ID M3J2S7_CANMX Unreviewed; 1174 AA.
AC M3J2S7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Lon protease homolog {ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU000592};
DE Flags: Fragment;
GN ORFNames=G210_3586 {ECO:0000313|EMBL:EMG46173.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG46173.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG46173.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix
CC {ECO:0000256|ARBA:ARBA00004253}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG46173.1}.
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DR EMBL; AOGT01002092; EMG46173.1; -; Genomic_DNA.
DR AlphaFoldDB; M3J2S7; -.
DR STRING; 1245528.M3J2S7; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_0_1; -.
DR OMA; NKSPIIM; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000011777; Unassembled WGS sequence.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:InterPro.
DR CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03121; lonp2_euk; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR027501; Lonp2_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF24; LON PROTEASE HOMOLOG 2, PEROXISOMAL; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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 {ECO:0000256|RuleBase:RU000591};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000256|RuleBase:RU000591};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000591};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 24..367
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 918..1157
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 412..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1026
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 1069
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMG46173.1"
SQ SEQUENCE 1174 AA; 132266 MW; 8CE04A4D9D4E4589 CRC64;
MGKYTKNSDS DTKSSGNLKQ QVVLPTYTLD SNLILLPGII YNVTFSRFKA AALLFRYKNL
VSQVSIINNL LNEYDFNNDD HHQEETVADN STHNGDNVNP RVISRDAVQG ITHFFKYENR
IKNNSNDEKL INEFDWLTLA IIPNLDKVKD FHDEASSNVV TVARVIGIVD DTTNIKLTLQ
AITRGVVLQD KQRSLKSNEQ LVGVDWNYHV YDLKARFKTL KNNYNLLYQS IERFLSDYRQ
ALNANSNGAN GKGNLSLVKK GDYKNIEKND THIPSSGNQD LLTLNPLANA LFLQLMGSKD
FNKAFSSLQN LFSQFSSNEF EIDNKTFLRL IDLTCGILPF PNRQKLSLLN KYKLDDRVTF
INEMIIQLHQ VFENLHTNNS FVNNWFQNDA TNIQKANVVA NQLKSIRYLL EGMTKNRPSG
NQRNSMTSSR PRQKITSGRV SHDDNGNNNN NEDDDDDDDE LRAITNFIKN KLPGVTTLSA
DTKRLIVKDF KRVKAAANSP GGGGNSDFHV LRNYLEIVMD IPWDNYVTKF KTNKEIDLKN
AKKQLDDDHY GLEHVKKRLI QYLVVLKLLG INAEANTKNT DSTTNPSSSS PQSPPPPPST
NNNQSTSKIV IANNDETSSS KEQARNKNKQ SIIEVQNDSL APSAESIHVS QHNKSPIIML
AGPPGTGKTS LARSIASALG RNFQRISLGG IKDESEIRGH RRTYVGAMPG IIIQALRKSR
CMNPVILLDE IDKVIGGNSA ANRFNGDPSA ALLEVLDPEQ NNTFIDHYLG FPVDLSQVIF
ICTANDPWNM TRPLLDRLEM IEVNAYDYNE KLIIGKKYLL PRQIKRNGFP DTSEKFIDIN
DKTMKKIILD YTREAGVRNF ERRLGTLCRF KAVEYCEWLN KDRKTYNPTI DENDLPIYLG
VPYANGDVVS NDATSIGNSR VGVVNGLSYN SDGSGSVLVF ESIGFDRRIS NKDSQGSGAT
LAMTGRLGDV LMESGKIGLI FIKSMIYKNL LKIDDSDNDR QLLDKFNNLD INMHVPMGSV
SKDGPSAGVT MALSFLSVLL DKPVPSDIAM TGEITLRGLV LPIGGVKEKL MGAHLNNTIK
RMIVPRENRK DLIEEYSRSI EEAGEVLDHN LINELLKDNE ETEFKMNQVE KYYLKKYGIS
LFYAKEFYDV IKIVWNDDEV LLKEDNSRLL EYHI
//
