UniProt: B9SS30

Database: UniProt
Entry: B9SS30_RICCO

LinkDB:  B9SS30_RICCO 
Original site:  B9SS30_RICCO

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Ontology (9)   
   GO (9)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (21)   
   InterPro (13)   
   Pfam (3)   
   PROSITE (3)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (35)   

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ID   B9SS30_RICCO            Unreviewed;       890 AA.
AC   B9SS30;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 90.
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   ORFNames=RCOM_0520240 {ECO:0000313|EMBL:EEF33621.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
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; EQ974105; EEF33621.1; -; Genomic_DNA.
DR   RefSeq; XP_002528799.1; XM_002528753.2.
DR   AlphaFoldDB; B9SS30; -.
DR   STRING; 3988.B9SS30; -.
DR   MEROPS; S16.003; -.
DR   GeneID; 8263721; -.
DR   KEGG; rcu:8263721; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   InParanoid; B9SS30; -.
DR   OrthoDB; 1103874at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
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:UP000008311};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW   Rule:MF_03121}.
FT   DOMAIN          11..256
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   DOMAIN          695..880
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   MOTIF           888..890
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT   ACT_SITE        786
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   ACT_SITE        829
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   BINDING         411..418
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   890 AA;  98643 MW;  C084C6CF7C0A48AD CRC64;
     MAESVELPGR LAILPFRNKV LLPGAIIRIR CTSPNSVKLV EQELWQREEK GLIGILPVRD
     SAAEETTTSV GPPPVLSQGV GNDSGKIQVN NSDNNLKLDG KSQQEVIRWH NRGVAARALH
     LSRGVEKPSG RVTYIVVLEG LCRFSVQELS KRGMYYTARI SSLEMTKAEM EQVEQDPDFV
     SLSRQFKATA MELISVLEQK QKTDGRTKVL LETVPIHKLA DIFVASFEMS FEEQLSMLDS
     IDLKIRLSKA TELVDRHLQS IRVAEKISQK VEGQLSKSQK EFLLRQQMRA IKEELGDNDD
     DEDDVAALER KMQSAGMPSN IWKHAQRELR RLKKMQPQQP GYNSSRVYLE LLADLPWQKD
     SEEHDLDLKA AKERLDSDHY GLVKVKQRII EYLAVRKLKP DARGPVLCFV GPPGVGKTSL
     ASSIATALGR KFVRLSLGGV KDEADIRGHR RTYIGSMPGR LIDGLKRVGV CNPVMLLDEI
     DKTGSDVRGD PASALLEVLD PEQNKTFNDH YLNVPFDLSK VIFVATANRA QPIPPPLLDR
     MEVIELPGYT PEEKLRIAMR HLIPRVLDQH GLGSEFLQIP EAMVKLVIQR YTREAGVRNL
     ERSLAALARA AAVRLAEQEQ ALPLSKNMHR LASPLLENRL ADGAEVEMEV IPMSDNNHEL
     SNSFRVASAL VVDEAMLEKV LGPPRFDDKE AAERVASPGI SVGLVWTAFG GEVQFVEATA
     MAGKGDLHLT GQLGDVIKES AQIALTWVRA RATDLQFAAA HEINLLEGRD IHIHFPAGAV
     PKDGPSAGVT LVTALVSLFS RKRVRADTAM TGEMTLRGLV LPVGGIKDKI LAAHRYGIKR
     VILPERNLKD LVEVPAAVLG SLEILLAKRM EDVLEQAFEG GCPWRIHSKL
//

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