ID A0A1I7XUB7_HETBA Unreviewed; 776 AA.
AC A0A1I7XUB7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Leishmanolysin-like peptidase {ECO:0000256|RuleBase:RU366077};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366077};
OS Heterorhabditis bacteriophora (Entomopathogenic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heterorhabditidae;
OC Heterorhabditis.
OX NCBI_TaxID=37862 {ECO:0000313|Proteomes:UP000095283, ECO:0000313|WBParaSite:Hba_20937};
RN [1] {ECO:0000313|WBParaSite:Hba_20937}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601577-2,
CC ECO:0000256|RuleBase:RU366077};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601577-2,
CC ECO:0000256|RuleBase:RU366077};
CC -!- SIMILARITY: Belongs to the peptidase M8 family.
CC {ECO:0000256|ARBA:ARBA00005860, ECO:0000256|RuleBase:RU366077}.
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DR AlphaFoldDB; A0A1I7XUB7; -.
DR WBParaSite; Hba_20937; Hba_20937; Hba_20937.
DR Proteomes; UP000095283; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042302; F:structural constituent of cuticle; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.90.132.10; Leishmanolysin , domain 2; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR002486; Col_cuticle_N.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001577; Peptidase_M8.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR PANTHER; PTHR24637:SF315; CUTICLE COLLAGEN 40; 1.
DR Pfam; PF01484; Col_cuticle_N; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00328; His_Phos_2; 1.
DR Pfam; PF01457; Peptidase_M8; 1.
DR SMART; SM01088; Col_cuticle_N; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366077};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601577-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|PIRSR:PIRSR601577-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366077};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601577-2}.
FT TRANSMEM 17..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..68
FT /note="Nematode cuticle collagen N-terminal"
FT /evidence="ECO:0000259|SMART:SM01088"
FT REGION 85..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-1"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 487
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
SQ SEQUENCE 776 AA; 83348 MW; B7C92281038B2349 CRC64;
MGDEKTKLVE AESLKRLAFF GIAISTVATL TAIVAVPMLY NYMQHVQSSL QNEVDFCRHR
TDGLWDEFHR FESMKGVDSR IKRQAWNNRP ARARGTGTYS QGGGGGGGYD TGVSGGGGGG
GSCCSCGIGA AGPPGPPGAD GHPGQDGSPG NAGAPGADAE AGAAPKADDF CFDCPPGPPG
PAGNAGPPGP PGSDGAPGQS PPSSSSGPPG PAGPPGPPGN DGQPGAPGNP GAPGQVTEVP
GTPGPAGPPG PPGPPGPAGN PGSGGSSQPG PPGPAGDPGP DGAPGNPGAP GAPGDIGLKL
AITNLTGIVS VLRYSNEKIS YEEISKCSAD FGKDKKAVVN GAELDIKIGK AIRLKKYNFV
LLIERESVIC KNDPTLLAFA TPCHLQANMR PIVGKLNICA GIRWKGFKGV TDLFRHEILH
SLGFGTLVSK NLSGVDGEMY KWEDGVEWQA ARRWFMDFAD TALVEARRHF NCSDLNGIEA
DSIDRIHLNE YLFGNELMTP KLSNLANHFT TISALILEQT YYGSRQWYLV NRTAIDIEEQ
GFWFGRGWGC IFAKRSCYEY IRQRERENKS PFPFCAKENY KMDQRIEVTV STRDGKIRTF
KSKCSTHERR KMNKADNGIM MLLIFLIFMA SHIFANDDIP TTPVIPVTPR TIKSNDKLLF
VQVVWRHGDR APVKSYPTDI HQEDAWPHGW GELTQVDLGM RQQYALGRLL RNRYMNGTNA
LLDRNYNPKQ VYIRSTDVNR TLVSAYANLA GMFEEGQAGK DYPEYHKYDH INNNKL
//
