ID Q7YU25_DROME Unreviewed; 1439 AA.
AC Q7YU25;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 22-FEB-2023, entry version 109.
DE SubName: Full=RE05911p {ECO:0000313|EMBL:AAQ22495.1};
GN ORFNames=CG42331 {ECO:0000313|FlyBase:FBgn0259233}, CG6879
GN {ECO:0000313|EMBL:AAQ22495.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAQ22495.1};
RN [1] {ECO:0000313|EMBL:AAQ22495.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Berkeley {ECO:0000313|EMBL:AAQ22495.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; BT010026; AAQ22495.1; -; mRNA.
DR UCSC; CG42331-RB; d. melanogaster.
DR AGR; FB:FBgn0259233; -.
DR FlyBase; FBgn0259233; CG42331.
DR VEuPathDB; VectorBase:FBgn0259233; -.
DR HOGENOM; CLU_251966_0_0_1; -.
DR OrthoDB; 4560at2759; -.
DR ChiTaRS; CG42331; fly.
DR ExpressionAtlas; Q7YU25; baseline and differential.
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; IBA:GO_Central.
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:SF109; CHORION PEROXIDASE-LIKE PROTEIN; 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 2: Evidence at transcript level;
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1026..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 318
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 1439 AA; 159946 MW; F9EFA61BF0B5BBAA CRC64;
MPASERYRTH DGTCNNKRRP RWGAAQMPFN RFLPPEYGDG VDTVRSSADG STLSSSRFVS
LLVHGAREGE APLTLMIAQW GQMLDHDMTS TAQPRSINGS IPSCCGGKDF HPACFPIKVP
LDDPWLAPLK VRCLEFLRSA PAQRRDCVLS WREQTNQVTS YIDASPIYSN SAKSSDNARV
FRHGLLVYGR GDPAEDVCQR GAIATKCIRS GDGRSGEQPG LLAMHHVWVG EHNRIAMELS
ELNPHWSDEK VYQETRRIVG AMFQHITFRE FLPVILGREV VKLFDLELMP SGYYERYSSK
VNPTVANAFA AAAFRFGHSL VQNSYTRCDC HHNVINNNVS LHEEFQRGDI GSAGSLHRLL
RGLASQRALK RDEFITPELT NHLFQTPGFP FGLDLAAINI QRGRDHGIAP YSAWRVPCGL
SPILSWDDFA NVVGPESAKR IGHAYRSVHD IDLFVGGIAE RPVVGGLVGP TFACIIAQQF
SNSRRGDRFW YENGGFESSF TPAQLHSLRR VSLAQVLCRT VGGGTLQPHI FIPAEFEDNE
RQTCGVGSLS PIDLSPWLEQ DPFHNQQVPE QVFTIGQPEL GSVQIIKEDK AGFSNRVKPI
KPQVEVSPSS LSGFHRPTNE NLTKVSDKLD LRRKTVTKKN NTNNRQQTTR KPVGGVNNKL
DKSPKITLNI KSVNVRRPEG SGLKRRVIIN NVPVELRSSG GNATAEETEP GNLTDEDDEF
HDDAGEVVDM EDIVEVRASK DDPSKLTKTD LNQNRNDSKT TETEQTEKNT TIEPTEDSTD
EPKTERRDAR KMEPHPAAKT PDKTADSRLL HNQRNRTTTP RDFQASSTVS LKRFTRQTKA
PKVSKPTKRA EELRQYQNRP LYERPQKVVV NGPNADQYEI EINIRQTNKN PASRPSTSDY
AQYTTANKPY YNSNYAPHYM DYASTTPIPL PSYGYHQPIG EISNQGVRTK PPTIIYLNDN
DDRRTTTRAP NIFQNFLTFA TNSFNPLGIR RPMPTTPSPI SQSHKEPGQF ENNVVHSPIS
NSHILTGGGP SASYSPRPPS VHSYPVATSS QIGGNPGSGF LHASSSAVSA GHFGSISGVA
TANGADSTFS FNIRPRPSPD LGSVVSSYPR PVSSQGGGSS YRPDYAPTQS ELYYDRELIT
DRNPSPFSGS SSAQRPHQQT FYGRSPELKE VGNNSNELTH TEHKLYLQDY DYASRTLSNL
TTDESHQTDD DTDYVYDEDI ASNDLDKTKT RKETDLNELT TKKFDQDGYM RPQLMRDATH
NSTGYNVTSL DDNYVMPMLE NRTRTNYVTE VPKPMLSTSS RSVTNSKVTV FPDSLGKQLA
NDILADEATD DYVDANGHTE ARLKAQKLKQ LASVAFAPIT VLTKPDRPDN WVIYNKASEE
PPLPQPPAVN MDVAPSGEVP TPIKNFNNAW LKQDLKARPE TPPTRLAEEV TTVAAADSI
//