ID A0A1A0HBQ3_9ASCO Unreviewed; 1109 AA.
AC A0A1A0HBQ3;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Lon protease homolog 2, peroxisomal {ECO:0000256|HAMAP-Rule:MF_03121};
DE EC=3.4.21.- {ECO:0000256|HAMAP-Rule:MF_03121};
GN ORFNames=METBIDRAFT_41884 {ECO:0000313|EMBL:OBA21318.1};
OS Metschnikowia bicuspidata var. bicuspidata NRRL YB-4993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX NCBI_TaxID=869754 {ECO:0000313|EMBL:OBA21318.1, ECO:0000313|Proteomes:UP000092555};
RN [1] {ECO:0000313|EMBL:OBA21318.1, ECO:0000313|Proteomes:UP000092555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-4993 {ECO:0000313|EMBL:OBA21318.1,
RC ECO:0000313|Proteomes:UP000092555};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., LaButti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of misfolded and unassembled polypeptides in the
CC peroxisomal matrix. Necessary for type 2 peroxisome targeting signal
CC (PTS2)-containing protein processing and facilitates peroxisome matrix
CC protein import. {ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000256|ARBA:ARBA00004253,
CC ECO:0000256|HAMAP-Rule:MF_03121}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_03121, ECO:0000256|PROSITE-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:OBA21318.1}.
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DR EMBL; LXTC01000003; OBA21318.1; -; Genomic_DNA.
DR RefSeq; XP_018711828.1; XM_018857462.1.
DR AlphaFoldDB; A0A1A0HBQ3; -.
DR STRING; 869754.A0A1A0HBQ3; -.
DR GeneID; 30030438; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000092555; Unassembled WGS sequence.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
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:0016558; P:protein import into peroxisome matrix; IEA:UniProtKB-UniRule.
DR GO; GO:0016485; P:protein processing; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03121; lonp2_euk; 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; IPR027501; Lonp2_euk.
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 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.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03121};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03121, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03121};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140, ECO:0000256|HAMAP-
KW Rule:MF_03121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_03121};
KW Reference proteome {ECO:0000313|Proteomes:UP000092555};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_03121}.
FT DOMAIN 12..318
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 871..1093
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 368..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1107..1109
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
FT ACT_SITE 968
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 1011
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 618..625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03121"
SQ SEQUENCE 1109 AA; 120936 MW; 01BBC4A3D1BF987B CRC64;
MPANPDLQPV CLPLYTLDSP LVLLPGILYN VSFPRLKAAA FLARYRTHAA RVPVVQAVLA
EYDFDAAAAG IPVLSPAAAA GIAAFREAEA SVHLLSGEPR DADPAAGLDW LVVAVFPNLA
RISSAAPAQT AATATVCRVV GIADDANTVR LTLQAIVRAV DAERRPEAGA PKRRGGSVAS
TPNERVFAVS WQHESAAVAQ HSAVFQASAT ALFALLNKFV EAYRAALAGA ESSPDMLTLN
PLANALFMQV AGLKDFDKAY ATLQRICGSA AADLAAQLLR LVDLTGAIVP FPSTEKLRIL
QCATLDERTR LAAEIADKMA SVFETVAENS ARATRWYHGE ASNTQKANLV ANQLKSIRVV
LEGLSSKKTP GSALQKQLTR RRNGAGIPLS NGSKGPPGRR GTGPGDGDDD DDDDDDDLHL
IADFIKNRLP RITSISSDSK RLLVKDFRRI KNAQPGNADF HVIRNYLEIV ADMPWDKHVA
RFQSNQEIDI ADARHRLDAD HHGLQHVKTR LLQYLVVLKL LAANAAQEYR DSGMQEAEEA
HRKQQQMDAL KFTRESTNGE SIIVPSQAES KAIQEAKEAA ETEEAQGETT QSSTENDQSV
KSLLVAKINR SPIILLAGPP GVGKTSLAKS IATTLGRNFQ RISLGGVRDE SEIRGHRRTY
IGAMAGSIVQ ALRKSRSMNP VILLDEIDKV VGGHNSGNKA NGDPAAALLE VLDPEQNSQF
VDHFLGFPID LSQVIFICTA NEPHALSRPL LDRLEMIEVG AYDYTEKLVI GSTYLLPRQM
KRNGLPDQDK VLISGNVMKK IILEYTREAG VRNLERTLGT ICRYKAVEYS ESLADPLKVF
QPEVEEFDLP RYIGLPLPSL SNRVVELPIM SSRYGVVNGL SYNTDGSGSV LIFESIGFEG
KGQTSLNMTG RLGEVLMESA KIGLTFIKNA LYKRLLNLED QEVLVKHLNS LEIHMHVPSG
AVQKDGPSAG ITMALLFLSL ILQKPVPSNI AMTGEITLRG LVLPIGGLQE KVLGAHLTGQ
IDKVIVPREN RRDVLEQYVQ KINDPSRLNG LLKDDAAAAF KDLSPEDYFA EKYGVRIVYA
REFWDVIKHV WGEELLANVE HSRLDEYHL
//
