LONM_YARLI
ID LONM_YARLI Reviewed; 1177 AA.
AC Q6C0B5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=PIM1 {ECO:0000255|HAMAP-Rule:MF_03120};
GN OrderedLocusNames=YALI0F26169g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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 -!- 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; CR382132; CAG78709.1; -; Genomic_DNA.
DR RefSeq; XP_505897.1; XM_505897.1.
DR AlphaFoldDB; Q6C0B5; -.
DR SMR; Q6C0B5; -.
DR STRING; 4952.CAG78709; -.
DR MEROPS; S16.010; -.
DR EnsemblFungi; CAG78709; CAG78709; YALI0_F26169g.
DR GeneID; 2908111; -.
DR KEGG; yli:YALI0F26169g; -.
DR VEuPathDB; FungiDB:YALI0_F26169g; -.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; Q6C0B5; -.
DR OMA; YVGPPIY; -.
DR Proteomes; UP000001300; Chromosome F.
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; 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.
FT CHAIN 1..1177
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395783"
FT DOMAIN 203..503
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 964..1150
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 72..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1056
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 1099
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 657..664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1177 AA; 129478 MW; 6F99BAF472E47A3A CRC64;
MIDNKVSVCS VGKVVITEVA TFASHPLYID RKTALTMIRS TRAASRLRLG ARYYASHAPY
GVLSEHLKRT PRTNSQHYYP PPQGAHDLPK VSSMGDSIAS IVRGRELWVQ EKDKSDKPEK
SDKPDKTDKT DKDKPEKQDK DKTDKPEKTK VSHTPSSTAS TGAGEAAAPP SAPPSGSGSS
SSSGGGSPPA KKKKSPAQTY PEILAVPISD RPLLPGFHRA LVIRDPNVMK AIDEMITRGE
PYLACFFLKE FSNADVIQDA SEVHDIGVIA EIQIQSQDHK RSTVDASNEP VYVLILYPHK
RVRLNSLKNP PSSGGAVSYA SVSEDVAEDG ELLLTSKDLE GYSEEFLEAR EEAKKAKSGK
TEDSKHDSKV TSKDGKETTE KYDSSTLQES PYSFLSTYDV STAAISLIED KPHDKNNRVI
TTLTNEILNV FKMLRAEDAT LREQLSSVVG DILRTEPAVL QEPGRLADFA AALCAGEGKE
IQAVLTALDL ETRLNRALIL LKREHTNAKL QQKIARDVEN KLNSKHKKFL LTEQMKAIKK
ELGVDDGKEK LVEKFNERAE KLDMPENIQK VFEEEMTRLQ SMEPSSSEYS VTRNYLDWIT
QIPWNKTTED RFNLPQAKDV LDSEHYGMKE VKDRILEFIA VSRMKGGLTG KILLLQGPPG
VGKTSIGKSI AKALNRQFYR FSVGGTNDAS EVKGHRRTYV GAIPGRLVQA LKQTQTENPL
ILIDEIDKLS SSRTQGDPGA ALLEALDPEQ NNAFLDHYLD VPIDLSKVLF VCTSNDLSTI
PWPLLDRMEV IEMSGYVPDE KLNIANQYLV PQSKKETGLE NVNVQVTDDA INALNRQYCR
ESGVRNLKKH IEKIFRKVVV KIVGEYGQDE VAAEKIIDVE PVEKDKESAE KKTTKSKSKE
VNEEPAAKEE KDKATESAES SETKVGTKAP PVTVPEDYSL TIDEKDLYDY VNSPPYSSDR
MFEDPPPGVV MGLAYSPLGG SALYIECILD GGLSADSSAR LSSTGNLGNV MKESTNIAYS
FAKSFMIRNF PANRFFERAG IHLHCPAGAI SKDGPSAGCA VVTGLLSLAL NHPIDSSISM
TGEISLTGKV MKIGGLREKA VGAHSAGAKT IIIPKDNSGD WDELPDTVKE GLTPVFAGTY
QDVYDVVFQG LDTKVAAEVW KKQFDLIDRK LDKRGSK
