ID A0A1V9YG85_9STRA Unreviewed; 775 AA.
AC A0A1V9YG85;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ACHHYP_12980 {ECO:0000313|EMBL:OQR84755.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQR84755.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQR84755.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQR84755.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
CC -!- SIMILARITY: Belongs to the peptidase S16 family.
CC {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
CC 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:OQR84755.1}.
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DR EMBL; JNBR01001836; OQR84755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9YG85; -.
DR STRING; 1202772.A0A1V9YG85; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000243579; 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 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 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 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};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001174,
KW ECO:0000256|PIRSR:PIRSR001174-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001174};
KW Reference proteome {ECO:0000313|Proteomes:UP000243579};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001174}.
FT DOMAIN 6..211
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 588..767
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 214..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 675
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 718
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 350..357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 775 AA; 83669 MW; AF25EA2427E97C6E CRC64;
MRASPSPILT IRDAVLFPGA YLRVSVGRES SLRLVQETLW KSFHASLESA PIAPVHVGVF
TEHKDTSDTY VLGNVGTLAR VVQLQRTKKY RNRAHEYEYS MLVQGLSRVE IIETLQTAPF
IMASIATVED TYDAASLTEL VALIRSNFSL SKKMQLPRVN TADEADVVAK ISAWLDMLSA
HVQGSPAQKQ ALLSTSDVGE RLNKLVALVQ GPTSRALVSS RNPSPPRQVD DDDMDTDEND
TKLLTKKLSE LQSVLPPPTF KLLSRELKRL MRMTPQQPEH HVVQQYLEFM LDLPWQSAVP
PALDMATVQA QLDADHYGMQ LIKTRLVEYM AVRQLQDSAQ RKGLILCLVG PPGVGKTSLA
QSMATATGRP LERLALGGVC DETEIRGHRK TYVGAMAGSV LSALRRAQSS HALVVLDEID
KLGSRHASGA SSVSHALLEV LDPHQNHAFT DHYASAPFDL SHVLFVATAN SVETIPRPLL
DRMELLHLEG YTLEEKVAIA TQYIVPRQVR QHGLPAPVVF ADGALPYVIA HHTREAGVRD
LERKIAAVCR HLAVLVVQKK ELPATLSVEL LASVLGPDSV HDEVALRSGV AGVATGLAWT
PVGGAILFVE ATALRGATTA PLGLQLTGAL GDVMKESAQL ALTWLRGYLP PGRLDGISEF
HLHFPHGATP KDGPSAGIAI VCALVSVVTQ QVVPVDVAMT GEITLRGVVL PVGGVPQKLQ
AAKRAGIARV LLPAANKAEG DEWGPKLGLE VTYVSDLLAV LDTVFGTAAV VRSRL
//
