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Database: UniProt
Entry: A0A445BC71_ARAHY
LinkDB: A0A445BC71_ARAHY
Original site: A0A445BC71_ARAHY 
ID   A0A445BC71_ARAHY        Unreviewed;       803 AA.
AC   A0A445BC71;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Subtilisin-like protease SBT5.6 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Ahy_A10g051277 {ECO:0000313|EMBL:RYR36284.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR36284.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR36284.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR36284.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RYR36284.1}.
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DR   EMBL; SDMP01000010; RYR36284.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445BC71; -.
DR   STRING; 3818.A0A445BC71; -.
DR   Proteomes; UP000289738; Chromosome a10.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009610; P:response to symbiotic fungus; IEA:UniProt.
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:SF562; SUBTILISIN-LIKE PROTEASE SBT5.5-RELATED; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
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:UP000289738};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
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..803
FT                   /note="Subtilisin-like protease SBT5.6"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019162265"
FT   DOMAIN          31..112
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          162..648
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          411..502
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          699..800
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   ACT_SITE        171
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        244
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        589
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   803 AA;  87003 MW;  C0099553175E8981 CRC64;
     MILMKNIIFT TCLLLLLSAL ASCTKLTNQI YIVELGGLDE TQTQRELHHD DEEIENVHRS
     YLSSVKESEE EAKASLLYSY RHSMKGFAAL LSREEAKEVS EMEGVVRVHK SKGMMYSLHT
     TRSWEFVGLE GPLNPNWADY EELSSHQKIK NGQDLLCRAN YGQNLIVGMI DSGVWPESKS
     FSDEGMEPVP QKWRGICQNG TAFNSSQCNR KIIGARYYLQ GYESQYGPLN EEEDYKSARD
     KDGHGTHTAS IVAGRAVPSA SAIGGFANGT ASGGAPMARI AIYKACWPIK GQSKHKGNVC
     IDIDLLKAMD DAIGDGVDVL SASIGYKTPI PYKDDVIGTA ALHATKKNIV VVCSAGNNGP
     LPSNLSNIAP WIITVGASTV DRSFVAPIML QGGTIIEGRS ITPVHMPNSF YPLVLASQVE
     LPGLPTNASG FCLDNSLDPK KVKGKIVVCM RGEGENIRKG LEVERSGGVG FILGNNEQLG
     NTLYYAAYFI PSTVVTYQNV LKLIQYINSS SNPIAYILPG TTVLNTRPAP LLASFSSRGP
     NIIDPNILKP DIVAPGVDIL AAWTAEDGPT KVTNLDKRVV KYNILSGTSM ACPHVSAAAI
     LLKAIHPTWT SAAIRSALIT TAGTTDNTGN PLTDTNGDPA TPFAIGAGHF NPVKAADPGL
     VYDASYMDYL LYTCSIGATQ YFQVTYKCPN STSLPEPTDL NHPSIQIHRL NGTKNIKRTV
     TNVGKSTSVY TFTAKSSEEF SITATPNILA FNHVGQKISF NITVTAKMGQ ISNKDGPARY
     YFGWYAWTNK NHVVRSQVAV SFT
//
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