ID A0A0V0URV3_9BILA Unreviewed; 1379 AA.
AC A0A0V0URV3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Peroxidasin-like protein {ECO:0000313|EMBL:KRX53813.1};
GN ORFNames=T09_5843 {ECO:0000313|EMBL:KRX53813.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX53813.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX53813.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX53813.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX53813.1}.
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DR EMBL; JYDN01000190; KRX53813.1; -; Genomic_DNA.
DR STRING; 181606.A0A0V0URV3; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
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; 3.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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; 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; 3.
DR Pfam; PF13855; LRR_8; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Reference proteome {ECO:0000313|Proteomes:UP000054681};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1379
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006870216"
FT DOMAIN 297..384
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 389..475
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 482..568
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT COILED 1350..1377
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 1039
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 1379 AA; 156385 MW; DFF91F155F5B0B9A CRC64;
MAALNFWRFV IFVFSIVKCI LSAEIENGNC PSGCHCNEKY VECIALRMKH MPSVIFSSAL
HFDLSFNRIQ SINKMDLMNF NNLISLDMAH NLLKFIESYS FTWLANLKIL NLSYNQLQFL
NNDTFVGLSQ LRHLSLNDNA LLLIEEAALE PLINLIELDV SNNEHLNFSS LLTAIEKLNS
LKLLQTDEHS IRCNCSTVVA IVSLLQKNTE LGIQTGDCFY KYSEADNSRC LEELINFANY
CKGETGDVET IFHECSRKKI NKAKHHQQHK VHLGSKQADL ANARVRRIPR RHRRRSPVKI
VRPPENVDAD LDETVSFTCL VSGYPNPRIH WFCNGNKLIS SNRIKFYQHD QKVVITNVQR
EDNGVYTCVA ENAISQSTAT AFLQVKSRPE FRLRPQNTIA LEGAEVKLEC DPVGYPQPAI
VWTKNGRSIP TNRRISISNA GTVLKINSIS ADDEGQYTCY ATNALGSIEW SVVVKVKQSF
PPRMQNAPST LILTAGNTAS FPCRVVANPE PTITWLFNGN PIRTVKGHYE MSSQGTLYVF
NVTKSDEGFY TCQASNAVGA ISADAQLEVI APNLSSGQKA PAILNVDSEF IRSTVQQATV
NVDKAINWTR QKLYDDHPKS PAELMALLRY PGPAALEHAR AREIYEQTIS LIQSHVVQGL
HFNLSTPFEY PHVLSKGHVA LISELTGCNV HREMPKCNDM CFHRKYRSYD GSCNNFEHPL
RGASLTSFKR LLPPIYENGF DQPVGWRKGK LYYGYPKPNV RTVSQMLIST KQVTNDTEYS
HMLMQWGQFL DHDLTLTVNA PSILQFQTGV DCKRTCQNRP PCFNIEIPPN DRRIKYGVCM
EFERSSAVCG SGDTSVLFDT LQHREQLNVL TAYIDASNVY GSEEADALNL RDLFSDHGQL
KFDITSHKQK PYLPFNRNLP MDCRRNSTVP HSMRCLMAGD YRANEQVGLL AMHTLWMREH
NRIAAKLLRI NSHWDGEKIY QETRKIIGAQ MQHITYHSWL PKILGPQGMN MLGTYGGYNQ
AIDSTISNAF ATAAFRFGHT LIQPILIRLD ENFKPHSAGH LPLEEAFFAP ERLLNEGGID
PILRGMFSTP AKLPTTGQYL NSILTEQLFN KAHDVALDLA ALNIQRGRDH ALPGYLEYRK
FCNLSSPDTF DGLSEVIPDQ SIRRKLQILY GHPGNVDLWV GGVLEKLLPD ARVGETFACI
IADQFRRIRD GDRFWYENAG VFRPDQLYEI KKTTLARILC DSGDEIDRVQ RDIFKNIGST
NPEHYTRCEH LPNINLNMWQ ECCEEDCRAA IKFETVDDAL DKDITFLKPS NTDELLAIRR
KRSITASPIM YNYFNSSYKN KIPKISTETG HKLQSEINSL KEAVKHLEQI IMNLNLNNK
//
