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Database: UniProt
Entry: E3LZB4_CAERE
LinkDB: E3LZB4_CAERE
Original site: E3LZB4_CAERE 
ID   E3LZB4_CAERE            Unreviewed;       735 AA.
AC   E3LZB4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=CRE-YMEL-1 protein {ECO:0000313|EMBL:EFO86711.1};
GN   Name=Cre-ymel-1 {ECO:0000313|EMBL:EFO86711.1};
GN   ORFNames=CRE_04597 {ECO:0000313|EMBL:EFO86711.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; DS268419; EFO86711.1; -; Genomic_DNA.
DR   RefSeq; XP_003110879.1; XM_003110831.1.
DR   AlphaFoldDB; E3LZB4; -.
DR   STRING; 31234.E3LZB4; -.
DR   MEROPS; M41.A11; -.
DR   EnsemblMetazoa; CRE04597.1; CRE04597.1; WBGene00078742.
DR   eggNOG; KOG0734; Eukaryota.
DR   HOGENOM; CLU_000688_19_2_1; -.
DR   InParanoid; E3LZB4; -.
DR   OMA; WNQYESD; -.
DR   OrthoDB; 9585at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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   PANTHER; PTHR23076:SF97; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        197..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          276..413
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   735 AA;  81800 MW;  03A1008BF63D1B0D CRC64;
     MQAVNLNIGG LLQNTGLLRS RNGISRKPLD IDKTATSLCR IYYSVWRQFS TATPSEISKM
     SQNLRDSMLT RRMARKSEIF LNYDDAMIRI VPSTSSFYVQ RRGFRTRKQT FGVGNPGKTQ
     EEEVKSPLTY ISELLVGKKV KTSEGGVEKW NQYESDLKKL PEGQQRTYTD GFVKGLLSNG
     TSGAGKDVKK SSTLTRFYIF LVFCIFFGYL TGRIRVRVGD RQIGSLFFSN PQEVNPEDVQ
     VTFDDVRGMD EAKLEVEEIV DYLKDPEKYS RLGGRLPKGV LLVGPPGTGK TLLARAIAGE
     AQVPFFHTSG SEFDEVLVGQ GARRVRDLFD KAKARAPCII FIDEIDSVGS KRVSNSIHPY
     ANQTINQLLS EMDGFTRNEG IIVIAATNRV EDLDKALLRP GRFDVRVTVP KPDLAGRVDI
     FNFYLSKIVH NGAIDPNILA KGSTGFTGAD IENMVNQAAL KAATDNAVEV TMAYLDEARD
     RVLMGPARTG GRIPDEEANR NTAYHEAGHT LVSLYTKDAT PLHKVTIIPR GQSLGHTAML
     PDKDSYQLTK AQMLATLDVM MGGRVAEELI FGEDKVTTGA ADDLSKATQL AIQMVKVFGM
     SDKVGLRDFT AEDRDSSLVK VSDLSPQTAE LIDGEINRVL QESYKRAKVI LETKKVYIRV
     SDIYLFFNSF QKEHQLLAEA LLEYETLSAD EVRRVISGQK IKRPTPAAVK KSNEMRKNQP
     SLVLHLFEEE GRGKQ
//
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