ID A0A1B7N759_9AGAM Unreviewed; 924 AA.
AC A0A1B7N759;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=K503DRAFT_768352 {ECO:0000313|EMBL:OAX40690.1};
OS Rhizopogon vinicolor AM-OR11-026.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX40690.1, ECO:0000313|Proteomes:UP000092154};
RN [1] {ECO:0000313|EMBL:OAX40690.1, ECO:0000313|Proteomes:UP000092154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX40690.1,
RC ECO:0000313|Proteomes:UP000092154};
RG DOE Joint Genome Institute;
RA Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA Barry K., Grigoriev I.V., Spatafora J.W.;
RT "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT divergence of the mating type B locus.";
RL Submitted (JUN-2016) 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; KV448203; OAX40690.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B7N759; -.
DR STRING; 1314800.A0A1B7N759; -.
DR InParanoid; A0A1B7N759; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000092154; 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; 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; 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; 3.
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:UP000092154};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001174}.
FT DOMAIN 7..232
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 718..908
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 275..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 813
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 856
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 462..469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 924 AA; 100229 MW; 07396AB1C9B5E369 CRC64;
MPSSPRLPVL PLPHPLILLP TARLTFPISR SLAEAILTLL DDADATQPLL AAIPVPGPSE
GDGHDSQFDV SSAINSLPTY GTAARVVRLV RPRSSSSPGA PRQPYLLSLH GLTRIRLASP
LQIDTTSLDT LPIHKVLYPS AEGTPSRETV EAFKDAALSL LDRLAKDSVQ PQRKDDWLRV
AALVEDISEQ RAAWMADVLV AAISGQYGDK LAFLAATDVE DRLHHATELF VKQSSIQEVS
KKIATAVDES LSRQQKEYFL RQQLAAIQRE LHTLHNSPGT AGPGFGTGGA TSELDDDDQA
DADDLADLRR KIEALDVGTE ERKVGVREWR RLKRIPQGSV ENGVIRSYLE WLTSVPWPST
STPASASLDV LKDHSFLTRA RAQLDADHYG LDQIKRRLME YLAIVRLRAI ADAAAATSAP
PQTEGNGALA PASFVDKAVS TSHSASLQKS KGVKGPILLF VGPPGTGKTS LGQSIAKALD
RPFQRISLGG VRDEAEIRGH RRTYVASGPG AIVQALRKAG RNDPVILLDE VDKVGHSNFH
GDPAAALLEV LDPEQNHSFN DHYINVPIDL SQVLFICTSN TLDTISAPLL DRCEVVELSG
YTYDEKMHIA RRFLLPKQIQ ANGLSDSQLA LTDSALLHIA TMYTREAGVR SLERAIGAVV
RYKAVEWAEH LDTVVAPSSG EEGTIVATKS NWHAVVEEDE LEKILGIPRW DGEEREREEK
RGIVYGLVVT GMGEGGILPV ESTVVPGAGR LKLTGSLGDV IKESGEIALS WVKTHAFELG
ITAGRGIDPL KVPDPIDIHL HLPSGAQKKD GPSAGIAMVC AFVSLLSGAC VPKDIAMTGE
ITLRGRVTPV GGIRMKVLGA HRAQIRKVIL PWANRKDVEH DVAPEVRREM QFFFVRTIDE
ALEAAFGRGA LGWRRETVLL ESRL
//
