ID E3NN66_CAERE Unreviewed; 573 AA.
AC E3NN66;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Peptidase M1 leukotriene A4 hydrolase/aminopeptidase C-terminal domain-containing protein {ECO:0000259|SMART:SM01263};
GN ORFNames=CRE_24300 {ECO:0000313|EMBL:EFP10186.1};
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|PIRSR:PIRSR634015-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; DS269163; EFP10186.1; -; Genomic_DNA.
DR RefSeq; XP_003090155.1; XM_003090107.1.
DR AlphaFoldDB; E3NN66; -.
DR STRING; 31234.E3NN66; -.
DR MEROPS; M01.025; -.
DR EnsemblMetazoa; CRE24300.1; CRE24300.1; WBGene00073937.
DR eggNOG; KOG1047; Eukaryota.
DR HOGENOM; CLU_014505_1_2_1; -.
DR InParanoid; E3NN66; -.
DR OMA; CTALQWM; -.
DR OrthoDB; 443480at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09599; M1_LTA4H; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM01263; Leuk-A4-hydro_C; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634015-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634015-3}.
FT DOMAIN 466..573
FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT C-terminal"
FT /evidence="ECO:0000259|SMART:SM01263"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 387
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 137..139
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 268..273
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 320
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 564..566
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
SQ SEQUENCE 573 AA; 64183 MW; 879866094CC4A849 CRC64;
MAPPHPRDPS TASNYEQVSV SHYVVKWNVD FDKKCIDGDV QLVLDVKQET SEVILDTREL
TIRSVSCASN GETKEVEYAM KDNGALGQKL IVSTALLKPG DKPVLTVKYE SSNNAAALQF
LTAEQTTDKV APYLFSQCQA INARSIVPCM DTPSVKSTYE AEVCVPVGLT CLMSAIGQGS
KSSECGKHTI FSFKQPVSIP SYLLAIVVGH LERKEISDRC AVWSEPSQAE AALYEFGETE
KILKVAEDLV GPYVWGRYDL VVLPATFPFG GMENPCLTFI TPTLLAGDRS LVNVIAHEIT
HSWTGNLVTN FSWEHFWLNE GFTVFIERKI HGRMYGELER QFESESGYDE SLVRTVNDVF
GPDHEYTKLV QDLGSADPDE AFSSIPYEKG SALLFTVEQT IGDNARFEQF LKNYIQKYAY
KTVSTEEWKE YLYDTFSDKK VILDNINWDL WLHKAGLPPK PEYDSTLMRA CKDLANKWTA
EGSEAPTDGE VFEKMSNSQK LAVIDAIRVN KGIFGDRMPS LTATYKLDQA KNAELKFSWL
MLGLETKWTP IIDASLAFAL AVGRMKYCKP IYK
//
