ID A0A0E0CZH5_9ORYZ Unreviewed; 892 AA.
AC A0A0E0CZH5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI03G13360.2};
RN [1] {ECO:0000313|EnsemblPlants:OMERI03G13360.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI03G13360.2};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI03G13360.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-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; A0A0E0CZH5; -.
DR EnsemblPlants; OMERI03G13360.2; OMERI03G13360.2; OMERI03G13360.
DR Gramene; OMERI03G13360.2; OMERI03G13360.2; OMERI03G13360.
DR HOGENOM; CLU_004109_2_1_1; -.
DR Proteomes; UP000008021; Chromosome 3.
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; 2.30.130.40; LON domain-like; 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; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
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 SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001174};
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:UP000008021};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001174}.
FT DOMAIN 53..321
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 691..892
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 781
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 824
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 345..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 892 AA; 98577 MW; 4ED87433B8A38954 CRC64;
MYFASDSGSS GSAADSDSEA SSAAGAGEEE SEGNRSSSAV APAIVRPEDC HTVIALPLPH
QPLFPGFFMA MSVKDPKLLK ALVENHKRSF PYAGAFLVKN EEDTDSNTVT RSDSKKSIHD
LKGKELLKRL HEIGTLAKIT SIQGDQVLLL GHCRLRITEM VEEDPLTVKV DHLKVSKRLM
LTLELVKREL EITKLQQSIA KAIEEKITGE QRRYLLNEQL KAIKKELGLE TDDKTALSEK
FRKRIESRKE KCPSHILQVI EEELTKLQLL EASSSEFSVT SNYLDWLTVL PWGDYSDENF
DVLRAQRILD EDHYGLTDVK ERILEFIAVG KLRGSSQGKI ICLCGPPGVG KTSIGRSVAR
ALNRKFYRFS VGGLSDIAEI KGHRRTYVGA MPGKMVQCLK SVGTSNPLVL IDEIDKLGRG
YSGDPASALL ELLDPEQNAN FLDHYLDVPI DLSKVLFVCT ANVIEMIPGP LLDRMEIITI
AGYITDEKMH IARDYLEKNT REACGIMPEQ VEVTDSALLA LIENYCREAG VRNLQKQIEK
VYRKIALQLV RQGVSNEPAR EITLVEPSEQ PTGVSIATEV ENKSQRDSLA EDVSVHVIPT
DFSCEKINVV SLTTKSEVDH YEHPKGVSKE TSADDKATPT NTSGKMEANE HTEEVMEALV
DKTVEKVVVD ASNLDNFVGK AVFQPERIYD QTPVGVVMGL AWNAMGGSTL YIETAKVEDG
EKKGALVVTG QLGDVMKESA QIAHTICRSI LHEKEPNNSF FTKSKLHLHV PAGATPKDGP
SAGCTMVTSM LSLAMGKLVK KDLAMTGEVT LTGRILPIGG VKEKTIAARR SGIKTIIFPA
ANRRDFDELA PNIRVERRDE EKRCLDFPKE IKTCGLSSCS KYFKRWRKGM VP
//
