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LONM_OSTLU
ID   LONM_OSTLU              Reviewed;         936 AA.
AC   A4S6Y4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Lon protease homolog, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03120};
DE            EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03120};
DE   Flags: Precursor;
GN   ORFNames=OSTLU_41620, OSTLU_52138;
OS   Ostreococcus lucimarinus (strain CCE9901).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Ostreococcus; unclassified Ostreococcus.
OX   NCBI_TaxID=436017;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCE9901;
RX   PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA   Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA   Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA   Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA   Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA   Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA   Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA   Van de Peer Y., Moreau H., Grigoriev I.V.;
RT   "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT   of plankton speciation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
CC   -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC       degradation of misfolded, unassembled or oxidatively damaged
CC       polypeptides as well as certain short-lived regulatory proteins in the
CC       mitochondrial matrix. May also have a chaperone function in the
CC       assembly of inner membrane protein complexes. Participates in the
CC       regulation of mitochondrial gene expression and in the maintenance of
CC       the integrity of the mitochondrial genome. Binds to mitochondrial DNA
CC       in a site-specific manner. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03120};
CC   -!- SUBUNIT: Homohexamer or homoheptamer. Organized in a ring with a
CC       central cavity. {ECO:0000255|HAMAP-Rule:MF_03120}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC       Rule:MF_03120}.
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DR   EMBL; CP000593; ABO99468.1; -; Genomic_DNA.
DR   EMBL; CP000601; ABP01139.1; -; Genomic_DNA.
DR   RefSeq; XP_001421175.1; XM_001421138.1.
DR   RefSeq; XP_001422780.1; XM_001422743.1.
DR   AlphaFoldDB; A4S6Y4; -.
DR   SMR; A4S6Y4; -.
DR   STRING; 436017.A4S6Y4; -.
DR   EnsemblPlants; ABO99468; ABO99468; OSTLU_41620.
DR   EnsemblPlants; ABP01139; ABP01139; OSTLU_52138.
DR   GeneID; 5005054; -.
DR   GeneID; 5006932; -.
DR   Gramene; ABO99468; ABO99468; OSTLU_41620.
DR   Gramene; ABP01139; ABP01139; OSTLU_52138.
DR   KEGG; olu:OSTLU_41620; -.
DR   KEGG; olu:OSTLU_52138; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_1_0_1; -.
DR   OMA; YVGPPIY; -.
DR   OrthoDB; 528132at2759; -.
DR   Proteomes; UP000001568; Chromosome 13.
DR   Proteomes; UP000001568; Chromosome 21.
DR   GO; GO:0005759; C:mitochondrial 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:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0070407; P:oxidation-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.130.40; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_03120; lonm_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; IPR027503; Lonm_euk.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR43718; PTHR43718; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF02190; LON_substr_bdg; 1.
DR   PIRSF; PIRSF001174; Lon_proteas; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00763; lon; 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; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   Protease; Reference proteome; Serine protease; Transit peptide.
FT   TRANSIT         1..40
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   CHAIN           41..936
FT                   /note="Lon protease homolog, mitochondrial"
FT                   /id="PRO_0000395768"
FT   DOMAIN          112..350
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          748..932
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          65..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        838
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   ACT_SITE        881
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   BINDING         507..514
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ   SEQUENCE   936 AA;  101688 MW;  7BCF7680ABE28B8E CRC64;
     MYATRAIARR LERHAARCKG AHVARAVRGA RARTTSAPRA LLDALGAGRG DADAFGTRTR
     RTRNAFVSSV DGDGSTGSTG SSSSSSSSAF GDSASSGGIM VSASHPSSHP QVLAVPLPRR
     PLMPGIIMPV KVTDEKLIAE LEDMRNRGQA YVGAFLQRTD AASSASKGEG EDVFDALSAM
     KRTTTSVGLD GEEMVDEDEV DPADHMHDIG TFAQVHNIVR LPTDSTTGEE SATLLLLGHR
     RLRKLGTMKR DPMVVKVEHL KDEKFDANDD IIKATTNEVV ATIKDLLKTN PLHKETLQYF
     AQNFNDFQDP PKLADLGASM CSADDAQLQH VLELLSVKER LDATLELLKK EVEIGKLQAD
     IGKKVEEKIS GDQRRYFLME QLKSIKKELG MERDDKTALI EKFTKRFEPK RASVPEDTAK
     VIDEELQKLG GLEPSSSEFN VTRNYLEWLT SLPWGVCGDE KLDISHAQEV LDSDHYGLED
     VKDRILEFIA VGQLLGTTQG KIITMVGPPG VGKTSIGQSI AKALGRKFYR FSVGGMSDVA
     EIKGHRRTYV GAMPGKLIQC LKSTGVCNPV VLIDEIDKLG RGYQGDPASA LLELLDPEQN
     GTFLDHYLDV PVDLSKVLFV CTANVLDTIP GPLLDRMEVV RLSGYITDEK VQIARTYLEK
     AAREKSGLSD VDASITDAAM GKLIGDYCRE AGVRNLQKHL EKVYRKIALK VARAKSADEK
     LDSIVVDVDD LVDYVGQPPF ATDRIYDVTP PGVVTGLAWT AMGGSTLYIE CTAIDSGDGK
     GALKTTGQLG DVMKESSTIA HTFTRGFLEL KDPGNKYLAD TSLHVHVPAG ATPKDGPSAG
     ITITTSLLSL AMNKPVKPNL AMTGELTLTG RVLPIGGVKE KTIAARRSGV KTIIFPEGNK
     KDYDELSEDI REGLDAHFVS TYDEVYRQAL DWEASS
 
 
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