ID I1IS64_BRADI Unreviewed; 886 AA.
AC I1IS64;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 82.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000256|HAMAP-Rule:MF_03121};
DE EC=3.4.21.- {ECO:0000256|HAMAP-Rule:MF_03121};
GN Name=100825973 {ECO:0000313|EnsemblPlants:KQJ91185};
GN ORFNames=BRADI_4g36160v3 {ECO:0000313|EMBL:KQJ91185.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQJ91185};
RN [1] {ECO:0000313|EMBL:KQJ91185.1, ECO:0000313|EnsemblPlants:KQJ91185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ91185.1,
RC ECO:0000313|EnsemblPlants:KQJ91185};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ91185.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ91185.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ91185}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ91185};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded and unassembled polypeptides in the
CC peroxisomal matrix. Necessary for type 2 peroxisome targeting signal
CC (PTS2)-containing protein processing and facilitates peroxisome matrix
CC protein import. {ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000256|ARBA:ARBA00004253,
CC ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03121, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR EMBL; CM000883; KQJ91185.1; -; Genomic_DNA.
DR RefSeq; XP_003578503.1; XM_003578455.3.
DR AlphaFoldDB; I1IS64; -.
DR STRING; 15368.I1IS64; -.
DR MEROPS; S16.003; -.
DR EnsemblPlants; KQJ91185; KQJ91185; BRADI_4g36160v3.
DR GeneID; 100825973; -.
DR Gramene; KQJ91185; KQJ91185; BRADI_4g36160v3.
DR KEGG; bdi:100825973; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_2_1; -.
DR InParanoid; I1IS64; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000008810; Chromosome 4.
DR ExpressionAtlas; I1IS64; baseline and differential.
DR GO; GO:0005782; C:peroxisomal matrix; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
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:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR GO; GO:0006625; P:protein targeting to peroxisome; IBA:GO_Central.
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 HAMAP; MF_03121; lonp2_euk; 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; IPR027501; Lonp2_euk.
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; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 2.
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|HAMAP-
KW Rule:MF_03121};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03121, ECO:0000256|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03121,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03121};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03121}.
FT DOMAIN 12..255
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 691..876
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 68..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 884..886
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT ACT_SITE 782
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 825
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 410..417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 886 AA; 97340 MW; 14795697BB8D5E8F CRC64;
MADAPVELPG RLAILPFRNK VLLPGAIVRI RCTNPSSVKL VEQELWQRED KGLIGVLPVR
DSEAASVGSI LSPGVGGDSG EGGSKSPGGS GGESTKQDAK NGKEPIHWHN RGVAARALHL
SRGVEKPSGR VTYTVVLEGL CRFSVQELNA RGSYHVARVS RLDMTKTELE QAEQDPDLIA
LSRQFKATAM ELISVLEQKQ KTVGRTKVLL ETVPIYRLAD IFVASFEISF EEQLSMLDSV
DLKVRLSKAT ELVDRHLQSI LVAEKITQKV EGQLSKSQKE FLLRQQMRAI KEELGDNDDD
EDDVAALERK MQNAGMPANI WKHAQRELRR LRKMQPQQPG YSSSRAYLEL LADLPWQKVS
EEMELDLRAA KESLDHDHYG LTKVKQRIIE YLAVRKLKPD ARGPVLCFVG PPGVGKTSLA
SSIAKALNRK FIRISLGGVK DEADIRGHRR TYIGSMPGRL IDGLKRVSVS NPVMLLDEID
KTGSDVRGDP ASALLEVLDP EQNRTFNDHY LNVPFDLSKV VFVATANRMQ PIPPALLDRM
EVIELPGYTP EEKLKIAMKH LIPRVLEQHG LSTAYLQIPE AVVKLIIERY TREAGVRNLE
RNLAALARAA AVKVAELGST LRLGKEIQPI TTTLLDSRLA DGGEVEMEVI PMGQDISNAY
VNPSPMIVDE AMLEKVLGPP RFDDREAADR VASPGVSVGL VWTSFGGEVQ FVEATAMVGK
GDLHLTGQLG DVIKESAQLA LTWVRARAAD LKLSPTSDIN LLESRDIHIH FPAGAVPKDG
PSAGVTLVTS LVSLFSDRKV RADTAMTGEM TLRGLVLPVG GVKDKVLAAH RYGIKRVILP
ERNLKDLSEI PAPILAGIEI LLVKRIEEVL DHAFESGFPL RPRSSL
//
