PlantTFDB - Plant Transcription Factor Database @ CBI, PKU

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus

Family

NAC

Protein Properties

Length: 792aa MW: 88825.9 Da PI: 5.8778

Description

NAC family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
RrC1791_p3	genome	MSU	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	NAM	99.2	5.8e-31	381	515	1	128
NAM 1 lppGfrFhPtdeelvveyLkkk.vegkk....leleevikevd....iykvePwdLpkkvkaeekewyfFskrdkkyatgkrknratk.....sgyWka 85 lp+G++F+P+d e++++ L+k+ + g + ++ e+i++v+ i++++P++Lp vk++ + +fF+++ k+y+tg+rk+r+++ + +W++ RrC1791_p3 381 LPRGVKFDPSDPEIIWHLLAKSgLLGLSshpfID--EFIPTVNqddgICYTHPKNLP-GVKQDGTVSHFFHRAIKAYSTGTRKRRKIHdddfgDVRWHK 476 699**********9999988544444443422..33544433345******.677888999**************86555655889* PP NAM 86 tgkdkevlskkgelvglkktLvfykgrapkgektdWvmheyrl 128 tg++k+v+ +g + g+kk++v+y g+a kt+Wvmh+y+l RrC1791_p3 477 TGRTKPVVL-DGVQRGCKKIMVLYGGKAV---KTNWVMHQYHL 515 *******.99********76665...6******98 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
Pfam	PF04502	6.2E-65	11	307	IPR007590	CWC16 protein
SuperFamily	SSF101941	1.44E-36	366	534	IPR003441	NAC domain
PROSITE profile	PS51005	30.849	381	534	IPR003441	NAC domain
Pfam	PF02365	5.3E-12	382	515	IPR003441	NAC domain

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0000077	Biological Process	DNA damage checkpoint
GO:0006355	Biological Process	regulation of transcription, DNA-templated
GO:0010332	Biological Process	response to gamma radiation
GO:0040020	Biological Process	regulation of meiotic nuclear division
GO:0003677	Molecular Function	DNA binding

Sequence ? help Back to Top
Protein Sequence Length: 792 aa Download sequence Send to blast
MSTLSAARAD NFYYPPEWTP DQGSLNKFQG QHPLRERARK LGEGILIIRF EMPYNIWCGG 60 CNSMIAKGVR FNAEKKQVGN YYSTKIWSFA MKAPCCKQEI VIQTDPQNCE YVITSGAQKK 120 VEEYDVEDAE TMELTAEEEK GKLADPFYRL EHQEVDLQKK KAAEPLLVRL QRVSDARHAD 180 DYSLNKALRA QIRGHRKRVA EEEAASRKLG LGIRLLPKSE EDVAAASNVK FKSKFDKNRK 240 DKRALIHSSS IFPESSYSMS SSSSKKRLEL EAKRRKICAA SASSLLSGGF KASSLSKNPS 300 SASKSKSSIV SLISINSMSH VISKSRRSWL VDSNRIATKI KSASGQHDPH QVVWNSNPTK 360 HCPNCHHVID NNDEVDDWPG LPRGVKFDPS DPEIIWHLLA KSGLLGLSSH PFIDEFIPTV 420 NQDDGICYTH PKNLPGVKQD GTVSHFFHRA IKAYSTGTRK RRKIHDDDFG DVRWHKTGRT 480 KPVVLDGVQR GCKKIMVLYG GKAVKTNWVM HQYHLGTDED EKDGDYVVSK IFYQQPQQIL 540 KQGGGDKGEQ DVSDDIFAAT TTPKSDPLTP KLFTPEPPQA VRLCSDSHFA DDYVAAPEVS 600 LAEISEAVYM EDEVQGVQRN HERTSSEDEP GAPETWIENR DNEIMVYDEE EKENGKEDGN 660 NQEDRERYEN ENQAAAEEDG NDQDPNWFDS GGSQFILDSQ QLVEHLSLCD DLLQVGSQDA 720 NNGGGSRNKQ PCFGDYAHLG GSEAFKRDLE DCQKLVLDPS NIDLDTPPEF RLSQLEFGSQ 780 ESFLAWGTGK TD

