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

MDP0000428265

Organism

Malus domestica

Taxonomic ID

3750

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Rosales; Rosaceae; Maloideae; Maleae; Malus

Family

NAC

Protein Properties

Length: 1216aa MW: 136780 Da PI: 6.3989

Description

NAC family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
MDP0000428265	genome	GDR	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	NAM	158.9	2e-49	26	152	2	128
NAM 2 ppGfrFhPtdeelvveyLkkkvegkkleleevikevdiykvePwdLpkkvkaeekewyfFskrdkkyatgkrknratksgyWkatgkdkevlsk.. 95 pGfrFhPtdeelv++yL++k+++k++++ e ik++diyk++PwdLpk+ a++kewyfF+kr +ky+++ r+nr+t sg+Wkatg dk+++s+ MDP0000428265 26 LPGFRFHPTDEELVDFYLRRKIQKKPISF-ELIKSIDIYKYDPWDLPKT--AGDKEWYFFCKRGRKYKNSFRPNRVTGSGFWKATGIDKPIHSHgg 118 59***********************99.99***********44..589***********************************965 PP NAM 96 .kgelvglkktLvfykgrapkgektdWvmheyrl 128 +++ glkktLv+y+g+a kg+ktdW+mhe+rl MDP0000428265 119 eGHACNGLKKTLVYYRGSAGKGSKTDWMMHEFRL 152 444559************************98 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
PROSITE profile	PS51005	53.427	25	190	IPR003441	NAC domain
SuperFamily	SSF101941	5.23E-53	26	190	IPR003441	NAC domain
Pfam	PF02365	7.7E-25	27	152	IPR003441	NAC domain
Gene3D	G3DSA:3.40.50.300	4.9E-67	407	624	IPR027417	P-loop containing nucleoside triphosphate hydrolase
SuperFamily	SSF52540	3.66E-107	408	745	IPR027417	P-loop containing nucleoside triphosphate hydrolase
PROSITE profile	PS51722	53.319	421	748	IPR000795	Transcription factor, GTP-binding domain
Pfam	PF00009	5.2E-64	421	746	No hit	No description
TIGRFAMs	TIGR00231	2.0E-16	424	580	IPR005225	Small GTP-binding protein domain
CDD	cd01885	3.10E-119	424	634	No hit	No description
PRINTS	PR00315	2.2E-13	425	438	IPR000795	Transcription factor, GTP-binding domain
PROSITE pattern	PS00301	0	462	477	IPR031157	Tr-type G domain, conserved site
PRINTS	PR00315	2.2E-13	469	477	IPR000795	Transcription factor, GTP-binding domain
PRINTS	PR00315	2.2E-13	505	515	IPR000795	Transcription factor, GTP-binding domain
PRINTS	PR00315	2.2E-13	521	532	IPR000795	Transcription factor, GTP-binding domain
PRINTS	PR00315	2.2E-13	557	566	IPR000795	Transcription factor, GTP-binding domain
Gene3D	G3DSA:3.90.1430.10	4.3E-37	626	730	No hit	No description
Gene3D	G3DSA:2.40.30.10	1.1E-51	742	888	No hit	No description
SuperFamily	SSF50447	3.09E-39	746	880	IPR009000	Translation protein, beta-barrel domain
CDD	cd03700	7.25E-39	780	872	No hit	No description
Pfam	PF03144	4.2E-11	797	872	IPR004161	Translation elongation factor EFTu-like, domain 2
SuperFamily	SSF54980	6.83E-18	888	964	IPR009022	Elongation factor G, III-V domain
Gene3D	G3DSA:3.30.70.870	3.6E-24	890	965	No hit	No description
Pfam	PF14492	9.0E-12	891	953	IPR009022	Elongation factor G, III-V domain
CDD	cd01681	8.39E-98	963	1135	No hit	No description
SuperFamily	SSF54211	8.85E-65	966	1130	IPR020568	Ribosomal protein S5 domain 2-type fold
Gene3D	G3DSA:3.30.230.10	2.9E-67	977	1131	IPR014721	Ribosomal protein S5 domain 2-type fold, subgroup
SMART	SM00889	4.5E-26	1010	1126	IPR005517	Translation elongation factor EFG/EF2, domain IV
Pfam	PF03764	2.6E-33	1014	1126	IPR005517	Translation elongation factor EFG/EF2, domain IV
Pfam	PF00679	8.6E-10	1128	1187	IPR000640	Translation elongation factor EFG, V domain
SMART	SM00838	1.0E-4	1128	1206	IPR000640	Translation elongation factor EFG, V domain
SuperFamily	SSF54980	2.64E-15	1131	1187	IPR009022	Elongation factor G, III-V domain
CDD	cd04096	2.38E-29	1131	1200	No hit	No description
Gene3D	G3DSA:3.30.70.240	1.1E-23	1132	1187	IPR000640	Translation elongation factor EFG, V domain

