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

Tp57577_TGAC_v2_mRNA8161

Organism

Trifolium pratense

Taxonomic ID

57577

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; Trifolieae; Trifolium

Family

MYB_related

Protein Properties

Length: 844aa MW: 95480.5 Da PI: 6.3493

Description

MYB_related family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
Tp57577_TGAC_v2_mRNA8161	genome	JGI	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	Myb_DNA-binding	33.4	1e-10	597	646	2	46
SSS-HHHHHHHHHHHHHTTTT-HHHHHHHHT.....TTS-HHHHHHHHHH CS Myb_DNA-binding 2 grWTteEdellvdavkqlGggtWktIartmg.....kgRtlkqcksrwqk 46 ++WT eE++ lv ++k++G g W++I + + R+ ++k++w++ Tp57577_TGAC_v2_mRNA8161 597 LKWTSEEEDALVAGIKKHGAGKWRAILLDPQfapllTSRSNIDLKDKWRN 646 69***********************************************9 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
PROSITE profile	PS51393	210.378	2	622	IPR013819	Lipoxygenase, C-terminal
Gene3D	G3DSA:4.10.375.10	2.4E-33	5	81	No hit	No description
SuperFamily	SSF48484	9.29E-227	6	592	IPR013819	Lipoxygenase, C-terminal
Pfam	PF00305	2.8E-28	12	82	IPR013819	Lipoxygenase, C-terminal
PRINTS	PR00468	2.4E-14	34	50	IPR001246	Lipoxygenase, plant
PRINTS	PR00468	2.4E-14	67	86	IPR001246	Lipoxygenase, plant
Pfam	PF00305	5.1E-148	81	431	IPR013819	Lipoxygenase, C-terminal
Gene3D	G3DSA:4.10.372.10	7.2E-28	82	155	IPR027433	Lipoxygenase, domain 3
Gene3D	G3DSA:3.10.450.60	1.1E-50	166	297	No hit	No description
PRINTS	PR00087	5.7E-26	283	300	IPR013819	Lipoxygenase, C-terminal
Gene3D	G3DSA:1.20.245.10	3.3E-60	298	431	No hit	No description
PROSITE pattern	PS00711	0	301	315	IPR020833	Lipoxygenase, iron binding site
PRINTS	PR00087	5.7E-26	301	318	IPR013819	Lipoxygenase, C-terminal
PRINTS	PR00087	5.7E-26	321	341	IPR013819	Lipoxygenase, C-terminal
PROSITE pattern	PS00081	0	328	338	IPR020834	Lipoxygenase, conserved site
Pfam	PF00305	6.5E-66	433	592	IPR013819	Lipoxygenase, C-terminal
Gene3D	G3DSA:1.20.245.10	9.4E-49	434	591	No hit	No description
SMART	SM00717	2.3E-5	595	650	IPR001005	SANT/Myb domain
SuperFamily	SSF46689	1.0E-13	596	649	IPR009057	Homeodomain-like
Gene3D	G3DSA:1.10.10.60	3.5E-11	598	647	IPR009057	Homeodomain-like
CDD	cd11660	4.94E-19	598	648	No hit	No description
PROSITE profile	PS50090	7.921	598	648	IPR017877	Myb-like domain
Pfam	PF00249	1.0E-6	598	647	IPR001005	SANT/Myb domain
SMART	SM00526	2.7E-14	683	748	IPR005818	Linker histone H1/H5, domain H15
Gene3D	G3DSA:1.10.10.10	3.0E-13	684	754	IPR011991	Winged helix-turn-helix DNA-binding domain
SuperFamily	SSF46785	1.85E-13	685	761	IPR011991	Winged helix-turn-helix DNA-binding domain
CDD	cd00073	1.11E-11	685	770	No hit	No description
PROSITE profile	PS51504	23.377	685	753	IPR005818	Linker histone H1/H5, domain H15
Pfam	PF00538	1.3E-10	687	746	IPR005818	Linker histone H1/H5, domain H15

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0006334	Biological Process	nucleosome assembly
GO:0055114	Biological Process	oxidation-reduction process
GO:0000786	Cellular Component	nucleosome
GO:0005634	Cellular Component	nucleus
GO:0003677	Molecular Function	DNA binding
GO:0016702	Molecular Function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0046872	Molecular Function	metal ion binding

