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Database: UniProt
Entry: A0A0E0NU13_ORYRU
LinkDB: A0A0E0NU13_ORYRU
Original site: A0A0E0NU13_ORYRU 
ID   A0A0E0NU13_ORYRU        Unreviewed;       926 AA.
AC   A0A0E0NU13;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Lon protease homolog {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|RuleBase:RU000592};
DE            EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|RuleBase:RU000592};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI03G15210.2, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI03G15210.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family.
CC       {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
CC       ECO:0000256|RuleBase:RU000591}.
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DR   AlphaFoldDB; A0A0E0NU13; -.
DR   EnsemblPlants; ORUFI03G15210.2; ORUFI03G15210.2; ORUFI03G15210.
DR   Gramene; ORUFI03G15210.2; ORUFI03G15210.2; ORUFI03G15210.
DR   HOGENOM; CLU_004109_2_1_1; -.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd19500; RecA-like_Lon; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.5.5270; -; 1.
DR   Gene3D; 1.20.58.1480; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR004815; Lon_bac/euk-typ.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR003111; Lon_prtase_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00763; lon; 1.
DR   PANTHER; PTHR43718; LON PROTEASE; 1.
DR   PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF02190; LON_substr_bdg; 1.
DR   PIRSF; PIRSF001174; Lon_proteas; 3.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR   PROSITE; PS01046; LON_SER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PIRSR:PIRSR001174-
KW   2};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
KW   ProRule:PRU01122};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001174,
KW   ECO:0000256|PIRSR:PIRSR001174-2};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001174};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|PIRNR:PIRNR001174}.
FT   DOMAIN          735..919
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   REGION          64..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          660..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        825
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        868
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01122"
FT   BINDING         384..391
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ   SEQUENCE   926 AA;  101076 MW;  4C34085B7BBD9F4B CRC64;
     MLRAAAATTA GFLPPRLAAE TAPAARVVAA AGAEVRSSPL LRALGVPRGG AGIGSATPGR
     RMYFASGSDS SGSAADSDSE ASSAAGAGEE ESEGNRSSSA VAPAIIRPED CHTDPKLLKA
     LVENHKRSFP YAGAFLVKNE EDTDSNTVTR SDPKKSIHGL KGKELLKHLH EIGTLAKITS
     IQGDQVLLLG HCRLRITEMV EEDPLTVKVD HLKVSKRLML TLELVKRELE ITKLQQSIAK
     TIEEKITGEQ RRYLLNEQLK AIKKELGLET DDKTALSEKF RKRIESRKEK CPSHILQVIE
     EELTKLQLLE ASSSEFSVTS NYLDWLTVLP WGDYSDENFD VFRAQRILDE DHYGLTDVKE
     RILEFIAVGK LRGSSQGKII CLCGPPGVGK TSIGRSVARA LNRKFYRFSV GGLSDIAEIK
     GHRRTYVGAM PGKMVQCLKS VGTSNPLVLI DEIDKLGRGY SGDPASALLE LLDPEQNANF
     LDHYLDVPID LSKVLFVCTA NVIEMIPGPL LDRMEIITIA GYITDEKMHI ARDYLEKNTR
     EACGIMPEQV EVTDSALLAL IENYCREAGV RNLQKQIEKV YRKIALQLVR QGVSNEPARE
     ITLVEPSEQP TGVSIATEVE NKSQRDSLAE DVSVHVIPTD FSCEKINVVS LTTKSEVDHY
     EHPKGVSKET SADDKATPTN TSGKMEANEH TEEVMEALVD EALVDKTVEK VVVDASNLDN
     FVGKAVFQPE RIYDQTPVGV VMGLAWNAMG GSTLYIETAK VEDGEKKGAL VVTGQLGDVM
     KESAQIAHTI CRSILHEKEP NNTFFTKSKL HLHVPAGATP KDGPSAGCTM VTSMLSLAMG
     KLVKKDLAMT GEVTLTGRIL PIGGVKEKTI AARRSGIKTI IFPAANRRDF DELAPNVKEG
     LEVHFVDKYS EIYDLAFPSD SQALAS
//
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