ID Q572J2_PHYIN Unreviewed; 930 AA.
AC Q572J2;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 24-JAN-2024, entry version 101.
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=PI35.0330 {ECO:0000313|EMBL:CAI72282.1};
OS Phytophthora infestans (Potato late blight agent) (Botrytis infestans).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4787 {ECO:0000313|EMBL:CAI72282.1};
RN [1] {ECO:0000313|EMBL:CAI72282.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=15894622; DOI=10.1073/pnas.0500113102;
RA Armstrong M.R., Whisson S.C., Pritchard L., Bos J.I.B., Venter E.,
RA Avrova A.O., Rehmany A.P., Bohme U., Brooks K., Cherevach I., Hamlin N.,
RA White B., Fraser A., Lord A., Quail M.A., Churcher C., Hall N.,
RA Berriman M., Kamoun S., Beyon J.L., Birch P.R.J.;
RT "An ancestral oomycete locus contains late blight avirulence gene Avr3a,
RT encoding a protein that is recognized in the host cytoplasm.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7766-7771(2005).
CC -!- SIMILARITY: Belongs to the peptidase S16 family.
CC {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
CC ECO:0000256|RuleBase:RU000591}.
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; AJ893356; CAI72282.1; -; Genomic_DNA.
DR AlphaFoldDB; Q572J2; -.
DR VEuPathDB; FungiDB:PITG_14380; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
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}; Membrane {ECO:0000256|SAM:Phobius};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 720..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 751..768
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..307
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 747..929
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 683..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 837
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 878
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 465..472
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 930 AA; 103382 MW; B6EF15EDB82FC76A CRC64;
MATATALRRF AMARPRSHIT AVNTLRLQRA PVLAAYRVRA NPFACSNRNV FCAFYSTDSG
KDDDTDAEKP NEDAEDDGVE VVIDNDLATV GEGDNAPTYP HVLAVPALRR PFFPGVVLPM
TITNPEVTRA LMALKESGQK YVGVFLKKST GDPLKSGGGE DLVKNLSEIH HVGSFARIDN
MLPFDANSVQ VLMVSQRRIA IDDIRDEGPP LRVNISNLDN PTFDPKSKLI RAYSNEIVAT
LREIVKMNPL FKDHMQYFSQ RIDIHNPYKL ADFAASVTSA DGEELQQVME EMSCEARLKK
ALELITKELE LSKVQQTIKE QVEEKVSKNQ RNYLLMEQLK AIKKELGMEK DDKDAMITKY
RERLAQFEPG SIPQSVNEVV EDELNKMSML EKNSSEFNVT RNYLDWLTQL PWGKATEENF
DLAKAKQILD EDHYGLKDIK ERILEFIAVS KLKGDVQGKI ICFVGPPGVG KTSIGKSIAR
SLNREFYRFS VGGLSDVAEI KGHRRTYVGA MPGKIIQCLK STQSSNPLIL IDEIDKLGRG
YQGDPASALL ELLDPSQNSG FVDHYMDVPV DLSRVLFICT ANVTDTIPGP LLDRMEVLRL
SGYDSPEKLA IAKEYLVPKA LEKTGLQKSE TTPESLGLTD DAILTLVKQY CRESGVRNLE
KHVEKVFRKV ALEVVEDIEK AKAAESQEAG ESTTAEDIKE DSDDKDRFLI SPEKLSKYCG
LVTASILLSL LTLTILFLCS SDRMFDKQFP GVVMGLAWTA MGGASLYIET TKVHTKGDRS
GLITTGQMGS VMEESTKIAH TYARSKMHAI DSENKFFEEN EVHLHVPEGA TPKDGPSAGC
TMVTALLSLA MDKYPDLAMT GELSLVGKVL PVGGIKEKTI AAKRAGVKTL ILPLGNKRDF
DELDEYLQKD LDVHFADYYD DVYKVAFEQE
//
