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Database: UniProt
Entry: A0A3B6LQZ9_WHEAT
LinkDB: A0A3B6LQZ9_WHEAT
Original site: A0A3B6LQZ9_WHEAT 
ID   A0A3B6LQZ9_WHEAT        Unreviewed;       869 AA.
AC   A0A3B6LQZ9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5B02G322000.1};
RN   [1] {ECO:0000313|EnsemblPlants:TraesCS5B02G322000.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS5B02G322000.1};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS5B02G322000.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-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   AlphaFoldDB; A0A3B6LQZ9; -.
DR   PaxDb; 4565-Traes_5AL_FBB4F76B8-2; -.
DR   EnsemblPlants; TraesCS5B02G322000.1; TraesCS5B02G322000.1; TraesCS5B02G322000.
DR   Gramene; TraesCS5B02G322000.1; TraesCS5B02G322000.1; TraesCS5B02G322000.
DR   Gramene; TraesCS5B03G0812900.1; TraesCS5B03G0812900.1.CDS; TraesCS5B03G0812900.
DR   Gramene; TraesWEE_scaffold_116683_01G000200.1; TraesWEE_scaffold_116683_01G000200.1; TraesWEE_scaffold_116683_01G000200.
DR   OMA; KKMNPVM; -.
DR   Proteomes; UP000019116; Chromosome 5B.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
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:UP000019116};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW   Rule:MF_03121}.
FT   DOMAIN          1..238
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   DOMAIN          674..859
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   REGION          53..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           867..869
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT   ACT_SITE        765
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   ACT_SITE        808
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   BINDING         393..400
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   869 AA;  95757 MW;  73A5E953440472C7 CRC64;
     MADQFSLQLP TSRSVFESSS VKLVEQELWQ REDKGLIGVL PVRDSEAAAV GSILSPGVGS
     DSGEGGRRSP GGSGGESTKQ DAKSGKEPIH WHSRGVAARA LHLSRGVEKP SGRVTYIVVL
     EGLCRFSVEE LNARGSYHVA RVSRLDMTKT ELEQAEQDPD LIALSRQFKA TAMELISVLE
     QKQKTVGRTK VLLETVPVYR LADIFVASFE ISFEEQLAML DSVDLKVRLS KATELVDRHL
     QSILVAEKIT QKVEGQLSKS QKEFLLRQQM RAIKDELGDN DDDEDDIAAL ERKMQNAGMP
     ANIWKHAQRE LRRLRKMQPQ QPGYSSSRAY LELIADLPWQ KVSEERELDL RAAKESLDRD
     HYGLTKVKQR IIEYLAVRKL KPDARGPVLC FVGPPGVGKT SLATSIAKAL NRKFIRISLG
     GVKDEADIRG HRRTYIGSMP GRLIDGLKRV SVNNPVMLLD EIDKTGSDVR GDPASALLEV
     LDPEQNKTFN DHYLNVPFDL SKVVFVATAN RMQPIPPALL DRMEVIELPG YTPEEKLKIA
     MKHLLPRVLE QHGLSSAYLQ IPEAVVKLII ERYTREAGVR NLERNLAALA RAAAVKVAEL
     DSTLRLGKEM QPITTTLLDS RLADGGEVEM EVIPMGQDIS NTYENPSPMI VDEAMLEKVL
     GPPRFDDREA ADRVSSPGVS VGLVWTSFGG EVQFVEATAM VGKGDLHLTG QLGDVIKESA
     QLALTWVRAR SADLNLSPTS DINILESRDI HIHFPAGAVP KDGPSAGVTL VTSLVSLFSN
     RKVRADTAMT GEMTLRGLVL PVGGVKDKVL AAHRYGIKRV ILPERNLKDL AEIPAPILAG
     IEILLVKRIE EVLGHAFENG FPLRLHSSL
//
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