ID A0A9E8BWL7_9NEOP Unreviewed; 470 AA. AC A0A9E8BWL7; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 27-MAR-2024, entry version 5. DE SubName: Full=Cytochrome P450 CYP4XF3 {ECO:0000313|EMBL:UZE89878.1}; OS Chrysoperla zastrowi sillemi. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Neuroptera; Hemerobiiformia; Chrysopidae; OC Chrysopinae; Chrysoperla. OX NCBI_TaxID=482137 {ECO:0000313|EMBL:UZE89878.1}; RN [1] {ECO:0000313|EMBL:UZE89878.1} RP NUCLEOTIDE SEQUENCE. RA Pathak J., Ramasamy G.G., Agrawal A., Srivastava S., Basavaarya B.R., RA Muthugounder M., Muniyappa V.K., Maria P., Rai A., Venkatesan T.; RT "Comparative Transcriptome Analysis to Reveal Differentially Expressed RT cytochrome P450 in Response to Imidacloprid in the Aphid Lion, Chrysoperla RT zastrowi sillemi (Esben-Petersen)."; RL Insects 13:0-0(2022). RN [2] {ECO:0000313|EMBL:UZE89878.1} RP NUCLEOTIDE SEQUENCE. RA Pathak J., Thiruvengadam V., Gracy G.R.; RL Submitted (MAY-2022) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May be involved in the metabolism of insect hormones and in CC the breakdown of synthetic insecticides. CC {ECO:0000256|ARBA:ARBA00003690}. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ON646362; UZE89878.1; -; mRNA. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR Gene3D; 1.10.630.10; Cytochrome P450; 1. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR InterPro; IPR036396; Cyt_P450_sf. DR PANTHER; PTHR24291:SF189; CYTOCHROME P450 4V2; 1. DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 1. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 2: Evidence at transcript level; KW Coiled coil {ECO:0000256|SAM:Coils}; Heme {ECO:0000256|RuleBase:RU000461}; KW Iron {ECO:0000256|RuleBase:RU000461}; KW Metal-binding {ECO:0000256|RuleBase:RU000461}; KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, KW ECO:0000256|RuleBase:RU000461}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}. FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 39..93 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 174..201 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 470 AA; 53638 MW; 2F8F2AA339DBC6C0 CRC64; MDDDAMNIKQ QEQQNDKQTT TTILINNNHE EEEVYTTINN NNNNTTTTIS DNEQQQQPQQ SINRNTWSRT SLRRSPIHNN NGGGTGSGSI KRWGSFRTTN KRQLGSNALA SELYRSSSFN CTSGSGGNVT TRTTNCNLDD RMSTTSKDDL YGCSSMTTTY SSMSDHDQDI IDHGSLLEDD VLDLNHKVEQ LQQQVNILTS TTIEQQQHLN NNNINNNINN NNNNIIDDNS NVCLGSKKRI IFLDLLLQST HLSGEPLTDK EIIDEVTNFM FAGHDTTSVQ LSLLMYLLCE HPEIQNELYK EQCAILTDIN GDPSFKQIQE MNYLERTIKE SQRILPCVIS FSRKMTADIQ LKTNNLLLPK GCTASIFVYD VHHNPKIYEN PEKFDPDRFL PENIRGRHPY AYIPFSAGPR NCLGQKFALL EMKTVMSNII RNFKILPAYE DNGDKFKPIF RRYMLLTSLN GIQIRLESRR //