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0006355	Biological Process	regulation of transcription, DNA-templated
GO:0003677	Molecular Function	DNA binding
GO:0003924	Molecular Function	GTPase activity
GO:0005525	Molecular Function	GTP binding

Sequence ? help Back to Top
Protein Sequence Length: 1216 aa Download sequence Send to blast
MDNTYYSPST KDDHQYTDDD EDDVQLPGFR FHPTDEELVD FYLRRKIQKK PISFELIKSI 60 DIYKYDPWDL PKTAGDKEWY FFCKRGRKYK NSFRPNRVTG SGFWKATGID KPIHSHGGEG 120 HACNGLKKTL VYYRGSAGKG SKTDWMMHEF RLPNSSSSNE XNNRSSNPKN MNTDPQQEAE 180 IWTLCRIFKR NVSYRKYTPD WRDLSAAKRH PTDTVNSKKF ATDRQDLLDQ SNTYISFGAS 240 DICYEEKPLV NHTNNINSXN GSHQLHAHAV GQLSSNMQQP NSTHPYMDTF SNFSFQDLEN 300 DLLNENWDEL RSVVQQLAFD PTPFPVGIIS RVRAPSLRPS LLLPNAYSLH QGIAALSPPP 360 SQLPAEAPAT EEPKKEEKVL IVFLEVTFEE ETRWYDARFA ILVQWVKFTA EELRRIMDYK 420 HNIRNMSVIA HVDHGKSTLT DSLVAAAGII AQEVAGDVRM TDTRADEAER GITIKSTGIS 480 LYYEMTDESL SRFKGERNGN EYLINLIDSP GHVDFSSEVT AALRITDGAL VVVDCIEGVC 540 VQTETVLRQA LGERIRPVLT VNKMDRCFLE LQVDGEEAYQ TFQRVIENAN VIMATYEDPL 600 LGDVQVYPEK GTVAFSAGLH GWAFTLTNFA KMYASKFGVD ESKMMERLWG ENFFDPATKK 660 WTSKNTGTAT CKRGFVQFCY EPIKQIIKTC MNDQKDKLWP MLTKLGVTMK SDEKDLMGKA 720 LMKRVMQTWL PASTALLEMM IFHLPSPSTA QRYRVENLYE GPLDDQYANA IRNCDPEGPL 780 MLYVSKMIPA SDKGRFFAFG RVFAGKVQTG LKVRIMGPNF VPGEKKDLYV KNVQRTVIWM 840 GKRQETVEDV PCGNTVALVG LDQFITKNAT LTNEKEVDAH PIRAMKFSVS PVVRVAVQCK 900 VASDLPKLVE GLKRLAKSDP MVVCSIEESG EHIIAGAGEL HLEICLKDLQ DDFMGGAEII 960 KSDPVVSFRE TVLDKSCRTV MSKSPNKHNR LYMEARPLEE GLPEAIDXGR IGPRDDPKIR 1020 SKILAEEFGW DKDLAKKIWC FGPETTGPNM VVDMCKGVQY LNEIKDSVVA GFQWASKEGA 1080 LAEENMRGIC FEVCDVVLHA DAIHRGGGQV IPTARRVIYA SQLTAKPRLL EPVYLVEIQA 1140 PEGALGGIYS VLNQKRGHVF EEMQRPGTPL YNIKAYLPXV ESFGFSGKST LTDSLVAAAG 1200 IIAQEVAGDV RMTDM*

