ID A0A093PF10_9PASS Unreviewed; 1314 AA.
AC A0A093PF10;
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:KFW75493.1};
DE Flags: Fragment;
GN ORFNames=N305_13161 {ECO:0000313|EMBL:KFW75493.1};
OS Manacus vitellinus (golden-collared manakin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW75493.1, ECO:0000313|Proteomes:UP000053258};
RN [1] {ECO:0000313|EMBL:KFW75493.1, ECO:0000313|Proteomes:UP000053258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW75493.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL669208; KFW75493.1; -; Genomic_DNA.
DR STRING; 328815.ENSMVIP00005006320; -.
DR Proteomes; UP000053258; 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; 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; 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; 3.
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:UP000053258};
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 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"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW75493.1"
FT NON_TER 1314
FT /evidence="ECO:0000313|EMBL:KFW75493.1"
SQ SEQUENCE 1314 AA; 147700 MW; EED386C71978150C CRC64;
CPSRCLCFRT TVRCMHLMLE TIPEIPPQTN ILDLRFNHIK EIQPGAFRRL KNLNTLLLNN
NQIKQIVRRS FEDLENLKYL YLYKNEIQSI QQHAFHGLHS LEQLYLHFNN LESLELETFS
DLPKLERLFL HNNKISKIHP GTFSQLESLK RLRLDSNALF CDCDLMWLAE LLKKYAEQGS
IQTAATCEAP RDLHGRSIVT LTAQEFNCER PRITSEPHDV DVLLGNTVYF TCRAEGNPKP
AIIWLHNNNK IDMKDDNRLN LLQDGTLMIQ NTKESDKGVY QCMAKNIAGE VKTQEVVLRY
FGTPSKPTFV IQPQNTEVLI GESVTLECGV SGHPHPRISW TLGTGSPLPQ DSRFTITSSG
GLFIQNVTFS DQGQYNCNAT NSEGSIQATA RIIVQDSPRF LVIPTDQTVT EGQSVDFPCS
AEGHPPPVIT WTRAGGPLPN DRRHSILSTG TLRVLRVALH DQGQFECHAI SAIGVRTLPV
QLSVTPRVIP VFLQPPQDVV AETGQDVAIT CAAQGDPRPT ITWVKEGIQI TESGKFHIGQ
DGTLSIQDLG VADQGRYECI ARNPFGFTSS AMQLTITATD VGRSGDTFVA TSLREAISSV
DHAINSTRTE LFSKRPKTPN DLLALFRYPR DPYTIETARA GEIFERTLQL IQEHVQQGLI
VDMNVTGYRY NDLVSPHYLN MIANLSGCSA HRRTPNCSDI CFHKKYRTHD GSCNNLQHPM
WGASLTAFQR LLKPAYQNGF NLPRGFSLAE DARDLPLPLP RLVSTAMIGT ETITPDDQFT
HMLMQWGQFL DHDMDQTVAA ISMSRFSDGA PCSEVCSNDP PCFSVMVPAN DPRVRNGRCM
FFVRSSPVCG SGMTSLLMNS VYAREQINHL TSYIDASNVY GSTEQESQEL RDLSNQSGLL
KRGQVVPSSG KHLLPFAVGP PTECMRDENE SPVPCFLAGD HRANEQLGLT AMHTLWFREH
NRVATELAAL NPHWDGDLLY HEARKIVGAQ MQHITYAQWL PKVLGEAGMK MLGEYKGYDP
NVNAGILNAF ATAAFRFGHT LINPILYRLN ETFQPIQQGH IPLHKAFFSP FRITQEGGID
PLLRGLFGVP GKMRVPSELL NMELTEKLFS MAHSVSLDLA AINIQRGRDH GIPPYNDFRV
FCNLSSAQEF EDLRNEIKNL EIREKLRSLY GTAKNIDLFP ALMVEDLVPG TRVGPTLMCL
LTTQFRRLRD GDRFWYENPG VFTPAQLTQI RQTSLARVIC DNSDHIQQLQ RDVFQVASYL
QGMVSCEEIP AVDLRLWQDC CEDCQTRGQF RALSQRFRRK RSPGFSYPEE NPAK
//
