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Database: UniProt
Entry: A0A0D0BH06_9AGAM
LinkDB: A0A0D0BH06_9AGAM
Original site: A0A0D0BH06_9AGAM 
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
//
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