ID A0A261BNY6_9PELO Unreviewed; 885 AA.
AC A0A261BNY6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Lon protease homolog {ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU000592};
DE Flags: Fragment;
GN ORFNames=FL83_13415 {ECO:0000313|EMBL:OZG12021.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG12021.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG12021.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG12021.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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:OZG12021.1}.
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DR EMBL; NIPN01000099; OZG12021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261BNY6; -.
DR STRING; 1503980.A0A261BNY6; -.
DR Proteomes; UP000216463; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:InterPro.
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 HAMAP; MF_03120; lonm_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; IPR003111; Lon_prtase_N.
DR InterPro; IPR027503; Lonm_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; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 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; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000591};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000216463};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 55..301
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 698..885
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 148..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 792
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 835
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG12021.1"
SQ SEQUENCE 885 AA; 98876 MW; F4CD7994FF5F13AD CRC64;
MYRAGALVLR GSALRRTRFF TASIHQNFAT FSQKSILTKP IVSTIAAGNQ KKFYSSGNKD
HDDPIAVDDS LELYKDLIVK DDNLKALIRR QLSLKQPYAG VFVKRDDENK EETIASLSEV
YPTGSFVQII EVRDQGSVLE LVLSAHRRRA RGKRTGLPPT PPPSPPLSTP TSAPEFPTSS
TSTEEKDEKK TAPAEEKQRK GIVMVKTENV IADPVPKNNE TKATMMAIVQ TIRDVVQFNQ
LFGQQINLLL HPSQNVIDNP VYLCDLVATL VQSAETKDLQ EMMDETDVSK RLKIALLLIQ
KEKAVAKLKH DINKDVEKKV QDHHRKYLLN EQLKVIKKEL GIEKDEKTTI IEKNDERIKA
LAVPEYALKV INEEKTKLQF LDPHSSEFSV TRNYLEWLTS VPWGLTSPEN RRLSHAKKAL
DEGHYGMKDV KERIMEFIAV NLLRKSIGGK ILCFHGPPGV GKTSIAKSIA TALNREYFRF
SVGGMTDVAE IKGHRRTYVG AMPGKMIQCM KKVKTENPLV LIDEVDKIGG AGVLFICTAN
EISKIPGPLR DRMEMIDVSG YLAEEKVAIA HQHLIPQLRK ETSLSKDQLD IEDAALEELI
KHYCRESGVR NLQQHIERIF RKAALQIAEQ ETEDEEPSEK ATTAITENSD AEPITSTSST
TETESVKTTT AEKITISIDN LQKYVGRPKF TSDRMYEVTP PGVIMGLAWT AMGGSALYIE
TVLKRPVDLT SDKDGSIETT GNLGDVMKES VRTALTVAKG ILAREQPDNK FFDKSHIHIH
VPEGATPKDG PSAGVTLVSS LLSLALKRPV VQDMAMTGEI SLTGKVLPVG GIREKIIAAR
RVGAKRVFLP AENRRDFDDL PEFMKSELDI RFVSHYDELY EHLFQ
//