Sequence ? help Back to Top
Protein Sequence Length: 844 aa Download sequence Send to blast
MTYLSNDTPA PLVYYRQDEP KTLRGDGIGE RKEWDRVYDY DVYNDLGDPD KGQSYARPIL 60 GGSSGHPYPR RGRTGRKPTT TDVIPLIKSV FDRNFTPNEF DSFDDVLDLY EGGIKLPTDI 120 LSQISPLHVL SEIFRTDGEQ FLKFPTPKVI QVSKSAWMTD EELEERLLLE FPPKSKLDSA 180 VYGDHTSTIT KEHIQLNLEG LTVDEAIQNK TLFLLEHHDT IIPYLRLINS TSTKAYASRT 240 ILFLKNDGTL KPLAIELSLP HPEGDQFGVT SNVYLPAIEG VESTIWLLAK AYVIVNDSCY 300 HQLVSHWLNT HAVVEPFVIA TNRQLSVLHP IYKLLYPHYR DTMNINALAR SSLVNADGII 360 EKTFLWGGYA MEISSKVYKD WVFTDQALPA DLIKRGIAVE DSTSPHGLRI VIEDYPYAVD 420 GLDIWDAIKT WKWGHGDKKG EPWWPKMQTR EDLIQVCSII IWTASALHAA VNFGQYPYGG 480 FILNRPTLSR RLMPEKGTTE YDELATNPQK AYLRTITPKF QTLIDLSVIE ILSRHASDEY 540 YLGQRDSAEY WTSDTNALAA FKKFGKTLTE IEGQLIIRNN NESLRNRVGP VRPSPMLKWT 600 SEEEDALVAG IKKHGAGKWR AILLDPQFAP LLTSRSNIDL KDKWRNMNVY VTAEGVRTPK 660 PKVAATTSSD IVINDSCQNE QDVNTPPRYN AMVFEALSTL KDTNGSDLNA IASFIEQKHQ 720 VPQNFRRTLS SRIRTLVNQE KLEKVQNCYK IKKETSLVTK SPSSKQKAVK PQQQSSVADD 780 MLKKAADTAA YIVAEAENKS YLAVEACKET ERFSRLAEEN DAMLLLAEEL YKQCLRGETL 840 KWA*

Sequence ? help Back to Top

Protein Sequence Length: 844 aa Download sequence Send to blast

MTYLSNDTPA PLVYYRQDEP KTLRGDGIGE RKEWDRVYDY DVYNDLGDPD KGQSYARPIL  60
GGSSGHPYPR RGRTGRKPTT TDVIPLIKSV FDRNFTPNEF DSFDDVLDLY EGGIKLPTDI  120
LSQISPLHVL SEIFRTDGEQ FLKFPTPKVI QVSKSAWMTD EELEERLLLE FPPKSKLDSA  180
VYGDHTSTIT KEHIQLNLEG LTVDEAIQNK TLFLLEHHDT IIPYLRLINS TSTKAYASRT  240
ILFLKNDGTL KPLAIELSLP HPEGDQFGVT SNVYLPAIEG VESTIWLLAK AYVIVNDSCY  300
HQLVSHWLNT HAVVEPFVIA TNRQLSVLHP IYKLLYPHYR DTMNINALAR SSLVNADGII  360
EKTFLWGGYA MEISSKVYKD WVFTDQALPA DLIKRGIAVE DSTSPHGLRI VIEDYPYAVD  420
GLDIWDAIKT WKWGHGDKKG EPWWPKMQTR EDLIQVCSII IWTASALHAA VNFGQYPYGG  480
FILNRPTLSR RLMPEKGTTE YDELATNPQK AYLRTITPKF QTLIDLSVIE ILSRHASDEY  540
YLGQRDSAEY WTSDTNALAA FKKFGKTLTE IEGQLIIRNN NESLRNRVGP VRPSPMLKWT  600
SEEEDALVAG IKKHGAGKWR AILLDPQFAP LLTSRSNIDL KDKWRNMNVY VTAEGVRTPK  660
PKVAATTSSD IVINDSCQNE QDVNTPPRYN AMVFEALSTL KDTNGSDLNA IASFIEQKHQ  720
VPQNFRRTLS SRIRTLVNQE KLEKVQNCYK IKKETSLVTK SPSSKQKAVK PQQQSSVADD  780
MLKKAADTAA YIVAEAENKS YLAVEACKET ERFSRLAEEN DAMLLLAEEL YKQCLRGETL  840
KWA*

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
1hu9_A	0.0	2	611	166	851	LIPOXYGENASE-3
1ik3_A	0.0	2	611	166	851	LIPOXYGENASE-3
1jnq_A	0.0	2	611	166	851	lipoxygenase-3
1lnh_A	0.0	2	611	166	851	LIPOXYGENASE-3
1n8q_A	0.0	2	611	166	851	lipoxygenase-3
1no3_A	0.0	2	611	166	851	Lipoxygenase-3
1rov_A	0.0	2	611	166	851	Seed lipoxygenase-3
1rrh_A	0.0	2	611	166	851	Seed lipoxygenase-3
1rrl_A	0.0	2	611	166	851	Seed lipoxygenase-3
1rrl_B	0.0	2	611	166	851	Seed lipoxygenase-3
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Functional Description ? help Back to Top
Source	Description
UniProt	Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.

Cis-element ? help Back to Top
Source	Link
PlantRegMap	Tp57577_TGAC_v2_mRNA8161

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

Annotation -- Nucleotide ? help Back to Top
Source	Hit ID	E-value	Description
GenBank	Z73498	0.0	Z73498.1 V.faba mRNA for lipoxygenase.

