SBT47_ARATH
ID SBT47_ARATH Reviewed; 703 AA.
AC F4KGD4; Q9FIM7;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Subtilisin-like protease SBT4.7 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 4 member 7 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT4.7 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT4.7 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g58820 {ECO:0000312|Araport:AT5G58820};
GN ORFNames=K19M22.2 {ECO:0000312|EMBL:BAB09627.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16193095; DOI=10.1371/journal.pcbi.0010040;
RA Rautengarten C., Steinhauser D., Bussis D., Stintzi A., Schaller A.,
RA Kopka J., Altmann T.;
RT "Inferring hypotheses on functional relationships of genes: Analysis of the
RT Arabidopsis thaliana subtilase gene family.";
RL PLoS Comput. Biol. 1:E40-E40(2005).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
CC -!- PTM: The C-terminal propeptide is autocleaved.
CC {ECO:0000250|UniProtKB:Q39547}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09627.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016885; BAB09627.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97107.1; -; Genomic_DNA.
DR RefSeq; NP_568888.1; NM_125272.2.
DR AlphaFoldDB; F4KGD4; -.
DR SMR; F4KGD4; -.
DR STRING; 3702.AT5G58820.1; -.
DR MEROPS; S08.A11; -.
DR PaxDb; F4KGD4; -.
DR PRIDE; F4KGD4; -.
DR ProteomicsDB; 232762; -.
DR EnsemblPlants; AT5G58820.1; AT5G58820.1; AT5G58820.
DR GeneID; 835999; -.
DR Gramene; AT5G58820.1; AT5G58820.1; AT5G58820.
DR KEGG; ath:AT5G58820; -.
DR Araport; AT5G58820; -.
DR TAIR; locus:2154503; AT5G58820.
DR eggNOG; ENOG502QRA7; Eukaryota.
DR HOGENOM; CLU_000625_4_3_1; -.
DR InParanoid; F4KGD4; -.
DR OMA; SCTEEQA; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:F4KGD4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KGD4; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
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; PTHR10795; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..107
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435238"
FT CHAIN 108..?
FT /note="Subtilisin-like protease SBT4.7"
FT /evidence="ECO:0000255"
FT /id="PRO_5003315641"
FT PROPEP ?..703
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435239"
FT DOMAIN 29..106
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 111..556
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 350..411
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 194
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 495
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 633
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 703 AA; 75697 MW; DC00289E831C7CD6 CRC64;
MAKRDYFCFV VLFLSSVSAV IDDPQNKQVY VVYMGSLPSL LEYTPLSHHM SILQEVTGDS
SVEGRLVRSY KRSFNGFAAR LTESERIRVA EMEGVVSVFP NINYKLQTTA SWDFLGLKEG
KNTKRNLAIE SDTIIGFIDS GIWPESESFS DKGFGPPPKK WKGVCSGGKN FTCNNKLIGA
RDYTSEGTRD LQGHGTHTAS TAAGNAVADA SFFGIGNGTA RGGVPASRIA AYKVCSEKDC
TAASLLSAFD DAIADGVDLI SISLASEFPQ KYYKDAIAIG AFHANVKGIL TVNSAGNSGS
FPSTTASVAP WILSVAASNT NRGFFTKVVL GNGKTLVGRS VNSFDLKGKK YPLVYGDNFN
ESLVQGKILV SKFPTSSKVA VGSILIDDYQ HYALLSSKPF SLLPPDDFDS LVSYINSTRS
PQGTFLKTEA FFNQTAPTVA SFSSRGPNFI AVDLLKPDIS APGVEILAAY SPLGSPSEEE
SDKRRVKYSV MSGTSMSCPH VAGVAAYIRT FHPKWSPSVI QSAIMTTAWP MKPNRPGFAS
TEFAYGAGHV DQIAAINPGL VYELDKADHI AFLCGLNYTS KTLHLIAGEA VTCSGNTLPR
NLNYPSMSAK IDGYNSSFTV TFKRTVTNLG TPNSTYKSKI VLNHGAKLVK VSPSVLSFKR
VNEKQSFTVT FSGNLNLNLP TSANLIWSDG THNVRSVIVV YTT
