PlantTFDB - Plant Transcription Factor Database @ CBI, PKU

PlantRegMap/PlantTFDB v5.0

Plant Transcription Factor Database

Transcription Factor Information

Basic Information | Signature Domain | Sequence |

Basic Information? help Back to Top

TF ID

Bv9_224410_qxmk.t2

Organism

Beta vulgaris

Taxonomic ID

161934

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; Caryophyllales; Chenopodiaceae; Betoideae; Beta

Family

C3H

Protein Properties

Length: 1104aa MW: 124498 Da PI: 5.7326

Description

C3H family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
Bv9_224410_qxmk.t2	genome	TBVR	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	zf-CCCH	22.7	1.8e-07	164	188	5	26
--SGGGGTS...--TTTTT-SS-SS CS zf-CCCH 5 lCrffartG...tCkyGdrCkFaHg 26 +C+ a+tG Ck+Gd+C+F+H+ Bv9_224410_qxmk.t2 164 ICPAVAKTGdasSCKFGDKCRFSHD 188 69999*******************7 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
PROSITE profile	PS50103	11.882	159	190	IPR000571	Zinc finger, CCCH-type
SMART	SM00356	0.57	161	189	IPR000571	Zinc finger, CCCH-type
Gene3D	G3DSA:4.10.1000.10	6.4E-4	164	190	IPR000571	Zinc finger, CCCH-type
Pfam	PF00642	2.9E-5	164	188	IPR000571	Zinc finger, CCCH-type
SMART	SM00356	9.9	200	225	IPR000571	Zinc finger, CCCH-type
PROSITE profile	PS50103	7.62	203	228	IPR000571	Zinc finger, CCCH-type
Gene3D	G3DSA:3.20.20.70	1.3E-72	748	991	IPR013785	Aldolase-type TIM barrel
CDD	cd02801	4.02E-88	752	987	No hit	No description
SuperFamily	SSF51395	4.87E-61	752	1065	No hit	No description
Pfam	PF01207	4.0E-47	755	1022	IPR001269	tRNA-dihydrouridine synthase
PROSITE pattern	PS01136	0	836	854	IPR018517	tRNA-dihydrouridine synthase, conserved site

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0008033	Biological Process	tRNA processing
GO:0055114	Biological Process	oxidation-reduction process
GO:0017150	Molecular Function	tRNA dihydrouridine synthase activity
GO:0046872	Molecular Function	metal ion binding
GO:0050660	Molecular Function	flavin adenine dinucleotide binding

Sequence ? help Back to Top
Protein Sequence Length: 1104 aa Download sequence Send to blast
MDESVIEAPK IENTELSSQP ENSGEVHMSS ENQAAMEESP IEASIKKEPS FQPENSGEFH 60 PSSENQEVME ESPIEVSIKT EPSFQSENSG EGQLSPEKLI AKGIAPVKKE FLRPPPSSRS 120 TNLDNRDENG KSDSSKSTGI VKEKKSKRQL KRERREERES ALNICPAVAK TGDASSCKFG 180 DKCRFSHDFE AYKSQRPADL EGECPFISAQ KNCPYGVTCR FYGTHKDMPS ESLDVLQGGA 240 DVNPLKKDVQ KLLWKNKMKY PKSDAALKQL GLVYQEETSP NHEVHGHDED GQYQEEDDDD 300 YEEFAEPTQS FSQLLSPSLS QPPSTQSQIP PSPQTNFSRK RVWDPVEDEN LILAFMNTSL 360 AEVVGTSKKK SAFWGKVWDA FEAGRRINPI KFAPRNADMV KGRWSRVAPP VLRWDAFYDE 420 ALVRKRSGQN DSDVIREAHL LYNRKHGRFL LEHAWTMFKK FPEWKAIIKK SLENPRGRPK 480 VAQENLDSPG SRISSKRPRV DGSDSMPDTP TTGEGGEEEK RLDGVKKAKH MRKGVVGETI 540 DFNSFNERVR LPSESRSGDA EIERKRMEVH KKMLALKDRE IELATRSLNL QEYRMNLQEY 600 HMNYDILQTL SMKENRLPNE EAMGKGHTRV KEEEDIVPKI SNGSHCSEDN GCEKYDTPDK 660 QQDASAALLE PSADGVLDND DSRPLKKAKS VDDDGIDSSK DVNNGTSLSI EGLVNVCTED 720 ESHFPRDCLP PETDASLKLQ PRERKLIDFS KKLYLAPLTT VGNLPFRRVC KVLGAEVTCG 780 EMAMCTNLLQ GQSSEWALLR RHKSEDIFGV QICGAYPDTV ARAVELIDQE CSVDFIDINM 840 GCPIDIVVNK GAGSALLTKP LRMKNVIRAA CASAEKPITV KVRTGYIEGR NRADLFISDF 900 YEWGASALTI HGRSRQQRYS KAADWEYINT CVKKAPDSFQ VLGNGDVFSY LDWNKHFSDC 960 PELSSCMLAR GALIKPWLFT EIKEQRHWDI SSGERLDILK DYVRFGLEHW GSDSKGVETT 1020 RHFLLEWLNY TFRYIPVGLL DVVPQNVNWR PPSYYGRNDL ETLMASESAA DWIRISEMLL 1080 GKVPPGFTFA PKHKSNAYDS AENG