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_003627173.1	0.0	seed linoleate 9S-lipoxygenase-3
Swissprot	P09186	0.0	LOX3_SOYBN; Seed linoleate 9S-lipoxygenase-3
TrEMBL	G7LI99	0.0	G7LI99_MEDTR; Lipoxygenase
STRING	AET01649	0.0	(Medicago truncatula)

Orthologous Group ? help Back to Top
Lineage	Orthologous Group ID	Taxa Number	Gene Number
Fabids	OGEF3228	29	58

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT1G72740.2	1e-58	MYB_related family protein

Link Out ? help Back to Top
Phytozome	Tp57577_TGAC_v2_mRNA8161

Publications ? help Back to Top
Kariapper MS,Dunham WR,Funk MO Iron extraction from soybean lipoxygenase 3 and reconstitution of catalytic activity from the apoenzyme. Biochem. Biophys. Res. Commun., 2001. 284(3): p. 563-7 [PMID:11396936] Skrzypczak-Jankun E,Bross RA,Carroll RT,Dunham WR,Funk MO Three-dimensional structure of a purple lipoxygenase. J. Am. Chem. Soc., 2001. 123(44): p. 10814-20 [PMID:11686682] Skrzypczak-Jankun E,Zhou K,McCabe NP,Selman SH,Jankun J Structure of curcumin in complex with lipoxygenase and its significance in cancer. Int. J. Mol. Med., 2003. 12(1): p. 17-24 [PMID:12792803] Skrzypczak-Jankun E,Zhou K,Jankun J Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with EGC instead. Int. J. Mol. Med., 2003. 12(4): p. 415-20 [PMID:12964012] Borbulevych OY,Jankun J,Selman SH,Skrzypczak-Jankun E Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 A resolution. Proteins, 2004. 54(1): p. 13-9 [PMID:14705020] Vahedi-Faridi A, et al. Interaction between non-heme iron of lipoxygenases and cumene hydroperoxide: basis for enzyme activation, inactivation, and inhibition. J. Am. Chem. Soc., 2004. 126(7): p. 2006-15 [PMID:14971933] Skrzypczak-Jankun E,Borbulevych OY,Jankun J Soybean lipoxygenase-3 in complex with 4-nitrocatechol. Acta Crystallogr. D Biol. Crystallogr., 2004. 60(Pt 3): p. 613-5 [PMID:14993710] Fukushige H,Hildebrand DF A simple and efficient system for green note compound biogenesis by use of certain lipoxygenase and hydroperoxide lyase sources. J. Agric. Food Chem., 2005. 53(17): p. 6877-82 [PMID:16104814] Skrzypczak-Jankun E, et al. Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 A resolution. Acta Crystallogr. D Biol. Crystallogr., 2006. 62(Pt 7): p. 766-75 [PMID:16790932] Takamura H,Kitamura K,Kito M Inhibition by lipoxygenase-3 of n-hexanal generation in soybeans. FEBS Lett., 1991. 292(1-2): p. 42-4 [PMID:1959624] Lenis JM,Gillman JD,Lee JD,Shannon JG,Bilyeu KD Soybean seed lipoxygenase genes: molecular characterization and development of molecular marker assays. Theor. Appl. Genet., 2010. 120(6): p. 1139-49 [PMID:20058147] Zheng Y,Brash AR On the role of molecular oxygen in lipoxygenase activation: comparison and contrast of epidermal lipoxygenase-3 with soybean lipoxygenase-1. J. Biol. Chem., 2010. 285(51): p. 39876-87 [PMID:20923767] Reinprecht Y, et al. Molecular basis of seed lipoxygenase null traits in soybean line OX948. Theor. Appl. Genet., 2011. 122(7): p. 1247-64 [PMID:21243331] Lee KJ, et al. Selection and molecular characterization of a lipoxygenase-free soybean mutant line induced by gamma irradiation. Theor. Appl. Genet., 2014. 127(11): p. 2405-13 [PMID:25190478] Kanofsky JR,Axelrod B Singlet oxygen production by soybean lipoxygenase isozymes. J. Biol. Chem., 1986. 261(3): p. 1099-104 [PMID:3080416] Steczko J,Minor W,Stojanoff V,Axelrod B Crystallization and preliminary X-ray investigation of lipoxygenase-3 from soybeans. Protein Sci., 1995. 4(6): p. 1233-5 [PMID:7549886] Kramer JA,Johnson KR,Dunham WR,Sands RH,Funk MO Position 713 is critical for catalysis but not iron binding in soybean lipoxygenase 3. Biochemistry, 1994. 33(50): p. 15017-22 [PMID:7999759] Ohtsuki K, et al. A 96-kDa glycyrrhizin-binding protein (gp96) from soybeans acts as a substrate for casein kinase II, and is highly related to lipoxygenase 3. J. Biochem., 1995. 118(6): p. 1145-50 [PMID:8720128] Skrzypczak-Jankun E,Amzel LM,Kroa BA,Funk MO Structure of soybean lipoxygenase L3 and a comparison with its L1 isoenzyme. Proteins, 1997. 29(1): p. 15-31 [PMID:9294864] Pham C,Jankun J,Skrzypczak-Jankun E,Flowers RA,Funk MO Structural and thermochemical characterization of lipoxygenase-catechol complexes. Biochemistry, 1998. 37(51): p. 17952-7 [PMID:9922163]