ID A0A0G4H4L8_VITBC Unreviewed; 994 AA.
AC A0A0G4H4L8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Lon protease homolog {ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU000592};
GN ORFNames=Vbra_1842 {ECO:0000313|EMBL:CEM38739.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM38739.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM38739.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) 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; CDMY01001000; CEM38739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4H4L8; -.
DR STRING; 1169540.A0A0G4H4L8; -.
DR VEuPathDB; CryptoDB:Vbra_1842; -.
DR InParanoid; A0A0G4H4L8; -.
DR OMA; YVGPPIY; -.
DR OrthoDB; 1103874at2759; -.
DR PhylomeDB; A0A0G4H4L8; -.
DR Proteomes; UP000041254; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; 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 NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 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; 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|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:UP000041254};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 119..337
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 728..961
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 45..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 867
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 910
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 994 AA; 110455 MW; B04AD5D85CF3E7FC CRC64;
MLTRLSTPAL RHWPTLRSSV SSACLPHQHA RPPVHCSLTS AHRSFAGRRK GGDHKRWHRH
AEHAAEEGEA ADGSAAGGAG AAEAASGESA RAEGEGSADS GGASHVPSVI RGVPHFPQLF
AVPLFRKPAF PGFYQILQVQ DKEVVDFLLD LRKKGQEFVG AFLTKEEPKS DDEETYVATL
RVDAGKVAKI EDMYDTGSII HVLNFVPHQN SQGGQLIVMP HKRIRMLGPT DMDQKSNVLW
NVKVEYLQDE MIKFEKNTTL KALHHEIVAT LKELLRTSYF YKEHFESVIR FYNLDYPAKL
ADLVAGISMA KREELQNVLA EENIEQRLSL VLEIAKKDLE FAKLQSQVRA QVEEKISKEQ
RKYLLMEQLK SIKRELGLEK DDKETIIQGF HDAIKDKTVP EEAKKVIDHE LSRLSSLEMS
SSEFNVCRTY LEWLTSLPWG HHTDDNQDIK KAEQILNEDH YGLQDVKDRI LEFMAVNVLK
GDVQGKIMCL VGPPGVGKTS IGRSVARALD RKFYRFSLGG LFDVAELRGH RRTYVGAMPG
KLIQALKASG SCNPVILLDE VDKLGRDFRG DPASALLEIL DPSQNNTFRD HYMDVPVDLS
KVLFLCTANT SDTIPAPLLD RLEIIRIAGY VFQEKMAIAN EYLIPQTATA TGLKDDQIEV
PQNVISRLVR DYAREAGVRN LLKLIEKVYR KAALKIVKDG EEMVKVALDN LVKFVGQPTF
FSDRLYEETP PGVVMGLAWT QLGGATLYVE ATGRLKKDIR GGEVPVNTQP DEAIEASDEK
ESDEGEERET DKPKKRPPSD DETPDSSMGG PFKVTGQLGS VMSESSQIAL TFTRNFVKTI
DPKNSFLDQA TIHLHVPEGA TPKDGPSAGI TMATALVSLA VNKPVVRDLA MTGELTLTGR
VLRIGGVKEK VIAARRENAR ILLFPLDNKK DYDELADYIK EGLHVFFVSH YRDVYNYAFG
LADEVRNLPA REAPLPEAHS ANELPIPAAA ANAA
//
