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Database: UniProt
Entry: A0A1X2IAF0_9FUNG
LinkDB: A0A1X2IAF0_9FUNG
Original site: A0A1X2IAF0_9FUNG 
ID   A0A1X2IAF0_9FUNG        Unreviewed;       849 AA.
AC   A0A1X2IAF0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=BCR42DRAFT_419909 {ECO:0000313|EMBL:ORZ12756.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ12756.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ12756.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ12756.1,
RC   ECO:0000313|Proteomes:UP000193560};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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}.
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:ORZ12756.1}.
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DR   EMBL; MCGE01000018; ORZ12756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2IAF0; -.
DR   STRING; 90262.A0A1X2IAF0; -.
DR   OrthoDB; 1103874at2759; -.
DR   Proteomes; UP000193560; 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; 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; IPR004815; Lon_bac/euk-typ.
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; 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; 1.
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:UP000193560};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|PIRNR:PIRNR001174}.
FT   DOMAIN          8..245
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   DOMAIN          647..834
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   REGION          46..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        739
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        782
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01122"
FT   BINDING         404..411
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ   SEQUENCE   849 AA;  94530 MW;  372477E81E6BF8EE CRC64;
     MVDLPNSLLV VSLANKVLLP LVVLKLTLKG KDVTAMTRIH SKLTEQRKPM YLPTSNQPDI
     NVTERKASKE TPSETNLPTT SSTMTDDQLP ISNERDLLHD YGCVARILQV QRFGVDSYTV
     TVEGVLRCKV DQLLFPSSSA QNSTDSTLAK VSYIKAPTTQ ELDDATDELV AFRALSKEFL
     SRMRQLHLPE SLTTQLSKMI DNVSPLDLAD LMVSVIETSH DEKLLMLSTM SVKERLGHGS
     EWMTRQLHIF KISEQIHSNI EGKLNKKQRE FYLRQQLDAI KQELGESDAF SGGKDEDEMT
     QLAKRLDNAH LPKDAEIIAL RELKRIKKLQ SSSNEWSVAR NYLDLIADLP WNKKSDEIVD
     IGRAKLQLDG DHFGLDHVKK RIIEYLSVVK IKGDLKSPII CFVGPPGVGK TSFCKSIAVA
     LSRKFHRISL GGVRDEADMR GHRRTYVGAM PGLIIQGLRK VGVNNPVVLL DEVDKLVHSA
     HHGDPAAALL EVLDPEQNDT FSDHYLNIDF DLSNILFIAT ANTVDTIPEP LLDRMEIIHL
     NGYTFEEKLH IAKAHLLPKQ TVAHGLKPDQ VQMDDQVLLK LAENYTRESG VRTLERTLGS
     VVRAKCVAFA ELRESGKEHN YNPKVDLQDL EDILGIVKFE KELAERSPVP GVVTGLAYSG
     SGNGSILFVE TSKMPGEGKL QLTGSLGDVI KESAQIALTW VKSHAYALKI ASSNDQNIVE
     KYDIHVHFPM GALPKDGPSA GVTLVTSLVS LFSTCHVPST TAMTGEISLR GQILPVGGIK
     EKVISAHRAG IKKIILPYRN RKDVKQDVPE RVQKDIEFVY AKTMWDVLDA ALIISDKEKW
     TTRSYESHL
//
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