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Database: UniProt
Entry: I1NQE8_ORYGL
LinkDB: I1NQE8_ORYGL
Original site: I1NQE8_ORYGL 
ID   I1NQE8_ORYGL            Unreviewed;       522 AA.
AC   I1NQE8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Peptidase A1 domain-containing protein {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:ORGLA01G0208800.1, 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:ORGLA01G0208800.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   AlphaFoldDB; I1NQE8; -.
DR   MEROPS; A01.020; -.
DR   EnsemblPlants; ORGLA01G0208800.1; ORGLA01G0208800.1; ORGLA01G0208800.
DR   Gramene; ORGLA01G0208800.1; ORGLA01G0208800.1; ORGLA01G0208800.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_1_1; -.
DR   OMA; IGELWIL; -.
DR   Proteomes; UP000007306; Unassembled WGS sequence.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06098; phytepsin; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   Gene3D; 1.10.225.10; Saposin-like; 1.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033869; Phytepsin.
DR   InterPro; IPR007856; SapB_1.
DR   InterPro; IPR008138; SapB_2.
DR   InterPro; IPR011001; Saposin-like.
DR   InterPro; IPR008139; SaposinB_dom.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF4; OS01G0663400 PROTEIN; 1.
DR   Pfam; PF00026; Asp; 1.
DR   Pfam; PF05184; SapB_1; 1.
DR   Pfam; PF03489; SapB_2; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF47862; Saposin; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
DR   PROSITE; PS50015; SAP_B; 2.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..522
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003648155"
FT   DOMAIN          98..519
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          328..368
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   DOMAIN          392..433
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        129..135
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        294..298
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   522 AA;  55811 MW;  C5CE32C69FBFB15D CRC64;
     MGTRRVGLLL LVLLAAVLLQ PLLAAAAAEG VVRIALKKRQ VDETGRVGGH LAGEDAQRLL
     ARRHGFLTND AARAASRKAR AEAEGDIVAL KNYLNAQYYG EIAIGTPPQM FTVIFDTGSS
     NLWVPSSKCH LSIACYFHSR YKAGQSSTYK KNGKPASIHY GTGAISGYFS QDSVKVGDVA
     VKNQDFIEAT REPSITFMVA KFDGILGLGF KEISVGNAVP IWYNMVRQGL VVDPVFSFWF
     NRHADEGQGG EIVFGGIDPN HYKGNHTYVP VTRKGYWQFN MGDVLIGGNS TGFCAAGCAA
     IADSGTSLLT GPTAIITQIN EKIGATGVVS QECKAVVSQY GQQILDQLRA ETKPAKVCSS
     VGLCTFDGTH GVSAGIRSVV DDEVGKSSGP FSSAMCNACE TAVVWMHTQL AQNQTQDLVL
     QYIDQLCDRL PSPMGESSVD CSSLASMPDI AFTIGGNKFV LKPEQYILKV GEGTATQCIS
     GFTAMDIPPP RGPLWILGDV FMGAYHTVFD YGNLKVGFAE AA
//
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