ID A0A2K6VNG4_ONCVO Unreviewed; 615 AA.
AC A0A2K6VNG4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Leuk-A4-hydro_C domain-containing protein {ECO:0000313|EnsemblMetazoa:OVOC1285.1};
OS Onchocerca volvulus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=6282 {ECO:0000313|EnsemblMetazoa:OVOC1285.1, ECO:0000313|Proteomes:UP000024404};
RN [1] {ECO:0000313|Proteomes:UP000024404}
RP NUCLEOTIDE SEQUENCE.
RA Cotton J., Tsai J., Stanley E., Tracey A., Holroyd N., Lustigman S.,
RA Berriman M.;
RT "Genome sequencing of Onchocerca volvulus.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:OVOC1285.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (FEB-2018) to UniProtKB.
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; CMVM020000034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2K6VNG4; -.
DR STRING; 6282.A0A2K6VNG4; -.
DR EnsemblMetazoa; OVOC1285.1; OVOC1285.1; WBGene00238094.
DR EnsemblMetazoa; OVOC1285.2; OVOC1285.2; WBGene00238094.
DR OMA; CTALQWM; -.
DR Proteomes; UP000024404; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblMetazoa.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:EnsemblMetazoa.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043171; P:peptide catabolic process; IEA:EnsemblMetazoa.
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:UP000024404};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634015-3}.
FT DOMAIN 468..613
FT /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT C-terminal"
FT /evidence="ECO:0000259|SMART:SM01263"
FT ACT_SITE 300
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 389
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 140..142
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 270..275
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 569..571
FT /ligand="a peptide"
FT /ligand_id="ChEBI:CHEBI:60466"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-2"
SQ SEQUENCE 615 AA; 70116 MW; F699B97E675CEA58 CRC64;
LFNIMHQFIS EIMYDPSSSA NINEATIDHF SLDWIIDFCK SQISGSVILS IRIIKPTDQI
ILDSQSLEII NIKLDDEIVN YRAENAGVLG EKIIIDVGKQ KDGDKLNLSI SYKTGEKCSA
LQFLKAEQTV TKKKPYLFSQ CQSIHARSIV PCMDTPAVKQ TYNAVVAVPS DLICLMSAIA
VGQPEEVGKL TKYSFKQSIR IPSYLLAIVV GLMEKRDLSV RCAIWAEPKI IDEAFYEFGE
TEKMLQTAEN LVGKYQWERY DLVVLPSSFP FGGMENPCLT FVTPTLLAGD RSAAYVIAHE
ISHSWTGNLV SNANWEHFWL NEGFTTFLER KIIGKLEGEK QRHFESQCGW EDNLLSAVKE
QYFDDHPFTK LIPDLQNKDP EDAYSLIPYE KGSALLMILE QQLGVTEFDE FLKKYIEKFA
QKSIVTDDWK AFLYEYFSDK KNVLDGIDWN NWLHGTGIPK TKPQFDDTAM HEAVSLAEEW
MSMADSEIMN IDKTKYLSLS TLQKVKVLSH LRLAKERLSH IKLARLDEVN QFSKIGNCDI
LSSWIQLCLK NYWKPIIPVA LDFVTQQGRI KYVRLIYKDL FLWSESAGRA IETFTKNAPS
MHPITVSVVA KLIPK
//