAGL VNAERAKDPG LVYDMNLDDY IHYFCATGYN
DTAITLITGK PTKCSSPLPS VLDLNYPAIT IPDLEEEVTV TRTVTNVGPV DSVYRAVVEP
PRGVKIVVEP ETLVFCSNTK KLEFKVRVSS SHKSNTGFIF GSFTWTDGTR NVTIPLSVRT
RVLNP
//
