ID E1Z3L7_CHLVA Unreviewed; 757 AA.
AC E1Z3L7;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFN59870.1};
GN ORFNames=CHLNCDRAFT_33715 {ECO:0000313|EMBL:EFN59870.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN [1] {ECO:0000313|EMBL:EFN59870.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN59870.1,
RC ECO:0000313|Proteomes:UP000008141};
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01122}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GL433835; EFN59870.1; -; Genomic_DNA.
DR RefSeq; XP_005851972.1; XM_005851910.1.
DR AlphaFoldDB; E1Z3L7; -.
DR STRING; 554065.E1Z3L7; -.
DR GeneID; 17359389; -.
DR KEGG; cvr:CHLNCDRAFT_33715; -.
DR eggNOG; KOG2004; Eukaryota.
DR InParanoid; E1Z3L7; -.
DR OMA; YVGPPIY; -.
DR OrthoDB; 1103874at2759; -.
DR Proteomes; UP000008141; 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; IPR008268; Peptidase_S16_AS.
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 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.
DR PROSITE; PS01046; LON_SER; 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:UP000008141};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01122}.
FT DOMAIN 1..93
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 551..740
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 465..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 646
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 689
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 757 AA; 81995 MW; 41A718614B283FB6 CRC64;
MHLKEQPYNA SDDMLRATTM EIISTLKELL HMHPLYNEQM RNFIQFGADF HDLSRLADLA
TSLTSGDSAA LQAVLEQLSV PERAHQALVL LKKEVELCRL QADIGKRVEE KISKDQRRYF
LMEQLKSIKK ELGLEKDEKT ALVQKFRERL EPLREHLPEA AEKVIEEELE KLQAIEPASS
EFNVTRNYLD WLTSIPWGQH SQEKLEVTAA KQVLDEDHYG LEDVKDRILE FIAVGKLRGS
TQGKILCLVG PPGVGKTSIG RSIARALNRK YYRFSVGGLS DVAEIKGHRR TYVGAMPGKM
VQCLKTTGTS NPFVLIDEID KLGRGYQGDP ASALLELLDP EQNSGFLDHY LDVPVDLSKV
LFMCTANVLD TIPGPLLDRM EIIRLSGYIF DEKVAIARTY LEPQARTNAG VPEGAVRVTD
AALAALVDDY AREAGVRNLK KQLEKIYRKA ALKLVTMGVV PEAAAAPPSD QQQQQAAAAA
AAAEGEAGAA GSSSSPSSEN DGGSRAQQLA ESAEGAAATA LAEPLIVIDG GDLKEYVGQP
PYPTDKIYAE GTPVGVVMGL AWTALGGSTL YVEAARVERG EGKGSLKTTG QLGDVMKESA
AIAHTFARKF LEQAAPSMQG QAAAFFADHA IHLHVPAGAT PKDGPSAGCT IITALLSLAL
DRPVLPDLAM TGEVTLTGKV LPIGGVKEKT LAARRSGVRH LVFPEGNRRD WEELTEDVKA
GLDPHFVSHY DQIYALAFGD EAASPRQQQE AAAATAA
//