Sequence ? help Back to Top

Protein Sequence Length: 1104 aa Download sequence Send to blast

MDESVIEAPK IENTELSSQP ENSGEVHMSS ENQAAMEESP IEASIKKEPS FQPENSGEFH  60
PSSENQEVME ESPIEVSIKT EPSFQSENSG EGQLSPEKLI AKGIAPVKKE FLRPPPSSRS  120
TNLDNRDENG KSDSSKSTGI VKEKKSKRQL KRERREERES ALNICPAVAK TGDASSCKFG  180
DKCRFSHDFE AYKSQRPADL EGECPFISAQ KNCPYGVTCR FYGTHKDMPS ESLDVLQGGA  240
DVNPLKKDVQ KLLWKNKMKY PKSDAALKQL GLVYQEETSP NHEVHGHDED GQYQEEDDDD  300
YEEFAEPTQS FSQLLSPSLS QPPSTQSQIP PSPQTNFSRK RVWDPVEDEN LILAFMNTSL  360
AEVVGTSKKK SAFWGKVWDA FEAGRRINPI KFAPRNADMV KGRWSRVAPP VLRWDAFYDE  420
ALVRKRSGQN DSDVIREAHL LYNRKHGRFL LEHAWTMFKK FPEWKAIIKK SLENPRGRPK  480
VAQENLDSPG SRISSKRPRV DGSDSMPDTP TTGEGGEEEK RLDGVKKAKH MRKGVVGETI  540
DFNSFNERVR LPSESRSGDA EIERKRMEVH KKMLALKDRE IELATRSLNL QEYRMNLQEY  600
HMNYDILQTL SMKENRLPNE EAMGKGHTRV KEEEDIVPKI SNGSHCSEDN GCEKYDTPDK  660
QQDASAALLE PSADGVLDND DSRPLKKAKS VDDDGIDSSK DVNNGTSLSI EGLVNVCTED  720
ESHFPRDCLP PETDASLKLQ PRERKLIDFS KKLYLAPLTT VGNLPFRRVC KVLGAEVTCG  780
EMAMCTNLLQ GQSSEWALLR RHKSEDIFGV QICGAYPDTV ARAVELIDQE CSVDFIDINM  840
GCPIDIVVNK GAGSALLTKP LRMKNVIRAA CASAEKPITV KVRTGYIEGR NRADLFISDF  900
YEWGASALTI HGRSRQQRYS KAADWEYINT CVKKAPDSFQ VLGNGDVFSY LDWNKHFSDC  960
PELSSCMLAR GALIKPWLFT EIKEQRHWDI SSGERLDILK DYVRFGLEHW GSDSKGVETT  1020
RHFLLEWLNY TFRYIPVGLL DVVPQNVNWR PPSYYGRNDL ETLMASESAA DWIRISEMLL  1080
GKVPPGFTFA PKHKSNAYDS AENG

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
6ei9_A	2e-26	749	996	27	266	tRNA-dihydrouridine synthase B
6ei9_B	2e-26	749	996	27	266	tRNA-dihydrouridine synthase B
Search in ModeBase

Nucleic Localization Signal ? help Back to Top

No.	Start	End	Sequence
1	520	528	RLDGVKKAK

Functional Description ? help Back to Top
Source	Description
UniProt	Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. {ECO:0000250}.

Regulation -- PlantRegMap ? help Back to Top
Source	Upstream Regulator	Target Gene
PlantRegMap	Retrieve	-

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_010665865.1	0.0	PREDICTED: uncharacterized protein LOC104883109 isoform X2
Swissprot	Q9T0J6	0.0	DUS3L_ARATH; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like
TrEMBL	A0A0J8E092	0.0	A0A0J8E092_BETVU; tRNA-dihydrouridine(47) synthase [NAD(P)(+)]
STRING	XP_010665864.1	0.0	(Beta vulgaris)

Publications ? help Back to Top
Szponarski W,Sommerer N,Boyer JC,Rossignol M,Gibrat R Large-scale characterization of integral proteins from Arabidopsis vacuolar membrane by two-dimensional liquid chromatography. Proteomics, 2004. 4(2): p. 397-406 [PMID:14760709]