Sequence ? help Back to Top

Protein Sequence Length: 1216 aa Download sequence Send to blast

MDNTYYSPST KDDHQYTDDD EDDVQLPGFR FHPTDEELVD FYLRRKIQKK PISFELIKSI  60
DIYKYDPWDL PKTAGDKEWY FFCKRGRKYK NSFRPNRVTG SGFWKATGID KPIHSHGGEG  120
HACNGLKKTL VYYRGSAGKG SKTDWMMHEF RLPNSSSSNE XNNRSSNPKN MNTDPQQEAE  180
IWTLCRIFKR NVSYRKYTPD WRDLSAAKRH PTDTVNSKKF ATDRQDLLDQ SNTYISFGAS  240
DICYEEKPLV NHTNNINSXN GSHQLHAHAV GQLSSNMQQP NSTHPYMDTF SNFSFQDLEN  300
DLLNENWDEL RSVVQQLAFD PTPFPVGIIS RVRAPSLRPS LLLPNAYSLH QGIAALSPPP  360
SQLPAEAPAT EEPKKEEKVL IVFLEVTFEE ETRWYDARFA ILVQWVKFTA EELRRIMDYK  420
HNIRNMSVIA HVDHGKSTLT DSLVAAAGII AQEVAGDVRM TDTRADEAER GITIKSTGIS  480
LYYEMTDESL SRFKGERNGN EYLINLIDSP GHVDFSSEVT AALRITDGAL VVVDCIEGVC  540
VQTETVLRQA LGERIRPVLT VNKMDRCFLE LQVDGEEAYQ TFQRVIENAN VIMATYEDPL  600
LGDVQVYPEK GTVAFSAGLH GWAFTLTNFA KMYASKFGVD ESKMMERLWG ENFFDPATKK  660
WTSKNTGTAT CKRGFVQFCY EPIKQIIKTC MNDQKDKLWP MLTKLGVTMK SDEKDLMGKA  720
LMKRVMQTWL PASTALLEMM IFHLPSPSTA QRYRVENLYE GPLDDQYANA IRNCDPEGPL  780
MLYVSKMIPA SDKGRFFAFG RVFAGKVQTG LKVRIMGPNF VPGEKKDLYV KNVQRTVIWM  840
GKRQETVEDV PCGNTVALVG LDQFITKNAT LTNEKEVDAH PIRAMKFSVS PVVRVAVQCK  900
VASDLPKLVE GLKRLAKSDP MVVCSIEESG EHIIAGAGEL HLEICLKDLQ DDFMGGAEII  960
KSDPVVSFRE TVLDKSCRTV MSKSPNKHNR LYMEARPLEE GLPEAIDXGR IGPRDDPKIR  1020
SKILAEEFGW DKDLAKKIWC FGPETTGPNM VVDMCKGVQY LNEIKDSVVA GFQWASKEGA  1080
LAEENMRGIC FEVCDVVLHA DAIHRGGGQV IPTARRVIYA SQLTAKPRLL EPVYLVEIQA  1140
PEGALGGIYS VLNQKRGHVF EEMQRPGTPL YNIKAYLPXV ESFGFSGKST LTDSLVAAAG  1200
IIAQEVAGDV RMTDM*

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
4v6w_Az	0.0	406	1187	2	784	Elongation factor 2
Search in ModeBase

Expression -- UniGene ? help Back to Top
UniGene ID	E-value	Expressed in
Mdo.5420	0.0	bud\| cell culture\| flower\| fruit\| leaf\| root\| stem

Expression -- Description ? help Back to Top
Source	Description
Uniprot	TISSUE SPECIFICITY: Expressed in root, stem, leaves, flowers and siliques. {ECO:0000269\|PubMed:12032361}.

Functional Description ? help Back to Top
Source	Description
UniProt	Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). Involved in cold responses leading to freezing tolerance via the induction of cold-responsive genes (PubMed:9401119, PubMed:12032361). {ECO:0000250\|UniProtKB:P32324, ECO:0000269\|PubMed:12032361, ECO:0000269\|PubMed:9401119}.

Regulation -- Description ? help Back to Top
Source	Description
UniProt	INDUCTION: Induced by cold. {ECO:0000269\|PubMed:12032361}.

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	JQ732180	0.0	JQ732180.1 Prunus persica translation elongation factor 2 (TEF2) mRNA, complete cds.

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_028958612.1	0.0	elongation factor 2
Refseq	XP_028958613.1	0.0	elongation factor 2
Swissprot	Q9ASR1	0.0	EF2_ARATH; Elongation factor 2
TrEMBL	A0A498JZA1	0.0	A0A498JZA1_MALDO; Uncharacterized protein
STRING	XP_009361805.1	0.0	(Pyrus x bretschneideri)

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT3G12910.1	5e-78	NAC family protein

