ID M1A1D2_SOLTU Unreviewed; 776 AA.
AC M1A1D2;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Subtilase family protein {ECO:0000313|EnsemblPlants:PGSC0003DMT400012537};
GN Name=102595687 {ECO:0000313|EnsemblPlants:PGSC0003DMT400012537};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400012537, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400012537}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400012537};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR RefSeq; XP_006357406.1; XM_006357344.2.
DR AlphaFoldDB; M1A1D2; -.
DR MEROPS; S08.A28; -.
DR PaxDb; 4113-PGSC0003DMT400012537; -.
DR EnsemblPlants; PGSC0003DMT400012537; PGSC0003DMT400012537; PGSC0003DMG400004891.
DR GeneID; 102595687; -.
DR Gramene; PGSC0003DMT400012537; PGSC0003DMT400012537; PGSC0003DMG400004891.
DR KEGG; sot:102595687; -.
DR eggNOG; ENOG502QZDA; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR InParanoid; M1A1D2; -.
DR OMA; YCYMGSL; -.
DR OrthoDB; 11910at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
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; 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:SF785; SUBTILISIN-LIKE PROTEASE SBT1.4; 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:UP000011115};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..776
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004012334"
FT DOMAIN 32..111
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 135..589
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 375..459
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 662..766
FT /note="Subtilisin-like protease fibronectin type-III"
FT /evidence="ECO:0000259|Pfam:PF17766"
FT REGION 199..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 216
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 545
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 776 AA; 82801 MW; BAA277420D6339E2 CRC64;
MAKISVLSSI FFIISFCLTP VAISVQSDGH ETFIIHVAKS DKPHVFSTHH HWYSSIVRSI
SPPSHHRSKI LYTYERAAVG FSARLTAGQA DQLRRVPGVI SVIPDQVRYL HTTHTPTFLK
LADSFGLWPD SDYADDVIVG VLDTGIWPER PSFSDEGLSP VPAGWKGKCV TGPGFPRSSC
NRKIIGARMF YKGYEASHGP MDESKEAKSP RDTEGHGTHT ASTAAGSLVA NASFYQYAKG
EARGMAIKAR IAAYKICWKD GCFDSDILAA MDQAVADGVH VISLSVGANG YAPHYLHDSI
AIGAFGASEH GVLVSCSAGN SGPGPYTAVN IAPWILTVGA STIDREFPAD VILGDDRVFG
GVSLYSGNPL TDSKFPVVYS GDCGSKYCYP GKLDHKKVAG KIVLCDRGGN ARVEKGSAVK
LAGGVGMILA NLAESGEELV ADSHLLPATM VGQKAGDKIR EYVTSDTSPT ATIVFRGTVI
GNSPAAPRVA AFSSRGPNHL TPEILKPDVI APGVNILAGW TGSTGPTDLA IDPRRVEFNI
ISGTSMSCPH VSGLAALLRR AHSKWTPAAI KSALMTTAYN LDNSGKIFTD LATGEESTPF
VHGSGHVDPN RALDPGLVYD IETSDYVNFL CTIGYDGDDI AVFVRDSSRV NCSERSLATP
GDLNYPSFSV DFTSDSNGVV KYKRVVKNVG GDSNAVYEVK VNAPSAVEVS VSPAKLVFSE
ENNSLSYEIS FTSKRSEDIM VKGIQSAFGS IEWSDGIHSV RSPIAVRWRY QSAVSM
//
