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YME1_CAEEL
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   03-AUG-2022, entry version 142.
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; 5.
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) familly.
DR   EPD; P54813; -.
DR   PaxDb; P54813; -.
DR   PeptideAtlas; P54813; -.
DR   EnsemblMetazoa; M03C11.5.1; M03C11.5.1; WBGene00010842.
DR   UCSC; M03C11.5.1; c. elegans.
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; 217929at2759; -.
DR   PhylomeDB; P54813; -.
DR   Reactome; R-CEL-8949664; Processing of SMDT1.
DR   PRO; PR:P54813; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00010842; Expressed in adult organism and 4 other tissues.
DR   GO; GO:0005745; C:m-AAA complex; IBA:GO_Central.
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; IEA:InterPro.
DR   GO; GO:0034982; P:mitochondrial protein processing; IBA:GO_Central.
DR   GO; GO:0065003; P:protein-containing complex assembly; IBA:GO_Central.
DR   Gene3D; 1.20.58.760; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   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; SSF140990; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01241; FtsH_fam; 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
 
 
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