ID A0A2C9UUF3_MANES Unreviewed; 770 AA.
AC A0A2C9UUF3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=MANES_12G067800 {ECO:0000313|EMBL:OAY35046.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY35046.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY35046.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY35046.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CM004398; OAY35046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9UUF3; -.
DR EnsemblPlants; OAY35046; OAY35046; MANES_12G067800.
DR Gramene; OAY35046; OAY35046; MANES_12G067800.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000091857; Chromosome lg12.
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; IPR046450; PA_dom_sf.
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:SF688; SUBTILISIN-LIKE PROTEASE SBT5.3; 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; SSF52025; PA domain; 1.
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:UP000091857};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..770
FT /note="Subtilisin-like protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012790604"
FT DOMAIN 29..114
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 142..598
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 400..474
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 672..768
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 559
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 770 AA; 82572 MW; FAB3BC3C4CF2A540 CRC64;
MRILNHTLFF LSFIFLISLL RPTFASKKSY VVYLGAHSHA HDFTSVDQSL VTDSHYDLLG
SFLGSRELAQ DAIFYSYTRH INGFAATIED EVAAELAKHP KVVSVFLNTG KKLHTTHSWS
FLGLEQNGIV PSNSIWKKAR FGEDIIIGNL DTGVWPESKS FRDEVLGPIP SKWKGICESG
SDPGFHCNRK LIGARYFNKG YASVAGPLNS TFNTPRDKEG HGTHTLSTAG GNFVAGASVF
GLGNGTAKGG SPKSRVAAYK VCYPPVGGNE CFDADILAAF DAAINDGVDV LSLSLGGDPT
PFFNDSVAIG SFHAVKKGIV VVCSAGNSGP ADATVSNLAP WQITVGASTM DREFPSYVTL
GNDMTLKGES LSRKALPKDK YFPIISAADA REANASAEDA LLCKAGTLDP NKAKGKILVC
LRGVNARVEK GEQAALAGAV GMVLANDRDS GNEILADPHV LPVSHVNYAN GVAILAYINS
TKSPIAHITP PISQIGTKPA PFMAAFSSKG PNRIAPEILK PDITAPGVSI IAAYTEAEGP
TNEDFDTRRI QFNSISGTSM SCPHVSGIAG LLKTLHPTWS PAAIKSAIMT SSMTRDNNRE
PILNATHSKA TPLNYGSGHV RPNRAMDPGL VYDLSVNDHL NFLCAMGYNA TQILSFSETP
YSCPSKPINL VNFNYPSIAI PDFNGSVTVT RRVKNVGSGP SSYTARVRKP SGFAISVEPK
VLKFDKVGEE KSFSVTFKSK KSSARKDFVF GELIWSDNKH YVRSPIVVKW
//
