ID A0A238FJ26_9BASI Unreviewed; 1022 AA.
AC A0A238FJ26;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Lon protease homolog {ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU000592};
GN ORFNames=BQ2448_7080 {ECO:0000313|EMBL:SCV73155.1};
OS Microbotryum intermedium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV73155.1, ECO:0000313|Proteomes:UP000198372};
RN [1] {ECO:0000313|Proteomes:UP000198372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR EMBL; FMSP01000017; SCV73155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238FJ26; -.
DR STRING; 269621.A0A238FJ26; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000198372; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 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; IPR046336; Lon_prtase_N_sf.
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 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 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.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000591};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000256|RuleBase:RU000591};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000591};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000198372};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 12..294
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 814..998
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 73..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 906
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 946
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 1022 AA; 111254 MW; 4493FBFA1030442F CRC64;
MASRTYNIPT HLPILPLPEK QVLYPSLVLS IQVVAKHSIA LLQNVLREAE QNSGNKPLII
GVVPLRDTAS PATGSAPAIA VPKRSPNPAL TSNKRDPYRT PPQSDDESDN KDNSNPYKSS
ALVLHKSSTA QGKPPISDLY ECPSFKHGVA ARIVRLERLS SGGFIVVLEG LARIVLHMDD
FGPSTLPFHE TTVTVLNSTP LSPSSPLLEA LQAISNQVLT SLSAIAPLSL LLNRRLKSLI
GALTPETAPT LVDALIGSIP VNTTTGLQFS DRLTILSTLE GDDRVAQAIE ILGRVDESLN
LRKRIGDKVD QNTTRRQREY LLMQQLIAIR QELEELAAID AKNGRASSSP LSRLRGGPGG
KKKGPVDDDD DDEENEENEM AELEKKIKAK AWTEESRKVV MREFKRLKKS PPQGAEHGVI
RNYVEWLLAL PWNESTPLPL SKNFIEQARK QLDDDHYGLE KVKKRLLEWL AVLRLKQEQW
EVDNAAPVAS LEQAQLIDGA PTKASSEGAL EWTSGQVIAS TNDSAPPPAP ASSVPAPTKQ
NVVAKPRDKG PILLLCGPPG TGKTSIAKSL ASAMGRKFQR ISLGGVRDEA EIRGHRRTYV
AALPGAIAQA LRKCGTNNPV ILLDEIDKLG SSNTHGDPGA ALLEVLDPEQ NYSFEDHYLG
IPLDLSSVLF IATANSLDTI SEPLFDRMET IELSGYVHSE KLAIAKKYLI PKQLKANSLP
ADLLSIPDDV LLHLITSYTH EAGVRTLERE IGAVCRAKAV EYTKARDEAE AVNDPLGRLG
ADVTKYGYRV VLTKEDIGDI LGQSRHEAEE MDRENMIGVS TGLAYRGSGN GGVLHIETTS
MPGHGNFKLT GQLGDVITES AGLALAWTKS HAHELGIANS RTEDAFKDLD IHLHLPSGSI
KKDGPSAGVA MVVAIVSLMR GIRMIKGVAM TGEITLLTPV GGIREKVLGA HRAGIRTLIL
PFKNRRDVND DLPLEIKNDM EFIFIKNIFE ALEAAFGKEA LWRGREGDRT RDMVYSEMAS
RL
//
