ID A0A087HKV2_ARAAL Unreviewed; 781 AA.
AC A0A087HKV2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Subtilisin-like protease SBT1.2 {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=AALP_Aa1g035200 {ECO:0000313|EMBL:KFK42754.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK42754.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM002869; KFK42754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087HKV2; -.
DR MEROPS; S08.084; -.
DR EnsemblPlants; KFK42754; KFK42754; AALP_AA1G035200.
DR Gramene; KFK42754; KFK42754; AALP_AA1G035200.
DR eggNOG; ENOG502QV3N; Eukaryota.
DR OMA; VQLHPQG; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000029120; Chromosome 1.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:EnsemblPlants.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:EnsemblPlants.
DR GO; GO:0010103; P:stomatal complex morphogenesis; IEA:EnsemblPlants.
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:SF350; SUBTILISIN-LIKE PROTEASE SBT1.2; 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:UP000029120};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..781
FT /note="Subtilisin-like protease SBT1.2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001823443"
FT DOMAIN 32..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 143..615
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 408..469
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 673..776
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 152
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 558
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 781 AA; 84618 MW; BBF0A89417EC64CC CRC64;
MEHQTFFLCI ILLLFVSSSS SSSSLETLQK QTYIIQLHPN TETAKTFTSK FDWHLSFLQE
AVLSVEEEEE SSSRILYSYG SAMEGFAALL TEPEAETLRN LPQVVAVRPD HVLQVQTTYS
YKFLGLDDDG VGNSGLWSKS RFGQGTIIGV LDTGVWPESP SFDDTGMPSV PRKWKGICQE
GENFSSSSCN RKLIGARFFI RGHRVANSPL ESPNMPREYI SARDSTGHGT HTASTVGGSS
VSIANVLGNG AGVARGMAPG AHIAVYKVCW FSGCYSSDIL AAIDVAIQDK VNVLSLSLGG
FPIPLYDDTI AIGTFRAMEQ GISVICAAGN NGPIASSVAN TAPWVSTIGA GTLDRRFPAI
VRLDNGKLLY GESLYPGKGL KKAERELEVI YVTGGEKGSE FCLRGSLPRE KIKGKMVICD
RGVNGRSEKG QAIKEAGGVA MILANTEINQ EEDSIDVHLL PATLIGYTES VLLKAYVNAT
KKPKAKIIFG GTVTGRSRAP EVAQFSARGP SLANPSILKP DIIAPGVNII AAWPQNLGPT
GLPYDSRRVN FTVMSGTSMS CPHVSGITAL IRSTYPNWSP AAIKSALMTT ADMYDRRGKE
IKDGNKPAGL FAIGAGHVNP RKAINPGLVY NIQPVDYITY LCTLGFTRSD ILAITHKNVS
CSGILRKNPG FSLNYPSISV IFKRGKTMEM ITRRVTNVGS PNAIYSVNVK APEGIKVTVK
PKRLVFKHAD QTLSYRVWFV MKKRNRGEKV ASFAQGQLTW VNSRNLIQRV RSPISVTLKN
T
//
