ID YME1_CAEEL Reviewed; 723 AA.
AC P54813;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 27-MAR-2024, entry version 150.
DE RecName: Full=ATP-dependent zinc metalloprotease YME1 homolog;
DE EC=3.4.24.- {ECO:0000250|UniProtKB:Q96TA2};
GN Name=ymel-1; ORFNames=M03C11.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: ATP-dependent metalloprotease that catalyzes the degradation
CC of folded and unfolded proteins with a suitable degron sequence in the
CC mitochondrial intermembrane region (By similarity). Plays an important
CC role in regulating mitochondrial morphology and function (By
CC similarity). {ECO:0000250|UniProtKB:Q96TA2}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q96TA2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q96TA2};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q96TA2}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q96TA2}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
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DR EMBL; Z49128; CAA88955.2; -; Genomic_DNA.
DR PIR; T23690; T23690.
DR RefSeq; NP_499298.2; NM_066897.3.
DR AlphaFoldDB; P54813; -.
DR SMR; P54813; -.
DR BioGRID; 41652; 6.
DR STRING; 6239.M03C11.5.2; -.
DR MEROPS; M41.A11; -.
DR TCDB; 3.A.29.1.2; the mitochondrial inner membrane i-aaa protease complex (mimp) family.
DR EPD; P54813; -.
DR PaxDb; 6239-M03C11-5-2; -.
DR PeptideAtlas; P54813; -.
DR EnsemblMetazoa; M03C11.5.1; M03C11.5.1; WBGene00010842.
DR UCSC; M03C11.5.1; c. elegans.
DR AGR; WB:WBGene00010842; -.
DR WormBase; M03C11.5; CE43540; WBGene00010842; ymel-1.
DR eggNOG; KOG0734; Eukaryota.
DR GeneTree; ENSGT00550000074836; -.
DR HOGENOM; CLU_000688_19_2_1; -.
DR InParanoid; P54813; -.
DR OMA; WNQYESD; -.
DR OrthoDB; 9585at2759; -.
DR PhylomeDB; P54813; -.
DR PRO; PR:P54813; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00010842; Expressed in adult organism and 4 other cell types or tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
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 HAMAP; MF_01458; FtsH; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF37; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..723
FT /note="ATP-dependent zinc metalloprotease YME1 homolog"
FT /id="PRO_0000084665"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 510
FT /evidence="ECO:0000250|UniProtKB:P0AAI3"
FT BINDING 288..295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 509
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AAI3"
FT BINDING 513
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AAI3"
FT BINDING 587
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P0AAI3"
SQ SEQUENCE 723 AA; 79831 MW; 80D3179C811E843D CRC64;
MQSAINLNIG GLLQNTGLLR NSRNGINRKP LDIEATAASL SRVYHQVWRQ FSSDTSSPVT
INQMNNILRD STLSRRIARK SEISLNYDDA VVRIIPASSS FYIQRRGFRT RKQTFGVGNA
GKPTQDEVKS PLTYFSELLA GKKQKTSEGG VEKWNQYESD LKKLPENQQR TYTDGFVKGL
LSNGVSGAGK DGKKSNTLTR FYIFLVFCIF FGYLTGRIRV RVGDRQIGSL FFSNPQEVNP
EDVQVTFDDV RGMDEAKLEV EEIVDYLKDP EKYSRLGGRL PKGVLLVGPP GTGKTLLARA
IAGEAQVPFF HTAGSEFDEV LVGQGARRVR DLFDKAKARA PCIIFIDEID SVGSKRVSNS
IHPYANQTIN QLLSEMDGFT RNEGIIVIAA TNRVDDLDKA LLRPGRFDVR VTVPKPDLAG
RVDIFNFYLS KIVHSGGIDP KVLAKGSTGF TGADIENMVN QAALKAATDN AVEVTMAYLD
EARDRVLMGP ARTGGRIPDE EANRNTAYHE AGHTLVSLYT KDATPLHKVT IIPRGQSLGH
TAMLPEKDSY QLTKAQMLAT LDVMMGGRVA EELIFGDDKV TTGAADDLSK ATQLAVQMVK
VFGMSDKVGL RDFTAQDNES ALVKVSDLAP QTAELIDAEI NRVLQESYKR AKVILETKKK
EHQLLAEALL EYETLSADEV KRVISGQKIK RPTPAAVKKS NETKRNQPSL VLHLFEEEGR
GKQ
//
