ID W6NCZ0_HAECO Unreviewed; 1265 AA.
AC W6NCZ0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Leucine-rich repeat and Immunoglobulin I-set and Haem peroxidase domain containing protein {ECO:0000313|EMBL:CDL94720.1};
GN ORFNames=HCOI_01481400 {ECO:0000313|EMBL:CDL94720.1};
OS Haemonchus contortus (Barber pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6289 {ECO:0000313|EMBL:CDL94720.1};
RN [1] {ECO:0000313|EMBL:CDL94720.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISE/inbred ISE {ECO:0000313|EMBL:CDL94720.1};
RA Aslett M.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDL94720.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISE/inbred ISE {ECO:0000313|EMBL:CDL94720.1};
RA Laing R., Kikuchi T., Martinelli A., Tsai I.J., Beech R.N., Redman E.,
RA Holroyd N., Bartley D.J., Beasley H., Britton C., Curran D., Devaney E.,
RA Gilabert A., Jackson F., Hunt M., Johnston S., Kryukov I., Li K.,
RA Morrison A.A., Reid A.J., Sargison N., Saunders G., Wasmuth J.D.,
RA Wolstenholme A., Berriman M., Gilleard J.S., Cotton J.A.;
RT "The genome and transcriptome of Haemonchus contortus: a key model parasite
RT for drug and vaccine discovery.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hypobromite + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-
CC [protein] + H2O; Xref=Rhea:RHEA:69356, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29250, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC Evidence={ECO:0000256|ARBA:ARBA00033700};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69357;
CC Evidence={ECO:0000256|ARBA:ARBA00033700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O;
CC Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:166867; Evidence={ECO:0000256|ARBA:ARBA00033691};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66021;
CC Evidence={ECO:0000256|ARBA:ARBA00033691};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + H(+) + H2O2 + L-tyrosyl-[protein] = 3-bromo-L-
CC tyrosyl-[protein] + 2 H2O; Xref=Rhea:RHEA:69360, Rhea:RHEA-
CC COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:183512;
CC Evidence={ECO:0000256|ARBA:ARBA00033621};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69361;
CC Evidence={ECO:0000256|ARBA:ARBA00033621};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bromide + H2O2 = H2O + hypobromite; Xref=Rhea:RHEA:66016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:29250; Evidence={ECO:0000256|ARBA:ARBA00033705};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66017;
CC Evidence={ECO:0000256|ARBA:ARBA00033705};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hypobromite + L-lysyl-[collagen] + L-methionyl-[collagen] =
CC [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H(+) + H2O;
CC Xref=Rhea:RHEA:66024, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949,
CC Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15858, ChEBI:CHEBI:16044, ChEBI:CHEBI:29250,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:166867;
CC Evidence={ECO:0000256|ARBA:ARBA00033612};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66025;
CC Evidence={ECO:0000256|ARBA:ARBA00033612};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDL94720.1}.
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DR EMBL; CAVP010058471; CDL94720.1; -; Genomic_DNA.
DR AlphaFoldDB; W6NCZ0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0140825; F:lactoperoxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09826; peroxidasin_like; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR034824; Peroxidasin_peroxidase.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF58; PEROXIDASIN; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF01462; LRRNT; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00364; LRR_BAC; 3.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR619791-2};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:CDL94720.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 306..392
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 399..486
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT BINDING 963
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 1265 AA; 142543 MW; B391E5B176399E06 CRC64;
MLFLLLGLLT WAEAQSICPS QCNCTDTVVD CSHKGLGAFP TELPPSTITL NLRGNSIGRL
SIDDVRGLSH LETLIVSENN IRSVEENFLD YLPLLRRISL ARNKLRFLPS LAAQNSRLIS
LDLRHNEIET ADVQAFSYLP SLIQLDLAHN RLQSLPQMTF AKNKRLVTLK LHRNPWNCDC
RILNIGSLAM GKAKPMEEAR CFNPPNLRGK TLSSIKASDV PCAEPIVVEK EFNSILECTA
TGGGEIHWLF NNIDLDFSSA DSYQVTVNGS LIIPKGSPTQ GFTCTADYGA VPRRTLRQTS
SSGRRPQFTF KPKDSSYREG TAVKLHCEVI GDPRPTIVWY HRRQPIVNSR KHELINANSI
LKIYPFLEND VGSYTCIASN IHGRIEHTAR IHLVSSVPPN IYDGPSPQTV KLGQEVTFAC
RARGVPRPEI TWFYEGSVIP HIKGRFRVSD DGTELTITKV NRQDEGVYSC MAGNSVGAMM
ADAKLTVEGD FARTVDAFID DATLRSISTQ ARDNVNRAVD NTRIQLSQDR VSDPEDLKRL
FRFSIPAQAV ELSKARDIYE ESVRLVHEHI QRGLRLPVDK LAPKNVSYEA VLAPSHVQTL
MELSGCQTGQ FKSACNDLCF HNKYRSYDGQ CNNFEHPMWG VSQMPLLRLL PPIYENGFST
PVGWERGRLY YGYPKPNPRD VSRLLVATES ITPHSYLSAM VMQWGQFIDH DLTHTAMALS
RQSYSSGAIC NKTCENLDPC FNIPLSPSDP KLHTGVHQKY PCIEFERSGA VCGSGETSLI
FQRVTYRDQM NIITSYLDGS MIYGSTEVQA LELRDLFGDH GLLRFDIVST GQKPYLPFER
DSDMDCKRNF SQENPIRCFL AGDLRANEQL GLTAMHTLFL REHNRIAAKL LELNVNWDGE
TIFQEARKIV GAIIQHITYS EWLPTVLGKI GYNEMIGDYG GYNPHVDPSI SNAFATAAFR
FGHTLINPTL FRYDKDFNPI KDGHISLHKA FFAPERLLAE GGIDPLVRGL FASPLKMPMP
SQLLNMELTE KLFDRFHEVA LDLAVMNIQR GRDHGLPGYT EYRRFCNLSV PQTWDDLAAD
VPDASVRAKM RSLYGDPANV DLWVGGIAEQ RLPDALMGPT FACIIGDQFR RLRDGDRFWY
ENDGIFTKLQ LQQIKKASLA RIFCDNGDSI DRVQRNVFFY PGNSTKQYGR CENIPEINLN
MWMNCCDTSC SLSSPTSSRK RRAHNSCDVN GERRHHGDHW SEDKCTTCKC DHGKVWCSVR
EHCHD
//
