LONP2_DEBHA
ID LONP2_DEBHA Reviewed; 1147 AA.
AC Q6BJJ8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000255|HAMAP-Rule:MF_03121};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_03121};
GN OrderedLocusNames=DEHA2G01892g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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 and unassembled polypeptides in the
CC peroxisomal matrix. Necessary for type 2 peroxisome targeting signal
CC (PTS2)-containing protein processing and facilitates peroxisome matrix
CC protein import. {ECO:0000255|HAMAP-Rule:MF_03121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03121};
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000255|HAMAP-
CC Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_03121}.
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DR EMBL; CR382139; CAG90071.2; -; Genomic_DNA.
DR RefSeq; XP_461623.2; XM_461623.1.
DR AlphaFoldDB; Q6BJJ8; -.
DR SMR; Q6BJJ8; -.
DR STRING; 4959.XP_461623.2; -.
DR EnsemblFungi; CAG90071; CAG90071; DEHA2G01892g.
DR GeneID; 2904488; -.
DR KEGG; dha:DEHA2G01892g; -.
DR VEuPathDB; FungiDB:DEHA2G01892g; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_0_1; -.
DR InParanoid; Q6BJJ8; -.
DR OMA; NKSPIIM; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0005782; C:peroxisomal 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:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 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 SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 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; Hydrolase; Nucleotide-binding; Peroxisome; Protease;
KW Reference proteome; Serine protease.
FT CHAIN 1..1147
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000395793"
FT DOMAIN 20..346
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 903..1131
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 395..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..444
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1006
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 1049
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT BINDING 651..658
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ SEQUENCE 1147 AA; 129573 MW; 47D97BD950F24BCA CRC64;
MARYKPNQQN HTDPKQQVVL PTYKLDSNLV LLPGIIYNVT FSRFKAATLL SRFKSQVSNV
SLITNLLNEY DFDSKQEEKD DVESKYMPPP ISSDAVTGIK QFYQYEQQFK GKNDDSSKVE
AEPQSEFDWL VLAINPNLEK IKEPQTSSDD EYENIVTIAR VIGMVDDTSN IKLTLQALTR
GIKHNKVKPT QTNEVLIDID WNSNIDDVAS KYDVLNSKVL KLFRSIDGFI VDYRQALTVA
ASLAKKGKQS KDLKQKGDLL TLNPLANSLY LHLAASKDFT KAYISLQKLF GTFNSSSNTK
IDNKTFLRLI DLTCAIIPFP NHEKLKLLNK FNSIDRINEV NRMLESMIQV FYNLKKNNKI
INHWFYNEAT NIQRANVVAS QLKSIRLILE GMTNKPDKDI KTNQSPPRQL VRRGNNNKPA
KSPMSDDGNE SNDEYDDDED DDDDEDELKA ITSFIKGKLP NISTLSSDTK RLIVKDFKRI
KSSPPGNSDF HVIRNYLEIV ADIPWDRYVT RFKSNKDIDL EFAKKQLDSD HYGLQHVKTR
LIQYLVVLKL LGINAEKEFE KIESENSKKS KKNESSSGSM GKNDKQRSEK TFTRSDDSIV
IANNDETSIA HETARNKNKK SKSLTTIEKS SLNKSLMVSK NNKSPIIMLV GPPGTGKTSL
AKSIAKSLGR NFQRVSLGGI KDESEIRGHR RTYVGAMPGV IIQSLRKSRS MNPVILLDEI
DKIIGGNNGV NKFNGDPSAA LLEVLDPEQN TSFIDHYLGF PVDLSQVMFI CTANEASNLS
RPLLDRLEMI EVGAYDYDEK LVIGERYLLP RQIKRNGIPN ADLIDVDKSV MQKVILDYTR
EAGVRNFERS LGRICRFKAV EYSQSLEKLS EYQPKVEIED LPKYLGLPFA NLSTELFESP
IESAKCGVVN GLSYNSDGSG SVLVFESIGF NHEGKSGSSS LNMTGRLGDV LMESAKIGLT
FIKSIIYKNL LNLSDRNLSE NLIDKINNME IHLHVPSGSI QKDGPSAGIT VALSFLSLIL
EKPVPLDVAM TGEITLRGLV LPIGGIKEKI LGAHLNGIKR VIVPRENRKD LIEEYCRSTN
DFNQLNDLLL DNENKYNFKR CEPEKFWFDK YGITIHYARE FWDVIKAVWG DALLVKVEQA
RMVEYHL
