LONM_CANDC
ID LONM_CANDC Reviewed; 1073 AA.
AC B9WLN5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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}; ORFNames=CD36_29680;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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; FM992695; CAX39997.1; -; Genomic_DNA.
DR RefSeq; XP_002421996.1; XM_002421951.1.
DR AlphaFoldDB; B9WLN5; -.
DR SMR; B9WLN5; -.
DR STRING; 42374.XP_002421996.1; -.
DR MEROPS; S16.010; -.
DR EnsemblFungi; CAX39997; CAX39997; CD36_29680.
DR GeneID; 8050112; -.
DR KEGG; cdu:CD36_29680; -.
DR CGD; CAL0000159169; Cd36_29680.
DR VEuPathDB; FungiDB:CD36_29680; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000002605; Chromosome R.
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; 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.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Hydrolase; Mitochondrion; Nucleotide-binding;
KW Protease; Serine protease; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 28..1073
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395775"
FT DOMAIN 179..393
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 856..1044
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 69..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 950
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 993
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 543..550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1073 AA; 120378 MW; 086C50EBD91F67A6 CRC64;
MIKASKCNKA RALFLVRTSI PRTFIRNATS AIPTTVKLKD LSSLPPLTKS LPTNLPFLMP
DTLHNLLRFD SKKEKQPSTD KSNDKDKPSR KEKGKDKEKE NEERKDINED EKYDIKEETD
SKPTIDPNNP VSSKSSISSS SGGANNNNNN DDSDGRDDDG SPKDKEFLSP SDAGLHPPFL
AIAMKDRPFL PGATRHLHVT DPEVIKCVNH MINSNIKSPY FVLFHVRDTN SEDAALDVIK
DRDFVHEVGT LCQIIKTTGS EILVYPHYRV KLVDISTPNS RSERIEMEQD NSQTSYLKKF
EVSYAVTQQL KDEPYDEQSI TINAWTRRIK ELYEKLAPKY EQPENKEEIM NNPSMLADFI
ASKVHAKPEQ IQQILESSNV ETKLELSLQL LQVEADADEM RQTALKNIRE RTEKAYAQSL
IKEYTKELLK AAGIGENSKV HKFDERIKHL KMPEEAMKAY KTEKERLGTQ SDMEQNVVER
YLDWLTQIPF GVYTKDSFNV KKAREILDRD HYGLKDVKDR ILEFISVGKI SGNVDGRILC
LAGPPGTGKT SIAKSIAEAL NRKYTRIAVG GVQDVHDVKG HRRTYVASIP GRIVTALTQA
KTSNPLMLID EIDKLDTTSH GGAARAFLEI LDPEQNNSFV DNFIEVKVDL SKVLFVCTAN
YLGSIPAPLR DRMEIIEVNG YTKNDKIEIT KRHLIPAAAK KVGLEEGRVV IPDETILRLI
DKYCRESGLR HIKSLINRIF SKASRKIVEE LEDTDADPHS REIVEESLVA KENESVISDK
AKKDAGSSSI ESNDSNTEAK VSTTTENEKK QEQKQKQDEE IKKLDLPADL KIEVKPETLK
DFVGPEIYIK DRLYETLNPG VATGLAYNTS GDGDALYIES ILTDSISSDL GNAGLHVTGS
LKEVMKESAS IAYSFAKQFM VRQFPDNRFF EAAHIHVHCP GGAIPKDGPS AGIAFTSSLV
SLALNKSLPN DTAMTGEITL TGKVLAIGGL REKSLGAKRA GYTKIIFPKD CEYQLDEIPD
EVKEGLTYIP VEWYSEVFEH LFKGISKEEG NSVWKEEFAK LEEKKKSKKT HTV
