ID   LONH_MIMIV              Reviewed;        1023 AA.
AC   Q5UPT0;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Lon protease homolog;
DE            EC=3.4.21.-;
GN   OrderedLocusNames=MIMI_L251;
OS   Acanthamoeba polyphaga mimivirus (APMV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Imitervirales; Mimiviridae; Mimivirus.
OX   NCBI_TaxID=212035;
OH   NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rowbotham-Bradford;
RX   PubMed=15486256; DOI=10.1126/science.1101485;
RA   Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA   La Scola B., Susan M., Claverie J.-M.;
RT   "The 1.2-megabase genome sequence of Mimivirus.";
RL   Science 306:1344-1350(2004).
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01122}.
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DR   EMBL; AY653733; AAV50523.1; -; Genomic_DNA.
DR   SMR; Q5UPT0; -.
DR   PRIDE; Q5UPT0; -.
DR   Proteomes; UP000001134; Genome.
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:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008269; Lon_proteolytic.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   PANTHER; PTHR10046; PTHR10046; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..1023
FT                   /note="Lon protease homolog"
FT                   /id="PRO_0000076159"
FT   DOMAIN          810..1003
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        906
FT                   /evidence="ECO:0000250"
FT   BINDING         515..522
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1023 AA;  116827 MW;  02FABB4A83F42349 CRC64;
     MTENNYGIRD IKNQHLKYSY KKYTDLIIGF EKHAKRMYDD WVIDINNRNI IMHKLDNLVR
     SMIKIYNECI MEIYNKTPNE NESDNISNTN KKINNAIYNK IYNEINKIER IENKNNKLVD
     SFNSIREQLI ELAKNNGFHT INDFIGLYVG ENYESLFNNL DMETFELYKG VFVPLSISIN
     KIKKKYRDTD KQDTITISKI PSKCDGLIEN TCTVTITMNN IFTEIIFEGY VSADILNAYL
     RTSQIYSKHL FNVKNESKRI VKESYPHVDE YFIAKYAKLI NSNVYFINNP DEMATKIDSD
     YMLFTDLTAK NFNTIVKEFV NSNLPTMFSY INVLLMGSNQ DVNNAGLLFN LLKDRKIGSE
     TLSDIIYHNL SFHLQIKLKK IINSIKNELG KIRSLTPEEI PIEKKLASMV NMPENVKNYI
     IEKNNEIKTG ENNYKLQMAI NGLMQFPWKP KDFNNNNYFQ IKNSVTKSRN YLQNVAKKLN
     ETVFGHENSK KVLIELVGKW IQNPESSGQV IGLVGPPGVG KTLLAKGISA ALGIPLSIVG
     LGGMSDSADL IGHSFTYAGA QYGMIVRQMI KAGNWRSVMF FDEVDKVSKR NDTNEIYNTL
     IHITDPNMNQ NFQDRFYSSA IDFDLSGVLI VFSYNSSEKL DPILLDRIKE IKISPYSLKE
     KILIAQNHVI KELCSNIGFD RDKINIGDDI VEYIIEKYTM EAGVRELKRK LEQILLKVNI
     DRFYMRGPFY NLLKKYNPET QSDDNSHSLE ENQINMYVDY KPSLLEKNSD PNIINKIFNL
     DIDDHIIITK ELVHKYLDKP TLTTEEIHKT NMIGVINGLY ATSVGMGGIV PIQIYKNFVG
     DKNDGSNLKL KITGNQKQVM RESVMCALTT AVNVLNNSIK SKILDKFPHG FHVHAPDGGT
     PKDGPSAGCA FTTAFVSAIL GKKINRHVAM TGEIELTGKI SKIGGLMLTT GAKKAGIKCV
     YICEDNKEDY EIIKKKSPEL FQDGLEIKIV NHIIEIITDP NVIIDIDVND FDKDLISEFK
     KLK