Link Out ? help Back to Top
Phytozome	MDP0000428265

Publications ? help Back to Top
Yamazaki D,Motohashi K,Kasama T,Hara Y,Hisabori T Target proteins of the cytosolic thioredoxins in Arabidopsis thaliana. Plant Cell Physiol., 2004. 45(1): p. 18-27 [PMID:14749482] Rajjou L, et al. The effect of alpha-amanitin on the Arabidopsis seed proteome highlights the distinct roles of stored and neosynthesized mRNAs during germination. Plant Physiol., 2004. 134(4): p. 1598-613 [PMID:15047896] Slabas AR,Ndimba B,Simon WJ,Chivasa S Proteomic analysis of the Arabidopsis cell wall reveals unexpected proteins with new cellular locations. Biochem. Soc. Trans., 2004. 32(Pt3): p. 524-8 [PMID:15157177] Wienkoop S, et al. Cell-specific protein profiling in Arabidopsis thaliana trichomes: identification of trichome-located proteins involved in sulfur metabolism and detoxification. Phytochemistry, 2004. 65(11): p. 1641-9 [PMID:15276459] Job C,Rajjou L,Lovigny Y,Belghazi M,Job D Patterns of protein oxidation in Arabidopsis seeds and during germination. Plant Physiol., 2005. 138(2): p. 790-802 [PMID:15908592] Rouhier N, et al. Identification of plant glutaredoxin targets. Antioxid. Redox Signal., 2005 Jul-Aug. 7(7-8): p. 919-29 [PMID:15998247] Noir S,Bräutigam A,Colby T,Schmidt J,Panstruga R A reference map of the Arabidopsis thaliana mature pollen proteome. Biochem. Biophys. Res. Commun., 2005. 337(4): p. 1257-66 [PMID:16242667] Ndimba BK,Chivasa S,Simon WJ,Slabas AR Identification of Arabidopsis salt and osmotic stress responsive proteins using two-dimensional difference gel electrophoresis and mass spectrometry. Proteomics, 2005. 5(16): p. 4185-96 [PMID:16254930] Giavalisco P,Kapitza K,Kolasa A,Buhtz A,Kehr J Towards the proteome of Brassica napus phloem sap. Proteomics, 2006. 6(3): p. 896-909 [PMID:16400686] Kung CC,Huang WN,Huang YC,Yeh KC Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry. Proteomics, 2006. 6(9): p. 2746-58 [PMID:16526091] Rajjou L, et al. Proteomic investigation of the effect of salicylic acid on Arabidopsis seed germination and establishment of early defense mechanisms. Plant Physiol., 2006. 141(3): p. 910-23 [PMID:16679420] Chibani K, et al. Proteomic analysis of seed dormancy in Arabidopsis. Plant Physiol., 2006. 142(4): p. 1493-510 [PMID:17028149] Devos S, et al. A hormone and proteome approach to picturing the initial metabolic events during Plasmodiophora brassicae infection on Arabidopsis. Mol. Plant Microbe Interact., 2006. 19(12): p. 1431-43 [PMID:17153927] Marmagne A, et al. A high content in lipid-modified peripheral proteins and integral receptor kinases features in the arabidopsis plasma membrane proteome. Mol. Cell Proteomics, 2007. 6(11): p. 1980-96 [PMID:17644812] Jamet E, et al. Recent advances in plant cell wall proteomics. Proteomics, 2008. 8(4): p. 893-908 [PMID:18210371] Rutschow H,Ytterberg AJ,Friso G,Nilsson R,van Wijk KJ Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis. Plant Physiol., 2008. 148(1): p. 156-75 [PMID:18633119] Lenman M,Sörensson C,Andreasson E Enrichment of phosphoproteins and phosphopeptide derivatization identify universal stress proteins in elicitor-treated Arabidopsis. Mol. Plant Microbe Interact., 2008. 21(10): p. 1275-84 [PMID:18785823] Hajduch M, et al. Systems analysis of seed filling in Arabidopsis: using general linear modeling to assess concordance of transcript and protein expression. Plant Physiol., 2010. 152(4): p. 2078-87 [PMID:20118269] Ge W, et al. Proteomic analyses of apoplastic proteins from germinating Arabidopsis thaliana pollen. Biochim. Biophys. Acta, 2011. 1814(12): p. 1964-73 [PMID:21798377] Fares A,Rossignol M,Peltier JB Proteomics investigation of endogenous S-nitrosylation in Arabidopsis. Biochem. Biophys. Res. Commun., 2011. 416(3-4): p. 331-6 [PMID:22115780] Miao C,Liu F,Zhao Q,Jia Z,Song S A proteomic analysis of Arabidopsis thaliana seedling responses to 3-oxo-octanoyl-homoserine lactone, a bacterial quorum-sensing signal. Biochem. Biophys. Res. Commun., 2012. 427(2): p. 293-8 [PMID:22995300] Ueoka-Nakanishi H, et al. Thioredoxin h regulates calcium dependent protein kinases in plasma membranes. FEBS J., 2013. 280(14): p. 3220-31 [PMID:23615222] Černý M, et al. Proteome and metabolome profiling of cytokinin action in Arabidopsis identifying both distinct and similar responses to cytokinin down- and up-regulation. J. Exp. Bot., 2013. 64(14): p. 4193-206 [PMID:24064926] Ishitani M,Xiong L,Stevenson B,Zhu JK Genetic analysis of osmotic and cold stress signal transduction in Arabidopsis: interactions and convergence of abscisic acid-dependent and abscisic acid-independent pathways. Plant Cell, 1997. 9(11): p. 1935-49 [PMID:9401119]