ID A0A182QI48_9DIPT Unreviewed; 674 AA.
AC A0A182QI48;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Transcription factor CBF/NF-Y/archaeal histone domain-containing protein {ECO:0000259|Pfam:PF00808};
OS Anopheles farauti.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=69004 {ECO:0000313|EnsemblMetazoa:AFAF010623-PA, ECO:0000313|Proteomes:UP000075886};
RN [1] {ECO:0000313|Proteomes:UP000075886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAR1 {ECO:0000313|Proteomes:UP000075886};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles farauti FAR1 (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AFAF010623-PA}
RP IDENTIFICATION.
RC STRAIN=FAR1 {ECO:0000313|EnsemblMetazoa:AFAF010623-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Microsome membrane
CC {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004174}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; AXCN02000379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A182QI48; -.
DR STRING; 69004.A0A182QI48; -.
DR EnsemblMetazoa; AFAF010623-RA; AFAF010623-PA; AFAF010623.
DR VEuPathDB; VectorBase:AFAF010623; -.
DR OrthoDB; 3674251at2759; -.
DR Proteomes; UP000075886; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR CDD; cd11056; CYP6-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
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 InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR24292; CYTOCHROME P450; 1.
DR PANTHER; PTHR24292:SF54; CYTOCHROME P450 28A5-RELATED; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 500..556
FT /note="Transcription factor CBF/NF-Y/archaeal histone"
FT /evidence="ECO:0000259|Pfam:PF00808"
FT REGION 585..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..616
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..674
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 76205 MW; 481D3B634716FB44 CRC64;
LISTGGEEQT SAYIRSAGTP NLVSRLSGAL PTECVCYLPA FRRIIVAMFG LLVALTVLAV
CLYFKWSCSY WTRVGNVAGP KPLPIFGNLL EQLTGQKHFG EIFEEMYRSF PQASWVGYYK
FSNQPGVVVR DLELVREVLT SSFSSFNQND FQIDETIDPL LACNPFVQTG DRWKERRNQM
TSVFTMNRIR ATFPLVQQVA DDFVQFIQRT RRVDAHFEGK DICAKYTVNV VASIAFGIDA
ESFTNPDAEF VRMGNALFAP TWLTAIRSQL ALFAPGVAKL LRVPFVPGYV DRWFRSMVNE
TIRQRKTTKR QDMFQAMYDN LSENGKVEVD INELTGHSVT FLSEGFETSS TMMSYLLFEL
AANPTIQERV AQEVREVLKE SEGQLTEPGL HKLVYLEAAM METLRMHTPV FTLPRICTKD
FELPPQFPND TKRVTLRKGT SVIIPVYAIH NDPEIYPKPY VFDPERFSEE NRKSRPRHAF
LGFGEGPRLC LAMDGDRLTQ LPMARIRTVM KTSPDMGNIN AEALFLMCRA AEMFIEHMAK
GAYQKGSKTL EYKDLARFVE SEDNLEFLQQ ILPNKITVKE YKAMMEKKPD TDDDTETEDE
DESDAEQEED DDDVEIVDVT AKEKAAPAAD SEDSASDSGE SNSVISIDSS SDEKENSKNV
SNKKSPVKHK AGEN
//
