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Database: UniProt
Entry: A0A0E0BHG9_9ORYZ
LinkDB: A0A0E0BHG9_9ORYZ
Original site: A0A0E0BHG9_9ORYZ 
ID   A0A0E0BHG9_9ORYZ        Unreviewed;      1396 AA.
AC   A0A0E0BHG9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM11G08530.2};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM11G08530.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM11G08530.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-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   MEROPS; S08.A22; -.
DR   EnsemblPlants; OGLUM11G08530.2; OGLUM11G08530.2; OGLUM11G08530.
DR   Gramene; OGLUM11G08530.2; OGLUM11G08530.2; OGLUM11G08530.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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   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; IPR025315; DUF4220.
DR   InterPro; IPR007658; DUF594.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
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:SF821; PEPTIDASE_S8 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR10795; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN; 1.
DR   Pfam; PF13968; DUF4220; 2.
DR   Pfam; PF04578; DUF594; 1.
DR   Pfam; PF17766; fn3_6; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1396
FT                   /note="Peptidase S8/S53 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002354711"
FT   TRANSMEM        828..847
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1008..1028
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1040..1061
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..115
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          144..584
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          649..745
FT                   /note="Subtilisin-like protease fibronectin type-III"
FT                   /evidence="ECO:0000259|Pfam:PF17766"
FT   DOMAIN          828..902
FT                   /note="DUF4220"
FT                   /evidence="ECO:0000259|Pfam:PF13968"
FT   DOMAIN          903..1110
FT                   /note="DUF4220"
FT                   /evidence="ECO:0000259|Pfam:PF13968"
FT   ACT_SITE        153
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        224
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        542
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1396 AA;  153906 MW;  306AAA484C450C74 CRC64;
     MGFFGFGSAP TACALIFAVI LALHGPCFAL PEAPGEAKEL YIVYLGERQH EDADLVTASH
     HTMLATVLGS EELASESIVY SYKHGFSGFS AMLTESQARN IRGLPGVANV WMNQMHNVVT
     TRSWDFMGLP YNQTNGLLAH AKMGDGIIIG VIDSGIWPES PSFDDTGYAP PAAKWKGICQ
     SGMSFTAKSC NRKIIGARWY ADDFNKSQLE AAGEFLSPRD FDGHGTHVAS TAAGSVVRNV
     SFYGLASGVA QGGAPKAHIA VYKACWSIGC SEATIFKAID DAIHDGVDIL SLSILSPTGH
     APAFHAVVKG IPVIYAAGND GPYTQTVNSV APWLLTVAAS TMDRLFPTVV TLGDGQTLVG
     QSLFVAARKA NQFHKLKLYY NDMCNLTIAN STDVKGNIIL CSNLNAIFTT TQLVELATAL
     VKSGGKGFIF TQRSSDRLAT WQFQALTIPI VSVDLEVAFR IHQYFSTTQS PLVKVSPSQT
     TTGRGIPAPK MAAFSSRGPS FIYPTVLKPD IAAPGVNILA AVPPVGKYKK LGLPYFFNSG
     TSMACPHVSG IVALLKSLHP DWSPAALKSA IMTTAHITDN NGLPLVADAT PNKIADPFDY
     GAGFVNPTKA SDPGLIYDID PSDYQMLFNC MIGSNTNRSC TAIESSLFDL NLPSIAIPNL
     KTSQTISRTV TNVGQPDAMY KAFLQPPAGV DMLVKPKMLV FDKNTRSQCF KVTFKARQKF
     QGDYTFGSLA WHDGSSHWVR IPIAIRVVIE DFYSTKVVQF NILRKLFLPQ SYRIKSKELM
     GAPCGGADSA DQVSSSPAAA SEVGAPLLIG SLFFSLLSIN MLLRLIIWLA YVGADMVAVY
     ALGLISQNVQ SANISSVGFS RSSNQLAFFW VPFLLIHLGG QDTMTAFSIE DNNLWLRHLL
     NLYGERTWAL KCGSRNGLRE TSWQLPKLNV EVDKGSYIDT ICYVLQSILC VHDLFSGRTI
     SQMKERQVFR FQGDRPLEQV PKLLEIELAM MSDDLYTKAM VLQTRSGIIL RFISHVFMIA
     AFVLFLIASN KQQYKRVDIA ITYVLFIGGF VLDVCSFFLV AMSPWTWAFF RAQNCNRLAH
     ISWLILCSCI GWPEKKPLWS SSMGQYNFLS SSIGFDESRS SSKMFTILRK MLNAVNKKLW
     FRKIWHIKHV KVDKDIMDIM VTWVGRLARE EFTRITQQQS WANLRPIINC TLNIPANSFG
     DNIVLLHIYT DLHLRKQPDN EAIGAESETA SSSTADIMDI CRKISNYIVY LLVAQPSMLP
     LSGAADDTTA AFHEKISKKG SSKQDVLETC YQLVEDQLEF GYEECLKEQE QPGPWRETLM
     EIRDMWLRLL IYIAGKCQVE LHAQQLGRGG ELLTFVWLLM AHHDIGDVAH QVDLITSSET
     MSGQFCAFHF PKEPEQ
//
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