ID W6MP77_9ASCO Unreviewed; 1052 AA.
AC W6MP77;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 08-NOV-2023, entry version 46.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000256|HAMAP-Rule:MF_03121};
DE EC=3.4.21.- {ECO:0000256|HAMAP-Rule:MF_03121};
GN ORFNames=KUCA_T00004423001 {ECO:0000313|EMBL:CDK28441.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK28441.1};
RN [1] {ECO:0000313|EMBL:CDK28441.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28441.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK28441.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK28441.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_03121}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000256|HAMAP-
CC Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03121, ECO:0000256|PROSITE-ProRule:PRU01122}.
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DR EMBL; HG793129; CDK28441.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MP77; -.
DR STRING; 1382522.W6MP77; -.
DR HOGENOM; CLU_004109_4_0_1; -.
DR OrthoDB; 1103874at2759; -.
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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 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; 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 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; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03121};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03121, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03121};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03121};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03121}.
FT DOMAIN 792..1031
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 490..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1050..1052
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT ACT_SITE 893
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 936
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 528..535
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
SQ SEQUENCE 1052 AA; 116012 MW; BFE3149BE583DB9F CRC64;
MTMARNDTFE VQLPLMQLNP RLLFLPGIVY RTSFTHEQAV AILARFSSIL KDTDFNHREV
VQDALLKGGK SSISQSSLDG CQSVKKKLSV ESDENPWLVL VCLPGSTVTG DETVGTVCSI
VDISERSNEV TISFKALSRG LLRPAKSDPQ NESKVVVEFR AGSKLPTKDL RKTLTNCLRL
LGNVQSFSKQ YRDASKAFGD LDDDERLKNV MLVLTPLASV LYDQLSSQEM SQSFVRLNRM
FKGLDSEFAS MSSTEQAVRL LQLVDILTAV FPFTATHKNR VLSSFSQSLS RLDAANEAID
FGNKIFEETL NMNYLVETWK SLDVRSSPRR AATTKSRFIS NHLRSLKLLL EEINDARPKG
SNKGPLRPRD TNEDDDSDLV SVFVKNIDNL DLPEDGKKLI LKDFKRLSSM QQSSSEYQVI
RSYLEIVADI PWTKFDAARN YSAIDLENAK SQLDSDHFGL NSVKERILEY LAVLSLHSRL
EDVSSAKSKD SANSISIGDP DTKAPSPLAL SKKRPRSTVK SPILLLTGPP GVGKTSLAKS
IATALGRNFQ RISLGGLRDE SEIKGHRRTY LGSLPGMLVQ ALRKAQTMNP VILLDEIDKV
VGGSAESAAR AHGDPAAALL EVLDPEQNVN FHDHYIGFPI DLSQVVFICT SNDLYRLSDP
LRDRMEVIEL GGYSYMEKVE ICKRYLVPKQ LKRNGLPLET KSGDSYLQIS DKAILKIAVE
YTREAGIRSL ERMVGSVCRG KAIELSRLIK NSDDLKEFPP GYNPVVSEND LAKYIGLSPR
SSENGTAESG ITPNYGVVNG LSYNSDGSGG LLVFEMNGVE GGSQALTTTG RLGNVLVESI
KIANTIVKSV LNNHLLYSKS GEGIETSRLL KRFNSLDAHL HVPQGAISKD GPSAGITITL
CLLSLVLQKE VPTDVAMTGE IDLRGLVLPI GGVREKLLGA HLSKKVSKVL LPRANRKDVT
ESYLYSISGE DGSDDVLSRL IQEEENSVKS SDKHTRLTVF SDPERWVKDT LKIEISYVEE
FSDVVNAVWG QEISLHLTPD SIKSEEKVVS HL
//