ID A0A267G8T9_9PLAT Unreviewed; 861 AA.
AC A0A267G8T9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Lon protease homolog {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=BOX15_Mlig025870g2 {ECO:0000313|EMBL:PAA82396.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA82396.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA82396.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA82396.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA82396.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:PAA82396.1}.
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DR EMBL; NIVC01000474; PAA82396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267G8T9; -.
DR STRING; 282301.A0A267G8T9; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 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 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; 2.
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; 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 Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01122};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01122}; Reference proteome {ECO:0000313|Proteomes:UP000215902};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 21..246
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 639..828
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 252..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..861
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 732
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 775
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PAA82396.1"
SQ SEQUENCE 861 AA; 91685 MW; A9F0A08CF06DBBE2 CRC64;
IAKSIFMTAQ PNNKPEEEAE LPALIIGGDA CILPFELARI PIGNSQDCKA IAASLKLDGA
KHLVATFTSH DADDSETKLA GRIGTVCAVQ QLLLLPSPSL VLRGLSRCRF HAWVSGSNST
QVGRRFFWSQ QPQQQQSPRR ARVAMLTSDV EEVDAEATAE ELRQLISLCQ RLGVLRASPT
SAAASEAAAA AEDASDIKDG ERKRLASQLP DLLGGLLSLS TEQRLRLLAA TTHRERAAVL
LPILRSRLRD KTGDAAAANS SSPTSSPRAG GGPIGELASR LAAADLPKAA SEAANRELAR
LRSITSGAQH HHPEAGVIQT YLETLLALPW RRLTPPDAGP ATMADARRLL DAEHHGLASV
KERVLQFLAV RRLRPSLRPP LLCLVAPPGC GKTSVAGSLA RCLGRPLQRI ALGGVADAAE
LRGHRRTYVG AMPGRLLAAV RAAGVRDPVL LLDELDKLGR RGMHGDPSAT LLEALDAEQN
SAFVDHYLGV PFDLSQVLFV ATANTIDSIP PALLDRFELV HFDPLSRSDK VRIATDHLLP
KQLSQHGLEP GSVLLREAEL LRVIDAYTRE AGVRQLERRL ARLCRHAALL AAEAPPSEPL
RVDADVLRQI FEEADGADCR PTPSPYEQMT MSAANSGAPL EPGVCPVLAV TPHGGEVLLL
ECGWTLEPAV DGGGQTTDLA PVCTGQVGEV MRESVTLCIS WLSSRLNSQL RRNRCRLHVH
FPSGAVPKDG TSAGLPLAAA LTSLASGTPV RAGVALTGEV TLRGRVLAIG GVPAKLEAAA
RAGLHSVVLP MANRIEATRT AGRLGLAGRL RLHCVETVDQ ALRFALEPAA GHRGLGDWPA
LPIKDEDSTE DREALSARPK L
//