ID A0A0P7Z0Z0_SCLFO Unreviewed; 1006 AA.
AC A0A0P7Z0Z0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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 Name=LONP2 {ECO:0000256|HAMAP-Rule:MF_03121};
GN ORFNames=Z043_106860 {ECO:0000313|EMBL:KPP74014.1};
OS Scleropages formosus (Asian bonytongue) (Osteoglossum formosum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages.
OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP74014.1, ECO:0000313|Proteomes:UP000034805};
RN [1] {ECO:0000313|EMBL:KPP74014.1, ECO:0000313|Proteomes:UP000034805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP74014.1};
RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.;
RT "The genome of the Asian arowana (Scleropages formosus).";
RL Submitted (AUG-2015) 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|ARBA:ARBA00004253,
CC ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03121, ECO:0000256|RuleBase:RU000591}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01122}.
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:KPP74014.1}.
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DR EMBL; JARO02001941; KPP74014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7Z0Z0; -.
DR STRING; 113540.ENSSFOP00015019945; -.
DR Proteomes; UP000034805; Unassembled WGS sequence.
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; -; 2.
DR Gene3D; 2.30.130.40; LON domain-like; 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; 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; IPR027501; Lonp2_euk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008268; Peptidase_S16_AS.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
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; 2.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03121, ECO:0000256|RuleBase:RU000591};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03121,
KW ECO:0000256|RuleBase:RU000591};
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 Reference proteome {ECO:0000313|Proteomes:UP000034805};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03121}.
FT DOMAIN 129..340
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 769..988
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 366..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1004..1006
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT COMPBIAS 705..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 861
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT ACT_SITE 937
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT BINDING 495..502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
SQ SEQUENCE 1006 AA; 109852 MW; 579116B0D120DAF1 CRC64;
MDGEERMEKG RILRGGSSCE RVSARRGARS AVTLKEEDCC GGRSAREGAQ TEEVQLTEES
TGGGITSVKR ESVSEKPWIL AVFWSSQRFT DSMSQFTQIL VVLLGSVTVN FPSTTIMSSS
GDIRIPSRLP LLLTHEGVLL PGSTMRVSVD TARNMQLVRS RLLKGTSLKS TIIGVVPNSR
DPEHETEELP ALHSIGTAGL AVQVVGSNWP KPHYTLLITG LCRFRVEQLL RERPFPVAVV
QQLDKLEQYA GLDSGDADVS SELGELSQRF YEVALQLVGM LDISVPVVAK LRRLLDSLPR
EALPDVLTSM IHVSNKEKLE ILDAVSLAER FKKVLPLLTR QMEGLKLLQR TRKPRLDDDR
RIIPIRKGGG LAPGQLSMED DGEEEDSDDT SLLERRVRGS NMPEAALRVC LKELKRLKKM
PQSMPEYALT RNYLELMVEL PWSKSTTDCL DIRAARVLLD SDHYAMEKLK RRVLEYLAVR
QLRNSLKGPI LCFVGPPGVG KTSVGRSIAR TLGREFHRIA LGGVCDQSDI RGHRRTYVGS
MPGRIINGLK AVGVNNPVFL LDEVDKLTKS LQGDPAAALL EVLDPEQNHS FTDHYLNVPF
DLSQVLFIAT ANTTATIPPA LLDRMEVLQV PGYTQEEKVE IAHRHLIPHQ LEQHGLTPQQ
VQIPQDTTLD IISRYTREAG VRTLERKIGA ICRAVAVKVA EGHKATKTPS SSSSSEVTTA
QEGGNKGEEP IGGSVDLSLP PEMPIVIDCQ ALKDILGPPV FEMEVSERLT LPGVAIGLAW
TPLGGEIMFV EASRMEGDGQ LTLTGQLGDI MKESAHLAIS WLRTNAKAYQ LTNMAGGPDP
LEGTDVHLHF PAGAVTKDGP SAGVTIVTCL ASLFSGRLVR SDVAMTGEIT LRGLVLPVRE
ALVPLSRHPP LLWQVGFTCT LTSKPVLLCQ VGGIKDKVLA AHRAGLRCVI LPKRNEKDLE
EIPAHVRADL QFVATSCLAE VLDAAFDGGF RGPAPSLAPP PVLSKL
//
