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Database: UniProt
Entry: I1P4U5_ORYGL
LinkDB: I1P4U5_ORYGL
Original site: I1P4U5_ORYGL 
ID   I1P4U5_ORYGL            Unreviewed;       728 AA.
AC   I1P4U5;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
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:ORGLA02G0300100.1, 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:ORGLA02G0300100.1}
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR   AlphaFoldDB; I1P4U5; -.
DR   EnsemblPlants; ORGLA02G0300100.1; ORGLA02G0300100.1; ORGLA02G0300100.
DR   Gramene; ORGLA02G0300100.1; ORGLA02G0300100.1; ORGLA02G0300100.
DR   eggNOG; ENOG502QZDA; Eukaryota.
DR   HOGENOM; CLU_000625_4_6_1; -.
DR   OMA; WTPAMIM; -.
DR   Proteomes; UP000007306; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02120; PA_subtilisin_like; 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; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR045051; SBT.
DR   InterPro; IPR041469; Subtilisin-like_FN3.
DR   PANTHER; PTHR10795:SF406; OS02G0779900 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};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..728
FT                   /note="Subtilisin-like protease"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003649665"
FT   DOMAIN          39..123
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          190..570
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          373..447
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          616..715
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   REGION          189..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   728 AA;  76132 MW;  218F03CDC170CEE8 CRC64;
     MAKPPATTTL VLCCLLAVAA AAAATWIGHD DQQDDDVSTY IVHVMPAHAP RLATHRIARD
     HYAPFLRELL LPPHVARPPP RLLYSYAHAA TGFAARLTAR QAAHLEAHPC VAAVVRDEAY
     ELHTTLSSSF LRLSPSSGLQ AESNSATDAV IAVMNSTMRP SYQTRLCPQH RLLPFVANMF
     YEGYERASGK PINETEDSKS PLDTTGHGTH SAAIAAGSPV SDANLFGLAN GVAKGTAPGA
     RIAVYKVCWK MGCFGSDVVA GMDEAIADGV DVISLSLAVN RKRTFAQDPT AISGFNAVRK
     GIVVVASAGS GGPKESTVTN TAPWLLTVGA SSMNRQFQTI VVLGDGQTFS GTSLYLGDTD
     GSMKSLVFGG FAGSAACEIG KLDATKVAGK IVLCEAGQVL DAEKGVAVAQ AGGFGVIVSS
     RSSYGEYAKA TAHLIPGTTV PNAAALEILR YMARTPYPVG KILFFGTVLS SSPRIASFSA
     RGPSLAAPEI LKPDLVAPGV SILAAWSGLV SPTELDVDTR RVKFNILSGT SAACPHVSGV
     AALLKMARAS WTPAMIMSAL TTTAGLDPGL VYDAGVDDYL DVLCALGYSD EDIVGIFLRD
     GTITNCSTRA STTVADLNRA SISVAVKAYG DDITVRRTVR NVGGSVDAVY TVGGVPPPGT
     QLRIRPSKLV FDAEHQTRTY DVVIRTVSSG SFDEYTHGSI VWSDGAHKVR SPIAVTWPPS
     QSAAVAAI
//
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