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LONM_MAIZE
ID   LONM_MAIZE              Reviewed;         964 AA.
AC   P93648;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
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};
GN   Name=LON2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. B73;
RX   PubMed=9620272; DOI=10.1023/a:1005912831051;
RA   Barakat S., Pearce D.A., Sherman F., Rapp W.D.;
RT   "Maize contains a Lon protease gene that can partially complement a yeast
RT   pim1-deletion mutant.";
RL   Plant Mol. Biol. 37:141-154(1998).
RN   [2]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND SUBUNIT.
RA   Mertova J., Almasiova M., Perecko D., Bilka F., Benesova M., Bezakova L.,
RA   Psenak M., Kutejova E.;
RT   "ATP-dependent Lon protease from maize mitochondria - comparison with the
RT   other Lon proteases.";
RL   Biologia 57:739-745(1998).
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       ECO:0000269|Ref.2}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5-9.0. {ECO:0000269|Ref.2};
CC       Temperature dependence:
CC         Optimum temperature is 40-45 degrees Celsius. {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Homoheptamer. Organized in a ring with a central cavity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03120, ECO:0000269|Ref.2}.
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {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; U85495; AAC50021.1; -; mRNA.
DR   PIR; T04325; T04325.
DR   RefSeq; NP_001105895.1; NM_001112425.1.
DR   AlphaFoldDB; P93648; -.
DR   SMR; P93648; -.
DR   STRING; 4577.GRMZM2G113056_P01; -.
DR   PaxDb; P93648; -.
DR   GeneID; 732810; -.
DR   KEGG; zma:732810; -.
DR   MaizeGDB; 136450; -.
DR   eggNOG; KOG2004; Eukaryota.
DR   HOGENOM; CLU_004109_4_3_1; -.
DR   OrthoDB; 528132at2759; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P93648; baseline and differential.
DR   Genevisible; P93648; ZM.
DR   GO; GO:0005759; C:mitochondrial 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; IBA:GO_Central.
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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:UniProtKB-UniRule.
DR   GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central.
DR   GO; GO:0007005; P:mitochondrion organization; IBA:GO_Central.
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; IBA:GO_Central.
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; 2.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   Pfam; PF02190; LON_substr_bdg; 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   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW   Protease; Reference proteome; Serine protease.
FT   CHAIN           1..964
FT                   /note="Lon protease homolog, mitochondrial"
FT                   /id="PRO_0000026740"
FT   DOMAIN          89..298
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          773..957
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   REGION          663..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..719
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..740
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        863
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   ACT_SITE        906
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT   BINDING         455..462
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ   SEQUENCE   964 AA;  105659 MW;  D78A6C6B0F8A6D9E CRC64;
     MLRAAVAAAE ELRSPLLRVI GTLRDGRGSV LLGRRVRFCS NSSASDTEAA VAEAEAKAED
     ASAAEGEADS KASSAIVPTS TNIDDCLSVI ALPLPHRPLF PGFYMPINVK DQKLLQALIE
     NRKRSAPYAG AFLVKDEEGT DPNIVTGSDS AKSIDDLKGK DLLKRLHEVG TLAQITSIQG
     DHVVLLGHRR LRITEMVEED PLTVKVDHLK EKPYNKDDDV MKATSFEVIS TLREVLRTSS
     LWKDHVQTYT QHIGDFNYQR LADFGAAISG ANKLLCQEVL EELDVYKRLK LTLELVKKEM
     EISKLQQSIA KAIEEKISGD QRRYLLNEQL KAIKKELGLE TDDKTALSAK FRERIESKKD
     KCPPHVLQVI EEELTKLQLL EASSSEFSVT RNYLDWLTVL PWGNYSDENF DVHHAQKILD
     EDHYGLSDVK ERILEFIAVG KLRGTSQGKI ICLSGPPGVG KTSIGRSIAR ALNRQFYRFS
     VGGLADVAEI KGHRRTYVGA MPGKMVQCLK SVGTANPLVL IDEIDKLGKG HSGDPASALL
     ELLDPEQNVN FLDHYLDVPI DLSKVLFVCT ANVIEMIPNP LLDRMEIIAI AGYITDEKMH
     IARDYLEKNT RQACGIKPEQ VEVTDTALLA LIENYCREAG VRNLQKQIEK IYRKIALQLV
     RQGVSNEPDH ESVSASVTEE SGNGDNTTTK DEILKDPAVE DASVTNNVTN PASEEANEEN
     LTSEAAKEDS TSKGNKGTDG AADKAIEKVV VDSSNLGDFV GKPVFQAERI YEHTPVGVVM
     GLAWTAMGGS TLYIETKKVE EREGKGALVL TGQLGDVMKE SAQIAHTVGR AVLLEKEPDN
     HFFANSKVHL HVPAGSTPKD GPSAGCTMIT SMLSLAMGKP VKKDLAMTGE VTLTGRILPI
     GGVKEKTIAA RRSAIKTLIF PAANKRDFDE LASNVKEGLE VHFVDTYSEI YDLAFQSDAG
     TETS
 
 
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