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Database: UniProt
Entry: I1PLC6_ORYGL
LinkDB: I1PLC6_ORYGL
Original site: I1PLC6_ORYGL 
ID   I1PLC6_ORYGL            Unreviewed;       777 AA.
AC   I1PLC6;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Subtilisin-like protease {ECO:0008006|Google:ProtNLM};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA04G0099500.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|Proteomes:UP000007306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA04G0099500.1}
RP   IDENTIFICATION.
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   AlphaFoldDB; I1PLC6; -.
DR   SMR; I1PLC6; -.
DR   STRING; 4538.I1PLC6; -.
DR   EnsemblPlants; ORGLA04G0099500.1; ORGLA04G0099500.1; ORGLA04G0099500.
DR   Gramene; ORGLA04G0099500.1; ORGLA04G0099500.1; ORGLA04G0099500.
DR   eggNOG; ENOG502QTDB; Eukaryota.
DR   HOGENOM; CLU_000625_4_6_1; -.
DR   OMA; HGNRSKQ; -.
DR   Proteomes; UP000007306; 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; 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:SF597; OS04G0430700 PROTEIN; 1.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..777
FT                   /note="Subtilisin-like protease"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003649081"
FT   DOMAIN          30..111
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          134..589
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          389..462
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          667..772
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
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        549
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   777 AA;  80599 MW;  A604EB226F48D5B4 CRC64;
     MMAWRSLSLV AFMAAVAAAA AAAGDDRRPY VVRMDVSAMP APFATHDGWY RSVLSSASAR
     DAAAAPAAEH LYTYSHAMNG FSAVLTARQV EEIRRADGHV AVFPETYARL HTTRTPAFLG
     LSAGAGAWPA SRYGADVVVG IVDTGVWPES ASFSDAGVAA PVPARWKGAC EAGASFRPSM
     CNRKLVGARS FSKGLRQRGL NISDDDYDSP RDYYGHGSHT SSTAAGAAVP GASYFGYANG
     TATGVAPMAR VAMYKAVFSA DTLESASTDV LAAMDQAIAD GVDVMSLSLG FPESPYDTNV
     VAIGAFAAVR RGILVTCSAG NDGSDSYTVL NGAPWITTVG ASTIDRAFTA TVTLGAGAGG
     ARSIVGRSVY PGRVPAGAAA LYYGRGNRTK ERCESGSLSR KDVRGKYVFC NAGEGGIHEQ
     MYEVQSNGGR GVIAASNMKE IMDPSDYVTP VVLVTPSDGA AIQRYATAAA APRASVRFAG
     TELGVKPAPA VAYFSSRGPS PVSPAILKPD VVAPGVDILA AWVPNKEVME LDGGETKLYT
     NYMLVSGTSM ASPHVAGVAA LLRSAHPDWS PAAVRSAMMT TAYVKDNADD ADLVSMPGGS
     PGTPLDYGSG HVSPNQATDP GLVYDITADD YVAFLCGELR YTSRQVAAIA GHRAGCPAGA
     GAASHRDLNY PSFMVILNKT NSATRTFTRT LTNVAGSPAK YAVSVTAPAG MAVKVTPATL
     SFAGKGSTQG FSVTVQVSQV KRSRDGDNYI GNYGFLSWNE VGGQHVVRSP IVSAFAQ
//
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