LONM_CANAL
ID LONM_CANAL Reviewed; 1078 AA.
AC Q5A6N1; A0A1D8PSQ5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=CAALFM_CR04340WA; ORFNames=CaO19.522;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017630; AOW31171.1; -; Genomic_DNA.
DR RefSeq; XP_717385.1; XM_712292.1.
DR AlphaFoldDB; Q5A6N1; -.
DR SMR; Q5A6N1; -.
DR STRING; 237561.Q5A6N1; -.
DR MEROPS; S16.010; -.
DR PRIDE; Q5A6N1; -.
DR GeneID; 3640999; -.
DR KEGG; cal:CAALFM_CR04340WA; -.
DR CGD; CAL0000197537; PIM1.
DR VEuPathDB; FungiDB:CR_04340W_A; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_1_0_1; -.
DR InParanoid; Q5A6N1; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000000559; Chromosome R.
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; 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; Reference proteome; Serine protease; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT CHAIN 28..1078
FT /note="Lon protease homolog, mitochondrial"
FT /id="PRO_0000395774"
FT DOMAIN 184..398
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 861..1049
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 71..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 955
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT ACT_SITE 998
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
FT BINDING 548..555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03120"
SQ SEQUENCE 1078 AA; 120913 MW; 5DF978CFF3842A9C CRC64;
MIKASKCNKP RALFLVRVSI PRTFIRNATS AVPTTIKLND LASLPPITKS LPTNLPFLMP
DTLQSLLRFD SEKEKQPSTD KSNDKDKPSR KEKGKDKEKE NEEKKDINMD EKYEINEETD
TKPTIDPNNP VSSKSNISSS SGGDNNNNNN NNNNNNDSDG KNDDGSPKDK EFLSPSDSGL
HPPFLAIAMK DRPFLPGATR HLHVSDPEVI KCVNHMINSN IKSPYFVLFH VRDTNSEDAA
LDVIKDRDFV HEVGTLCQII KTTGSEILVY PHYRVKLVDI STPNSRSESI EKEQDNSQTS
YLKKFEVSYA VTQQLKDEPY DEQSITINAW TRRIKELYEK LAPKYDQPEN KEEIMSNPSM
LADFIASKVH AKPEQIQEIL ESSNVETKLE LSLQLLQVEA DADEMRQTAL KNIRERTEKA
YAQSLIKEYT KELLKAAGIG ENSKVHKFDE RIKHLKMPEE AMKAYKTEKE RLGTQSDMEQ
NVVERYLDWL TQIPFGVYTK DSFNVKKARE ILDRDHYGLK DVKDRILEFI SVGKISGNVD
GKILCLAGPP GTGKTSIAKS IAEALNRKYT RIAVGGVQDV HDVKGHRRTY VASIPGRIVT
ALTQAKTSNP LMLIDEIDKL DTTSHGGAAR AFLEILDPEQ NNSFVDNFIE VKVDLSKVLF
VCTANYLGSI PGPLRDRMEI IEVNGYTKND KIEITKRHLI PAAAKKVGLD EGRVVIPDET
ISRLIDKYCR ESGLRHIKSL INRIFSKASR KIVEELEETD VDSHNKDTVE GTLVAKESEK
VISDKAKIDT ENSPIEYIQS NTEVKAETTT ESQQEQEKEK EKDEEIKKLD LPADLKIEVK
PETLKDFVGP EIYIKDRLYE TLNPGVATGL AYNTSGDGDA LYIESILTDS ISSDLGNAGL
HVTGSLKDVM KESASIAYSF AKQFMVRQFP DNRFFEAAHI HVHCPGGAIP KDGPSAGIAF
TSSLVSLALN KSLPNDTAMT GEITLTGKVL AIGGLREKSL GAKRAGYTKI IFPKDCEYQL
DEIPDEVKEG LTYIPVEWYS EVFEHLFQGI SKEEGNSVWK EEFAKLEDKK KSKKTNTK
