ID D2VNP0_NAEGR Unreviewed; 1312 AA.
AC D2VNP0;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC41536.1};
GN ORFNames=NAEGRDRAFT_80660 {ECO:0000313|EMBL:EFC41536.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC41536.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC41536.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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}.
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DR EMBL; GG738885; EFC41536.1; -; Genomic_DNA.
DR RefSeq; XP_002674280.1; XM_002674234.1.
DR STRING; 5762.D2VNP0; -.
DR EnsemblProtists; EFC41536; EFC41536; NAEGRDRAFT_80660.
DR GeneID; 8862458; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_80660; -.
DR eggNOG; KOG0159; Eukaryota.
DR InParanoid; D2VNP0; -.
DR OrthoDB; 5486142at2759; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
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:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 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 InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR24303:SF31; CYTOCHROME P450 307A1-RELATED; 1.
DR PANTHER; PTHR24303; HEME-BINDING MONOOXYGENASE FAMILY; 1.
DR Pfam; PF00067; p450; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR PRINTS; PR00463; EP450I.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671}.
FT DOMAIN 287..314
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT DOMAIN 820..898
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT REGION 84..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 541..568
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 747..774
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 316..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1312 AA; 147881 MW; 69E6F65FCE8B7E51 CRC64;
MNNPNNMNNS SSAIPGNDFS ASSSVGVIGQ PLSGNGSSSG GGVLPPRLES YNNLHLINSS
GNLLTNHQHP LLNGTAGYYG LGQHQHHQQQ HHYGNHLPTQ PSQTNAGGAT ITTNNLLSSH
QQNQQQQLHH LMSAAASSYP NLSQNNNLSS SNISQQTSHT NSLLSHPSLS NLHHLQASTN
IANSGGLMDQ QLSFNHVRGT SYWWWFNGYH HELPINEFNS SSLNDQDAPP VPPSNNNNST
ITGKTDSNGS SSNNSDKTKE ASNSNMANMQ KEMSNMMKRP RRVAKLACVS CRKAHACCED
KRPCSRCLAH GLECQDQVGK KRGRKKKSGE DDNDEDLDDV PTEKPQSSQT SSNAVEPSSS
TNNNTATTIN AASSSTATAT TEKNEKKKKK KKASSPKKKK EKPTATASSS TTTQPKTEPE
QATQGQANQR IPPTQQQMIN PNLVNNLPLQ LTESELKTPG AMLTAGNVIF PNRDNHPLSL
PFLLNQPPEI QQLTQILMRT PVDTFYLHCN NLNSAYDYQN NQSLFGTPYS LHVDEALLHQ
HQQHMNALNN LKIQNQQHQQ QLHQQQLISP GGAASPLIDF TNDEFLRFSP QSPLFASIVE
MDENEIHNEV GHMMPISHSN ATEEQQADKM RSQNNSNVNN NDDVQIEDCE DTNQKPASSS
KQDEEIFEKL IKMSNEEMIK SLQIGDDTKQ MIEESIGHLK QFDSNPETAN MTYIEYLTQN
FPISLLLKHK LNDSAKRLST SNETEPGTDA QKEIEILREE NKRLKEENLR KANESAMLSA
INENLRNRFS ELASKGIIKM QYDEPPTYGE NNKPTAIQDS YQELVMLMEN KQEMDSSDFG
IILMFPGGRI ISLNKTLLTK LNYDPSDLYD NLERWEDVVH PESYPQIVAH VSRVLKTPPA
PRKSFKCKVN CRRRGGGMIP AELYLCIVGG KFSYIPVFAI IMELNGELLR RLVKHLQPVE
GSEKYKFAKN FEATSRYAFD AVLKVFLGVK LTDETVQSFP FDLRDFVKYS IVGLDLAILL
DNKPPLYKYF KTQEYKHFEH VWDKSLEYGR YCIKRFKTNP TEKPRLLEIL EERAKDQEYP
EERVENVMIT FLQAGTDITV RMVNNSLYRL AQHSEYQEKL FQESVEVFGQ PTIDELTLEN
GLEITMEQFK KLKHTKNFIE EVLRLNSFSY LTMGRQLSKD TEIGGFNVPK DTIVIAMQRW
GTLKDEFIPR GSEFIPERHE KGSDLAPVNN YVSVPFGVGA RKCPGSRIAL TEIHFAIINA
IRHFKLSHDN GNEMPPSSLD QSLLYIDSEK YPLYFTPREH VKEYVEKNSN KL
//
