ID A0A024UFH9_9STRA Unreviewed; 918 AA.
AC A0A024UFH9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Lon protease homolog {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|RuleBase:RU000592};
GN ORFNames=H310_03833 {ECO:0000313|EMBL:ETW04652.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW04652.1};
RN [1] {ECO:0000313|EMBL:ETW04652.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW04652.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S16 family.
CC {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
CC ECO:0000256|RuleBase:RU000591}.
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DR EMBL; KI913957; ETW04652.1; -; Genomic_DNA.
DR RefSeq; XP_008866093.1; XM_008867871.1.
DR AlphaFoldDB; A0A024UFH9; -.
DR EnsemblFungi; H310_03833-t26_7; H310_03833-t26_7-p1; H310_03833.
DR EnsemblProtists; ETW04652; ETW04652; H310_03833.
DR GeneID; 20080883; -.
DR VEuPathDB; FungiDB:H310_03833; -.
DR OrthoDB; 1103874at2759; -.
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; 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; 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; 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 PIRSF; PIRSF001174; Lon_proteas; 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|PIRNR:PIRNR001174};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001174,
KW ECO:0000256|PIRSR:PIRSR001174-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001174};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001174}.
FT DOMAIN 72..291
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 728..911
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 817
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 860
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 460..467
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 918 AA; 101511 MW; 9D7CEA164C5366A8 CRC64;
MRLTQAAASG LQRCFGRPHV RLPYAAHRPS APRWCRAFSD IKNYDEDDDE IPASKSIATF
GEGEKAPMVP HVLVIPTHKR PLFPGVVLPM TITNPDVTKA LAALRESGQK YVGVFLKKQG
GKIGAASKDE MGFTGMESQK DEDLVTDLSG IHHVGSYARI DNLINFENNS AAQLLLVGQR
RITIDDVHDS GTIPLRVTIS PVENPAFDKS NQMIKAYSNE IVATLREIVK MNPLFKEHMQ
YYSQRIDIHN PYILADFAAS VTTGDGEELQ SVLEELDCEN RLKKALELLT KEMELSRVQQ
SIKEQVEEKV TKNQRQYLLM EQLKTIKKEL GLEKDDKEAM LTKFRQRLDN FKIPPNPDTP
DAHLSHVPKD ILDVVEDEMN KLAMLEKNSA EFNVTRNYLD WLTLLPWGKS TTENFDIVAA
KMILDADHYG LSDVKQRILE FIAVSKLLGK VQGRIICLVG PPGVGKTSIG KSIARSLNRE
FYRFSVGGLS DVAEIKGHRR TYIGAMPGKV IQCLKSTQSS NPLILIDEID KLGRGYQGDP
ASALLELLDP SQNTSFVDHY LDVPVDLSRV LFVCTANVTD TIPGPLLDRM EVIRLSGYDG
PEKVAIANQY LVPKALEKSG LKDSEHVPPS LALPDDSIQD LVKRYCREAG VRNLEQHIEK
IFRKVALEVV ENLAKEAGSD DVVANFNISP DKLHKYVGQP RFTSFVGALD VALWIDATCA
TRERMYETLQ PGVVMGLAWT AMGGSSLYIE TTTVQSKGGK GSLLSTGQMG SVMEESTKIA
HTYARHKLEL IDPDNAFFES DIHLHVPEGA TPKDGPSAGC TMVTALLSLA LNKPVKADLA
MTGELSLTGK VLPVGGIKEK TIAARRSGVT TLVLPFGNQK DFNELPEYLK DGLDVHFAKE
FDDVFKVALD YSDCDGAK
//
