LONM_ASHGO
ID LONM_ASHGO Reviewed; 1058 AA.
AC Q754Q9;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 119.
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 Name=PIM1 {ECO:0000255|HAMAP-Rule:MF_03120}; OrderedLocusNames=AFR013C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 583; 588; 590 AND 612-619.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53384.2; -; Genomic_DNA.
DR RefSeq; NP_985560.2; NM_210914.2.
DR AlphaFoldDB; Q754Q9; -.
DR SMR; Q754Q9; -.
DR STRING; 33169.AAS53384; -.
DR MEROPS; S16.010; -.
DR EnsemblFungi; AAS53384; AAS53384; AGOS_AFR013C.
DR GeneID; 4621799; -.
DR KEGG; ago:AGOS_AFR013C; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; Q754Q9; -.
DR OMA; YVGPPIY; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0000262; C:mitochondrial chromosome; IEA:EnsemblFungi.
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 GO; GO:1901858; P:regulation of mitochondrial DNA metabolic process; IEA:EnsemblFungi.
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 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..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 48..1058
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395771"
FT DOMAIN 158..410
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 844..1030
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 72..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 936
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 979
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 564..571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1058 AA; 116150 MW; 6CBF6637AE54723D CRC64;
MLTRIRNAGV GGNAARRVRL LAGYTGARMA HAAALNSTTG AGGAARAAGA GRRAHSDVHV
WALRQQSGIH RGGQCILKQD REPDQSDDKK VPPRAEEGRD EEAVRDEEAE RQPREEQANR
SSEASSSRGS GGSASSAGGG GRSNPPSEGE VPRKYEELMV LPMSNRPLFP GYYKSVTVYD
PAVIEAICGL LRRNIPYLGA FLLKDRSMDK DSIDSIEEVH RVGVFAQITS VHHGVDVDGR
KAMSMVLYPH RRVQLDELVS TPKLVAEAKE KATDDGLVQA KKEKFRDMSE GGEEEENPTE
FLLETGVTVG NFSDHLDLPV DHSSVMLNAL TSETLNTFKH LSSINATVKQ QLIALSSITT
SLKPNIFESP SLLADFAAAI SVGDPNELQD VLETRDVEQR LEKALVFIKK EVYVAELQQK
IEKETDAKVQ KRYKDQVLTE QMRGIKKEMG VEDAKDKAIA TFRERAEKLK FPEHVKKIFD
EELARLSGLE SAMSEYSVTK NYLDWITSLP WGIASTDQYS ILSARKVLDN DHYGMQDVKD
RILEFIAVGK LKGQIDGKII CLVGPPGVGK TSIGQSISRA LNRTFFRFSV GGMSDVSEIK
GHRRTYIGAL PGRLIHALKR CQTENPLILI DEIDKLGRTG HQGDPASALL ELLDPEQNKT
FLDTYLDFPV DMSKVLFVCT ANTLDTIPRP LLDRMEVIEL SGYVADEKVK IAERHLIPAA
KKSTGLGSAN INLTSDSIVA LLKNYCRESG VRSLKKHIEK IYRKAALKIV QQLSIDDTPK
SAPAETNIEP ENGKPDASAK PLTNNLPAPE PLNIPDSVKI DITPETLVEY LGPPVFTADR
IYEKTPAGVV MGLAYTYLGG CTMYVESVLG QPLSKDSNPS LEHTGQLGDV MKESSRLAYS
FSKMFMSRRF PNNRFFEKAA IHLHCPEGAT PKDGPSAGIT MASSLLSLAM NKPLDPTIAM
TGELTLTGKV LRIGGIKEKT VAAKRSGAKT IIFPKDNMAD WEDLPAHVKE GLIPVAAEWY
DDVFNVLFGS VTEEEGNNVW KDQFDLIERS KATASSSN
