ID A0A316YGM7_9BASI Unreviewed; 1161 AA.
AC A0A316YGM7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Lon protease homolog {ECO:0000256|RuleBase:RU000592};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU000592};
GN ORFNames=FA10DRAFT_269057 {ECO:0000313|EMBL:PWN87758.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN87758.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN87758.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN87758.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR EMBL; KZ819639; PWN87758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316YGM7; -.
DR STRING; 215250.A0A316YGM7; -.
DR InParanoid; A0A316YGM7; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000245768; 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; 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; 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; 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 PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU000591};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122,
KW ECO:0000256|RuleBase:RU000591};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000591};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000245768};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 942..1129
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 391..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 1077
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01122"
SQ SEQUENCE 1161 AA; 124937 MW; 8708FFA3D4CC3BF3 CRC64;
MTDTIVVPDR LPVLPLPYPL VLHPSLLLSI PLSYAHSLSL LKAALQLTHS DRSSSGSNSG
AGNGGKTVDA HKPIIVACVP TLRAPSSPSP NQGARDVARR KHITVHNESE GDDNDRDGAK
VRKEEEDLRV RINDLFDWGC AARLVRLTRH PASQTCTLVV TGLTRVRVDR WLSVRAPLTS
TALDSARNLT VPDVPVPLAA VTPFADGAVR HNADDVAQLR RAAQDVIEAL ALSSPSTSAA
AVNKTQQQPP PAADPTASTL ALPLLPAALL KRLRTFVADA SDGQAGLLAD VLVGTLGGSC
EWGDRVAVLG DWDAKERVRN AAKVLSNGAA RVRQARELLT SLSAPLNNAS KESLARNQLE
ALLAQLAALN PNISARISTG NTSFSIGTAK GSGGNNDGGN GNNVNGIITI RSPNNVRNDD
ASNNPNGPRP LSAPRRNGNN PFAPPGSRVG GGAGGGAGNN EQDEEQDEVA ELSRKLQAAQ
LSDEARKVCD RELKRLQRIP AQSVERGVVI TYLETMAELP WDKTSADLDE LAAETRAVAT
TTKDVAVVEN DDEEGIVGRA RRILDEDHYG LDKIKKRLVE YLAVLELKTE QAKERLEHEE
RQAKEAAGQA KRSAASANQR GKVEAAKKQQ QQQIDLEGDS ASDDSQIGHL EERGQDEESD
SNKRKAAEER RKGKKRAAVA DKGPILLLVG PPGTGKTSIA RSLASALRRP FTRLSLGGVR
DESEIRGHRR TYVGAMPGSI ASSLRKVGVS DPVMLLDEVD KLGSGNGLHG DPMAAMLEVL
DPEQNFQFMD HYVNCPIDLS RVLFIATANT LETISPPLLD RTEVIHVSGY THDEKVAIAK
QYLLPKQAKA QGLRPNVDIK VDDDVLLKIA MSYTREAGVR SLEREIGAVA RGKAVQFSEA
RKGQLKDKKT GSKIEYDPNV RLEHLEDLLG VETFDPEVAE REARPGVATG LAYQGSGSGG
ILHIESLLLP PGNSSLKLTG KLGDVIRESA ELSLSWVKAH SFQLGIVSER SSEFPKHDIH
LHLPGGAIPK DGPSAGMAMT LALVSLFTRI PIDTKLAMTG EMTLRGQVTP VGGIKEKCLG
AHRAGIRRLI LPLRNRKDVE ADLPKQIRDE LNISYVRTIW QAIEIAFGQR ALLESALKGG
TGNLEGIEEG RRMMELEEAR L
//
