ID A0A091I5W4_BUCRH Unreviewed; 1309 AA.
AC A0A091I5W4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Peroxidasin {ECO:0000313|EMBL:KFO94793.1};
DE Flags: Fragment;
GN ORFNames=N320_06622 {ECO:0000313|EMBL:KFO94793.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO94793.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO94793.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO94793.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL537188; KFO94793.1; -; Genomic_DNA.
DR Proteomes; UP000054064; 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; cd05746; Ig4_Peroxidasin; 1.
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; 4.
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; IPR034828; Peroxidasin_Ig-like4.
DR InterPro; IPR034824; Peroxidasin_peroxidase.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF54; PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF07679; I-set; 4.
DR Pfam; PF13855; LRR_8; 2.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00082; LRRCT; 1.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 4.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS51450; LRR; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000054064};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 211..299
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 307..393
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 398..483
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 486..577
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT BINDING 1034
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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO94793.1"
FT NON_TER 1309
FT /evidence="ECO:0000313|EMBL:KFO94793.1"
SQ SEQUENCE 1309 AA; 146934 MW; 703EECFC5C4A7C06 CRC64;
CPSRCLCFRT TVRCMHLMLE TIPEIPPQTN ILDLRFNHIK EIQPGAFRRL KNLNTLLLNN
NQIKQIVRRS FEDLENLKYL YLYKNEIQSI QQHAFDGLRS LEQLYLHFNN LDSLEPETFS
DLPKLERLFL HNNKISRIHP GTFSQLESLK RLRLDSNALL CDCDLMWLAE LLKEYAEQGS
IQTAATCEAP PELHGRSIVT LTAQEFNCER PRITSEPHDV DVLLGNTVYF TCRAEGNPKP
AIIWLHNNNE IDMKDDNRLN LLQDGTLMIQ NTKESDKGVY QCMAKNIAGE VKTQEVVLRY
FGIPSKPTFV IQPQNTEVLI GESVTLECGV SGHPHPRISW TLGTGSPLPQ DSRFAITSSG
GLFIQNVSFS DQGQYNCNAS NTEGSIQATA RIIVQDSPRF LLIPTDQTVT EGQSVDFPCS
AEGHPPPVIA WTRAGGPLPS DRRHSILSTG TLRVMRVALH DQGQYECHAI SAIGVRTLPV
QLSVTPRVIP VFLHPPQDVV AETGQDVAIT CAAQGDPRPT ITWVKEGIQI TESGKFHISQ
DGTLAIQDLG VADQGRYECI ARNPFGFTSS AMQLTITATD VGRSGDTFVA TSLREAISSV
DHAINSTRTR PKTPNDLLAL FRYPRDPYTI ETARAGEIFE RTLQLIQEHV QQGLIVDVNV
TGYRYNDLVS PHYLNMIANL SGCSAHRRTP NCSDICFHKK YRTHDGSCNN LQHPMWGASL
TAFQRLLKPA YQNGFNLPRG FSLAEDARDL PLPLPRLVST AMVGTETITP DNQFTHMLMQ
WGQFLDHDMD QTVAAISMSR FSDGAPCSEV CSNDPPCFSI MVPANDPRVR NGRCMFFVRS
SPVCGSGMTS LLMNSVYARE QINHLTSYID ASNVYGSTEQ ESRELRDLSN QKGLLKQGQV
VSSSGKHLLP FAVGPPTECM RDENESPVPC FLAGDHRANE QLGLTAMHTL WFREHNRIAT
ELSALNPHWD GDLVYHEARK IVGAQMQHIT YAHWLPKVLG EAGMKMLGEY KGYDPNINAG
ILNAFATAAF RFGHTLINPI LYRLNESFQP IRHGHIPLHK AFFSPFRIMQ EGGIDPLLRG
LFGVPGKMRV PSELLNMELT EKLFSMAHSV SLDLAAINIQ RGRDHGIPPY NDFRVFCNLS
AAQEFEDLRN EIKNLEIREK LRSLYGTTKN IDLFPALMVE DLVPGTRVGP TLMCLLTTQF
RRLRDGDRFW YENPGVFSSA QLTQIRQTSL ARVICDNSDH IQQLQRDVFQ VASYPQGMVA
CDEIPAVDLR LWQDCCEDCQ TRGQFRALSQ QFRSRRSPGF SYAEENPAK
//
