ID A0A1I8AUV8_9BILA Unreviewed; 1307 AA.
AC A0A1I8AUV8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Peroxidase {ECO:0000313|WBParaSite:L893_g9747.t1};
OS Steinernema glaseri.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g9747.t1};
RN [1] {ECO:0000313|WBParaSite:L893_g9747.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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};
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DR WBParaSite; L893_g9747.t1; L893_g9747.t1; L893_g9747.
DR Proteomes; UP000095287; Unplaced.
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; 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; 2.
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; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
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};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..43
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 44..1307
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009315123"
FT DOMAIN 336..424
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 429..516
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT BINDING 991
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 1307 AA; 148782 MW; 80F081019D52C7A5 CRC64;
MASSESPPRC SNSARNLPLM ATSARKMRLA LLFFAFFLGA AAAECPRQCD CYPAQKRVDC
RKRGLSRMPE GIPRDTVTLD LRDNQLHHLS IHALRGLPAL ETLLATNNRI HKLDKNLLDA
LPSLNRLYLA RNKISELETL ASHTHRLHTL DAHANKISRI VEGALLHLRS LERVDLRHNL
LQTIDADSVE ALMGAKEFTL GRNHFNCDCR LKKLHLLLEA KKDSTEEEVS CWNPPHLRGR
EIASLEKVHF ECLIAEAMAT ANGHVVSCKT EFHNDVTWIF EGEVMKEELQ DIEVLGNGSL
LVHDDDFDVD DFRCAVQYPS RASKKFRRAL PQRKEPAFTL APRDRTFREG ASVKLNCEAV
GHPKPHIQWF FKGRPIEESL KHDFAKHNSE MVIYPFLKHD EGSYSCVAWN EFGRKEARFQ
LRMTPSSSPR IVDAPISQSV KPGAHVTFRC RAVGSPKPRI TWFFNGVEIA NLKGHLTVSD
DETELTVAHA TRQDHGTYSC MAGNDVGAMT SEFRLTVEIA HQNAIDQQLN DRTLKQIVHE
AERNVDRAIH NTKAEIRFAK TTSPHDLMRI FKFAVPRTSD LTRSREIYEE SLRLIQKHVQ
QGLRLPTHQL PGNVSYESVL SVSHIQTLME LSGCQAGVFK DPCTNMCFHS KYRAYDGQCN
NFDHPMRGVS QMPLLRLLPP IYENGFNTPL GWDPSRLYNG FPLPNPRTVS RRLIGTEDIT
PHHRFSSMLM QWGQFVDHDL DHTSMALSRQ TYSTGAICNR TCENIDPCFN IPLPPDDPRL
RHPERVKFPC IEFERSAAVC GSGETSLIFQ RVAYREQMNL ITSYLDASNV YGSTEVDALD
LRDLFGDHGL LRFDIVSTSQ KPYLPFERDS PMDCRRNRSI DNPIRCFLAG DFRANEQLGL
AAMHTLWLRE HNRIATRLLE MNPDWDGERI YQESRKIVGA QIQHITYAHW LPKVIGEEGF
RQRIGPYAGY DSSVDASISN AFATAAFRFG HTLINPKLAR MDKEFKTIPQ GDIPLHEAFF
APERLLAEGG VDPLLRGLFA APLKKPMSHQ LLNTELTEKL FKKSEDVSLD LASVNIQRAR
DHGLQGYMAY RKWCNLTVAS TWDELAVDIP DAGVRQKLRE LYGHPANIDL WVGGITEKKL
PDALVGPTFS CIIADQFRRL RDGDRFWYEN EGVFTPLQLQ QLRKTSLAKV LCNNGDEIDR
VQKDVFLFVG ENTRQRKECS TLEDVNLNMW MSCCDGSCGA REDEGVSEAQ KRRRRTVKKY
TKQGEEKCRF DGKEFEHLEQ WSVGSCVVCE CRNKKVWCTT NADCANE
//
