LONM_CANGA
ID LONM_CANGA Reviewed; 1026 AA.
AC Q6FPE6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
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};
GN OrderedLocusNames=CAGL0J04422g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380956; CAG60847.1; -; Genomic_DNA.
DR RefSeq; XP_447898.1; XM_447898.1.
DR AlphaFoldDB; Q6FPE6; -.
DR SMR; Q6FPE6; -.
DR STRING; 5478.XP_447898.1; -.
DR PRIDE; Q6FPE6; -.
DR EnsemblFungi; CAG60847; CAG60847; CAGL0J04422g.
DR GeneID; 2889636; -.
DR KEGG; cgr:CAGL0J04422g; -.
DR CGD; CAL0132864; CAGL0J04422g.
DR VEuPathDB; FungiDB:CAGL0J04422g; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; Q6FPE6; -.
DR OMA; YVGPPIY; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0000262; C:mitochondrial chromosome; IEA:EnsemblFungi.
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:0035694; P:mitochondrial protein catabolic process; IEA:EnsemblFungi.
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 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..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 30..1026
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395776"
FT DOMAIN 62..343
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 815..1001
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 29..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 907
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 950
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 497..504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1026 AA; 114998 MW; 6ECE5E9BA7726BC1 CRC64;
MLGTRVTRAV YTRAPLKLQL RALGLHRRYV HNGSKNDEGS STSTTTNKEE NDKKLPDVYP
QMLALPISRR PLFPGFYKAV VISEPRVMKA ITDMVERQQP YIGAFMLKDS NNDTDIIHDI
SEVHELGVLA QVTSAFPSKD EKTGKETMTA LLYPHKRIKI DQLIPPKDVK IEDIVVEKVV
DNEVASEETK DEETVDKTES ATDKVSEEIT EEIAKAPSTE VTEDPDNYEN PTDFLKDYNV
TLVNVSNLED EPFDIKSPII NALTSEILKV FKEISQLNSM FREQIATFSA SIQSATTNIF
EEPAKLADFA AAVSAGEEEE LQEVLESLNI EQRLEKSLLV LKKELMNAEL QNKISKDVET
KIQKRQKEYY LMEQLKGIKR ELGIDDGRDK LVDTYKKRVE KLNLPENVQK TFDEEITKLA
TLETSMSEFG VIRNYLDWLT SLPWGINSKE QYSIPRARKI LDEDHYGMKD VKDRILEFIA
VGKLLGKVDG KIICFVGPPG VGKTSIGKSI SRALNRQFFR FSVGGMTDVA EIKGHRRTYI
GALPGRIIQA LKKCQTQNPL ILIDEIDKIG HGGIHGDPSA ALLEVLDPEQ NNSFLDNYLD
IPIDLSKVLF VCTANSLDTI PRPLLDRMEV IELTGYVAED KIKIAEQYLV PSAKKTAGLQ
NATVSMDEEA INALMKYYCR ESGVRNLKKH IEKIYRKAAL EVVKKMSIED TEPLVSTSEE
PQLSQTNQNI SSSSAEDSTT DLEDSVNPDT AKEASKPNNS QEGASVEETK KAVKTEEEED
TSMIVPEDIK VEITPEDLKK YVGPPIYTTD RLYETTPPGV IMGLAWTNMG GCSLYVESVL
EQPLHNCKHA NLERTGQLGD VMKESSRLAY SFSKMYLSKK FPENRFFEKA AIHLHCPEGA
TPKDGPSAGV TMATSFLSLA LNKPVDPTVA MTGELTLTGK VLRIGGLREK VVAAKRSGAK
TVIFPKDNLN DWEELPENVK EGMEPLAADW YDDIYKRLFS GVKKSEGNNV WKSEFELIDK
KKKEND
