LONP2_CANAL
ID LONP2_CANAL Reviewed; 1258 AA.
AC Q59YV0; A0A1D8PK96;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=CAALFM_C305360CA; ORFNames=CaO19.6973, orf19.6973;
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 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; CP017625; AOW28550.1; -; Genomic_DNA.
DR RefSeq; XP_714679.1; XM_709586.1.
DR AlphaFoldDB; Q59YV0; -.
DR SMR; Q59YV0; -.
DR STRING; 237561.Q59YV0; -.
DR GeneID; 3643676; -.
DR KEGG; cal:CAALFM_C305360CA; -.
DR CGD; CAL0000175783; orf19.6973.
DR VEuPathDB; FungiDB:C3_05360C_A; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_0_1; -.
DR InParanoid; Q59YV0; -.
DR OMA; NKSPIIM; -.
DR OrthoDB; 528132at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0005782; C:peroxisomal 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; 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; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR GO; GO:0006625; P:protein targeting to peroxisome; IBA:GO_Central.
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..1258
FT /note="Lon protease homolog 2, peroxisomal"
FT /id="PRO_0000395791"
FT DOMAIN 22..402
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 990..1241
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 270..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1110
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT ACT_SITE 1153
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
FT BINDING 728..735
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03121"
SQ SEQUENCE 1258 AA; 140936 MW; ED4AAEFE9BCC3A36 CRC64;
MAKYNNNSNA SKATNLKQQV VLPTYTLDSN LVLLPGIMYN VTFSRFKAAA LLYRYKNFIS
QVSIINNLLN EYDFNSGNTN EEERFEAEQK LEQPETYHEI NPSVISPEAV EGIKEFFQYE
TGMKTGRGVE KGVKSTQNDA IKEFDWLTLA IIPNLEKIKN PETNSSAGDG SSSSKVVTVA
RIVGIVDDTT NIKLTLQAIT RGVQIKDDGK NNHHKRGLKT NEQVIGIDWN HNVSDLKGKF
TTLQKNYQQL FQSIDKFLID YREALDYNKN NSNNNNNNNN NRNGNLSLIK GNSTTYSNNK
NYDDKPNQDI KSQNLLTLNP LANALYMQLV GSKDFNKAFH RLQKLFSQVI QGDEYKIDNE
TYLRLVDLTC GILPFPNFQK LALLNEYKLD DRSILINEMM SQLIQIFGNL QTNTSFVNSW
FHSEATNIQK ATVVANQLKS IRNLLEGMTK NRPIKPNKRN SGPASSAPSF SNGKTPPARP
KVNHHQDGSH GHDSDYDNND DDDDGDEDLK AIFNFIKHKL PTISSLSADS KRLILKDFKR
VKASANSPGG GGNSDFHVLR NYLEIVMDIP WDNYVTKFKS NKDIDLKLAK KQLDDDHYGL
EHVKKRLIQY LVVLKLLGIN AEKDQALQSK DEENSKNPAH SDSNSNSNCN SNSRSLTKSP
TSSLASKTPS SIVIANNDET YLAKQQAKTR NQKSITEAKT NVSTKMVPSN ESIQVSKNNK
SPIIMLAGPP GTGKTSLAKS IASALGRNFQ RISLGGIKDE SEIRGHRRTY VGAMPGLLIQ
ALRKSRCMNP VILLDEIDKV IGGNSGGVNK FNGDPSAALL EVLDPEQNNT FIDHYLGFPV
DLSQVIFICT ANDPWNMTRP LLDRLEMIEI GAYDYNEKLI IGKKYLLPRQ IKRNGFPVTK
VGKNNTGNQD EFIKINDDTM KKVILDYTRG EAGVRNFERR LGTLCRFKAV EYCEWLNKDI
KNYNPIIDEN DLPIYLGVPY SSGDVTTEGT VGVGVVHGLS YNSDGSGSVL VFESIGFDRR
ISNGNKEHNG GDGSGGNGAT LNMTGRLGEV LMESGKIGLV FIKSMIYKNI LKFDNNNNNN
TNRHLLLDKY NNLDIHMHVP MGSVSKDGPS AGVTMALSFL SVLLDKPVPS DIAMTGEITL
RGIVLPIGGV KEKLMGAHLN ANIKRMIVPR ENRKDLIKEY SRSIEEAGEV LDHHLINDLI
KDNEDNEFKL TQVEDYYQNK YGISLFYAKE FYDIIKIVWN EDEVLLKENN SRLLEYHI
