ID A0A1V9XY51_9ACAR Unreviewed; 745 AA.
AC A0A1V9XY51;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Peroxidasin-like {ECO:0000313|EMBL:OQR78414.1};
DE Flags: Fragment;
GN ORFNames=BIW11_06428 {ECO:0000313|EMBL:OQR78414.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR78414.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR78414.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR78414.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
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:OQR78414.1}.
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DR EMBL; MNPL01002251; OQR78414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XY51; -.
DR STRING; 418985.A0A1V9XY51; -.
DR InParanoid; A0A1V9XY51; -.
DR OrthoDB; 4560at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09823; peroxinectin_like; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR PANTHER; PTHR11475:SF106; CURLY SU; 1.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247}.
FT BINDING 499
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:OQR78414.1"
SQ SEQUENCE 745 AA; 85491 MW; 62CDCD6290354200 CRC64;
KEFVLFIHCR VLFILTMCVY WVTLSFAHSD HAGLFWRPKI SFPVDPTSPT VPDVHAHLID
EAVDEAQTII VQNKLFERAS VSSKTHLYPM CPAAQRHMQF RAAKSQAMHM DDMSSIFEET
TKILSKKMKM FWEDEFHGLA RANLGGSKLE QAAQQCHHHS NLICSDKPYR TADGSCNNLE
HAEWGKSFTC LRRLLPPRYA DGVSMPRISE TGLQLPNPRL VSTTIHVDLD RPSRHVSHML
MQWGQFLDHD FALSPIMSHP EEIVDLGNPN DVVDCCSQSK RHDPKCFSFD IPENDKFFSK
YGEHCMNFPR SARCPQCALG PRQQIDALTS FIDGSNIYGS NQEDTYRLRT LSGDGRLKFD
VGQRGDMILP ASFHPTRDRC SRPEEGDLCF RAGDERVNEQ PGLTAMHTLW LRHHNGIADK
LARLNPHWED ERIFQEARRI LIGQIQHITY SEFLPLILGN AFYREFGLET LPYGYTTYNK
NIDPTILNEF AGAVFRFGHT ILNGHFMEVD THGNIKRIKL QDNFFKPFEF RHGKMERIMR
GLQKQPSQVF DNFITHDVTN HLYRLSNESF GLDLIALNIQ RGRDHGLRGY TDYLKGCFGI
EVNTFEDLDN VMPRPVRERL ESLYAHVNDI DLFTGGVSEY QLPGGVVGPT FGCIMGIQFW
RLKYGDRFYY EHGGQAGSFT PSQLTQIRKI TMAKIVCDNS IGQQFSQQWS LQMVNENNPE
LPCDSFADMD MNNWIEHGAA HKKKK
//
