ID K1VBM4_TRIAC Unreviewed; 711 AA.
AC K1VBM4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=Lon protease homolog {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1Q2_07507 {ECO:0000313|EMBL:EKC98175.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98175.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC98175.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98175.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
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:EKC98175.1}.
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DR EMBL; AMBO01000395; EKC98175.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VBM4; -.
DR STRING; 1220162.K1VBM4; -.
DR eggNOG; KOG2004; Eukaryota.
DR HOGENOM; CLU_004109_2_0_1; -.
DR InParanoid; K1VBM4; -.
DR OMA; VLDCVPM; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000006757; 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; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 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 SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR001174-2};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR001174-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 1..52
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 501..688
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 420..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 593
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 636
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 711 AA; 78339 MW; AF1A34AACBE6A4B9 CRC64;
MSNSAANVFD EPDKLADFAA AVSTGDVEDL QAVLESLSLE DRLQKALLIL KKELINAQLQ
SKISRDVESK IQKRQREYYL MEQLKGIKKE LGMESDGKDK LVERFKEKAG KLAMPDGVKK
VFDEELNKLM HLEPAASEFN VTRNYLDWLT AIPWGVHSPE NFNIAHASKV LDEDHYGLKD
VKDRILEFLA VGKLRGTVEG KIICLAGPPG VGKTSIGKSI ARALGRQFFR FSVGGLTDVA
EIKGHRRTYI GAMPGKPIQA LKKVAVENPL ILIDEVDKIG RGHNGDPASA LLEMLDPEQN
KSFLDHYMDV PVDLSRVLFV CTANVLDTIP APLLDRMEVL EVNGYVAAEK MNIAEKYLSP
QAKEASGLKD VDIELDPEAI ESLIRWYCRE SGVRNLKKHI DKIYRKAAFK IVDDLGETAL
PEPDAKETAN SVETQEADVK PASERLPGDE QGTEPDRVNV TTAVREPLKI PDSVQIRVNK
ENLKDYVGPP VYHKDRLYSK TPPIGVSTGL GYLGNGSGSV MPIEVTSMPG KGALQLTGKL
GEVIRESAQI ALSWVKANAF LLGITKSEAD LTMNDRDIHL HMPEGAIGKE GPSAGTAILT
AFVSLFTRTP VDPDIAMTGE VTLNGKVLPV GGLKEKILAA HRSGIKKLLL PIACKSDVDE
NVPKSVKDGI EFVFVDDVTQ VLHEVFHNSK IEQDRWRETL PVEEEAVREK Y
//