ID A0A0D0BH06_9AGAM Unreviewed; 911 AA.
AC A0A0D0BH06;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=CY34DRAFT_801597 {ECO:0000313|EMBL:KIK45397.1};
OS Suillus luteus UH-Slu-Lm8-n1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Suillineae; Suillaceae; Suillus.
OX NCBI_TaxID=930992 {ECO:0000313|EMBL:KIK45397.1, ECO:0000313|Proteomes:UP000054485};
RN [1] {ECO:0000313|EMBL:KIK45397.1, ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|EMBL:KIK45397.1,
RC ECO:0000313|Proteomes:UP000054485};
RG DOE Joint Genome Institute;
RA Kuo A., Ruytinx J., Rineau F., Colpaert J., Kohler A., Nagy L.G.,
RA Floudas D., Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C.,
RA LaButti K., Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C.,
RA Sun H., Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA Nordberg H.P., Cantor M.N., Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UH-Slu-Lm8-n1 {ECO:0000313|Proteomes:UP000054485};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) 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; KN835173; KIK45397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0BH06; -.
DR STRING; 930992.A0A0D0BH06; -.
DR HOGENOM; CLU_004109_4_0_1; -.
DR InParanoid; A0A0D0BH06; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000054485; 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:UP000054485};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001174}.
FT DOMAIN 9..212
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 705..895
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 254..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 800
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 843
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 428..435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 911 AA; 99258 MW; 571FA627FBEE8B7D CRC64;
MAVMGSPKLP VLLLPHPLIL LPNARLTLPI SRSLADAILS LLDDSDAVLA AIPLPAHDSP
SEVTYGTAAR IARLVRPRNQ SSPTQPYLLS LHGIQRIRFP SPIQIDQLDT LPVHNVVYPS
SEGTPSRDTV EAFKQAALIL LDRLAKDSAQ PQRKDDWLRV AAIVEDISEQ RAAWMADVLV
AAVSPQYPDK LAFLAAADVE DRLRHATELF VKQSSIQEVS KKIASAVDES FSRQQKEYFL
RQQLAAIQRE LQSLQSSPTS VGPGFGTGGA TSELDDDDQA DADDLADLRR KIEALDVSSE
ERKVGVREWR RLKRIPQGSV ENGVIRSYLE WLTSVPWPSN STTAPLDVLR DRSFLTRARA
QLDADHYGLD QIKRRLMEYL AVVRLRALAD AAQTQAQGDT PSTGASPSAV LTSTKGKSVK
GPILLFVGPP GTGKTSLGQS IAKALGRPFQ RISLGGVRDE AEIRGHRRTY VASGPGSIVQ
ALRKAGRNDP VILLDEVDKV GHSNFHGDPA AALLEVLDPE QNHSFNDHYI NVPIDLSQVL
FICTSNTLDT ISAPLLDRCE VVELSGYTYD EKMHIAKRFL LPKQICANGL SDSQLTLTDD
ALLHVATMYT REAGVRSLER AIGAVVRFKA VEWAEWLDKG NGSDGGECNA NVSGNGNKKP
NENEKQDGNA NENGVGNEWR ATVEPNELEK ILGIPRWDGE ERDREEKRGV VYGLVVTGMG
EGGILPVEST ALPGTGRLKL TGSLGDVIKE SGEIALSWVK THAFELGITA GRGVDPLKVP
DVIDVHLHLP AGAQKKDGPS AGIAMICAFV SLLSGACVPK DIAMTGEITL RGRVTPVGGI
RMKVLGAHRA QIRKVILPWA NRKDVEHDVA LEVRREMQFF FVRTIDEALE AAFGRGALGW
RKETILLESR L
//