ID W6Z627_COCMI Unreviewed; 928 AA.
AC W6Z627;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=COCMIDRAFT_95500 {ECO:0000313|EMBL:EUC45430.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC45430.1};
RN [1] {ECO:0000313|EMBL:EUC45430.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC45430.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(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: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|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI963984; EUC45430.1; -; Genomic_DNA.
DR RefSeq; XP_007688042.1; XM_007689852.1.
DR AlphaFoldDB; W6Z627; -.
DR STRING; 930090.W6Z627; -.
DR GeneID; 19128670; -.
DR KEGG; bor:COCMIDRAFT_95500; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_4_0_1; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000054032; 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; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
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; IPR015947; PUA-like_sf.
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 PIRSF; PIRSF001174; Lon_proteas; 3.
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; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 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|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03121,
KW ECO:0000256|PIRNR:PIRNR001174};
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 14..256
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 727..914
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 298..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 926..928
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT ACT_SITE 820
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 863
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 484..491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 928 AA; 101329 MW; 12F808B9CB2B735F CRC64;
MMGKGSSKTS TTVLPLIPLA PPLAVLPGTT LKIPITNRSD VAAILAKIYS ISPTAKPDAA
ITVACVPLKS NTLGSDGNML IEDGHQRDKT HYESDPILAT KKDIFGWACV AKVSGVQGRK
QGDLSLIVEG LERVQVVDVV QERPYFEGEL AAVEEYIDIA SADLLNQFNL LKQLSRELLA
LVRLSAILPR TPQVTLSPIV ARRLEMFITR KDLSDAGLLA DFMANVVDTT HEETLRVLAS
VDVKERVDRV IEILQRQISN IQGNTRMTVA TTQSSNGTLD MDTLRKLQQE ALKRRSKMGG
MPPGFPAGFP GGGAQQAGED EPNEIDELKK RLEDAKLSAE ANKVAQRELA RLQKMNPAQA
EYQVCRNYLE NLAEIPWSKM TVDQLDSNTL VRAKQQLDND HYGLEKIKKR LLEYLAVLKL
KEQANKTIDD QIRSLTEAPN AEAEAEAKQP VATQKVTREP SETEVRLLEK KRMVDKSPIM
LLVGPPGVGK TSLAKSVATA LGRKFHRISL GGVRDEAEIR GHRRTYVAAM PGLIVNGLKK
VGVANPVFLL DEIDKLGMSN HNGDPGAAML EVLDPEQNHT FTDHYVNIPI DLSKILFIAT
ANSLDTIPPP LLDRMETIQL SGYTTLEKRH IASRHLIPKQ ITSNGLQTEH IQIPTEVLDK
IITSYTRESG VRNLEREIGS VCRAKAVEYA TAKDTNTVAA YSPVVTVEDV EATLGIEKFA
QEVTEQSARP GVITGLVAYS TGGQGSILFI EIADMPGQGR VQLTGKLGDV LKESVEVALT
WVKAHAFDLG LSTTHDEDIM KNRSIHVHCP SGAIPKDGPS AGLAHTIGLI SLFSNQPVPP
TLAMTGEISL RGRVLPVGGI KEKLIGALGA GVERVLLPEG NRKDASELPE EVVRGLKIEF
VGHIWEALGK VWPERWEGEG ARGWDSRL
//
