ID G5EGR7_CAEEL Unreviewed; 388 AA.
AC G5EGR7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 3.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=AAA_lid_3 domain-containing protein {ECO:0000313|EMBL:CCD73339.3};
GN ORFNames=CELE_Y47C4A.1 {ECO:0000313|EMBL:CCD73339.3}, Y47C4A.1
GN {ECO:0000313|EMBL:CCD73339.3, ECO:0000313|WormBase:Y47C4A.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD73339.3, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD73339.3, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD73339.3,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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DR EMBL; BX284606; CCD73339.3; -; Genomic_DNA.
DR AlphaFoldDB; G5EGR7; -.
DR SMR; G5EGR7; -.
DR STRING; 6239.Y47C4A.1.1; -.
DR MEROPS; M41.A12; -.
DR PaxDb; 6239-Y73B3A-21; -.
DR PeptideAtlas; G5EGR7; -.
DR EnsemblMetazoa; Y47C4A.1.1; Y47C4A.1.1; WBGene00021615.
DR AGR; WB:WBGene00021615; -.
DR WormBase; Y47C4A.1; CE53586; WBGene00021615; -.
DR eggNOG; KOG0731; Eukaryota.
DR GeneTree; ENSGT00940000156329; -.
DR HOGENOM; CLU_1166753_0_0_1; -.
DR InParanoid; G5EGR7; -.
DR OrthoDB; 9585at2759; -.
DR PhylomeDB; G5EGR7; -.
DR Proteomes; UP000001940; Chromosome X.
DR GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
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:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF8; PARAPLEGIN; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 64..118
FT /note="ATPase AAA-type core"
FT /evidence="ECO:0000259|Pfam:PF00004"
FT DOMAIN 148..186
FT /note="AAA ATPase AAA+ lid"
FT /evidence="ECO:0000259|Pfam:PF17862"
FT DOMAIN 203..371
FT /note="Peptidase M41"
FT /evidence="ECO:0000259|Pfam:PF01434"
SQ SEQUENCE 388 AA; 43498 MW; 3E872F4DD63FAB02 CRC64;
MSDMMSNMTK GKFTIIDPHS VEGKKQLKIK FKDVAGCSEA KVEIREFVDY LKNPGRFTVG
ISGGSGEEEQ TLNQLLVEMD RMGSGNGAVV VLASTNRADV LDKALLRPGR FDRHISIDLP
TVLERKDMFE LYMRKIKLDH APQEYSQRLA VLTPSFTGAD IMNVCNESAI RAASNKCHVV
TIKDMEYALD RVLAGSEKRS RSLVEEEREV VAYHEAGHAL VGWMLEHTDA LLKVTIIPQT
SAALGFAQYS PRDDKHLYSK DELFDRMCMM LGGRCAENLK FGRITSGAQD DLQKMTKSAY
AQVKLYGMSS IVGPLSFPNT ERFQIKPYLK KFASTFDQEA TLIVAKANEA TTDLIKNNMD
KLETVCARLL SIGGEYCNKY SQTRESWR
//