Sequence ? help Back to Top

Protein Sequence Length: 792 aa Download sequence Send to blast

MSTLSAARAD NFYYPPEWTP DQGSLNKFQG QHPLRERARK LGEGILIIRF EMPYNIWCGG  60
CNSMIAKGVR FNAEKKQVGN YYSTKIWSFA MKAPCCKQEI VIQTDPQNCE YVITSGAQKK  120
VEEYDVEDAE TMELTAEEEK GKLADPFYRL EHQEVDLQKK KAAEPLLVRL QRVSDARHAD  180
DYSLNKALRA QIRGHRKRVA EEEAASRKLG LGIRLLPKSE EDVAAASNVK FKSKFDKNRK  240
DKRALIHSSS IFPESSYSMS SSSSKKRLEL EAKRRKICAA SASSLLSGGF KASSLSKNPS  300
SASKSKSSIV SLISINSMSH VISKSRRSWL VDSNRIATKI KSASGQHDPH QVVWNSNPTK  360
HCPNCHHVID NNDEVDDWPG LPRGVKFDPS DPEIIWHLLA KSGLLGLSSH PFIDEFIPTV  420
NQDDGICYTH PKNLPGVKQD GTVSHFFHRA IKAYSTGTRK RRKIHDDDFG DVRWHKTGRT  480
KPVVLDGVQR GCKKIMVLYG GKAVKTNWVM HQYHLGTDED EKDGDYVVSK IFYQQPQQIL  540
KQGGGDKGEQ DVSDDIFAAT TTPKSDPLTP KLFTPEPPQA VRLCSDSHFA DDYVAAPEVS  600
LAEISEAVYM EDEVQGVQRN HERTSSEDEP GAPETWIENR DNEIMVYDEE EKENGKEDGN  660
NQEDRERYEN ENQAAAEEDG NDQDPNWFDS GGSQFILDSQ QLVEHLSLCD DLLQVGSQDA  720
NNGGGSRNKQ PCFGDYAHLG GSEAFKRDLE DCQKLVLDPS NIDLDTPPEF RLSQLEFGSQ  780
ESFLAWGTGK TD

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
5yzg_Y	1e-12	4	196	1	177	Coiled-coil domain-containing protein 94
Search in ModeBase

Functional Description ? help Back to Top
Source	Description
UniProt	Transcription factor regulating the transcriptional activation response to gamma irradiation (PubMed:19549833). Required for stem-cell death induced by UVB or by gamma irradiation (PubMed:20634150). Not required for ATM activation, but participates in pathways governed by both ATM and ATR sensor kinases (PubMed:19549833). Involved in DNA damage response (DDR) system that regulates cell cycle arrest (PubMed:24399300). Functional homolog of animal p53 (PubMed:24736489). Regulates SMR5 and SMR7 transcription (PubMed:24399300). Regulates DNA repair and cytokinin signaling separately and plays a key role in controlling lateral root formation under genotoxic stress. {ECO:0000269\|PubMed:19549833, ECO:0000269\|PubMed:20634150, ECO:0000269\|PubMed:24399300, ECO:0000305\|PubMed:24736489}.

Regulation -- Description ? help Back to Top
Source	Description
UniProt	INDUCTION: Not induced by zeocin or ionizing radiation treatment. {ECO:0000269\|PubMed:23907539}.

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_018433044.1	0.0	PREDICTED: NAC domain-containing protein 8-like
Refseq	XP_018486643.1	0.0	PREDICTED: NAC domain-containing protein 8-like
Swissprot	Q6NQK2	0.0	NAC8_ARATH; SUPPRESSOR OF GAMMA RESPONSE 1
TrEMBL	A0A397XYK3	0.0	A0A397XYK3_BRACM; Uncharacterized protein
STRING	Bra024733.1-P	0.0	(Brassica rapa)

Orthologous Group ? help Back to Top
Lineage	Orthologous Group ID	Taxa Number	Gene Number
Malvids	OGEM9707	27	36

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT1G25580.1	0.0	NAC family protein

Publications ? help Back to Top
Yi D, et al. The Arabidopsis SIAMESE-RELATED cyclin-dependent kinase inhibitors SMR5 and SMR7 regulate the DNA damage checkpoint in response to reactive oxygen species. Plant Cell, 2014. 26(1): p. 296-309 [PMID:24399300] Biever JJ,Brinkman D,Gardner G UV-B inhibition of hypocotyl growth in etiolated Arabidopsis thaliana seedlings is a consequence of cell cycle arrest initiated by photodimer accumulation. J. Exp. Bot., 2014. 65(11): p. 2949-61 [PMID:24591052] Hu Z,Cools T,Kalhorzadeh P,Heyman J,De Veylder L Deficiency of the Arabidopsis helicase RTEL1 triggers a SOG1-dependent replication checkpoint in response to DNA cross-links. Plant Cell, 2015. 27(1): p. 149-61 [PMID:25595823] Chen P,Umeda M DNA double-strand breaks induce the expression of flavin-containing monooxygenase and reduce root meristem size in Arabidopsis thaliana. Genes Cells, 2015. 20(8): p. 636-46 [PMID:26033196] Sjogren CA,Bolaris SC,Larsen PB Aluminum-Dependent Terminal Differentiation of the Arabidopsis Root Tip Is Mediated through an ATR-, ALT2-, and SOG1-Regulated Transcriptional Response. Plant Cell, 2015. 27(9): p. 2501-15 [PMID:26320227] Yoshiyama KO SOG1: a master regulator of the DNA damage response in plants. Genes Genet. Syst., 2016. 90(4): p. 209-16 [PMID:26617076] Weimer AK, et al. The plant-specific CDKB1-CYCB1 complex mediates homologous recombination repair in Arabidopsis. EMBO J., 2016. 35(19): p. 2068-2086 [PMID:27497297] Davis OM,Ogita N,Inagaki S,Takahashi N,Umeda M DNA damage inhibits lateral root formation by up-regulating cytokinin biosynthesis genes in Arabidopsis thaliana. Genes Cells, 2016. 21(11): p. 1195-1208 [PMID:27658920] Pedroza-García JA, et al. Function of the Plant DNA Polymerase Epsilon in Replicative Stress Sensing, a Genetic Analysis. Plant Physiol., 2017. 173(3): p. 1735-1749 [PMID:28153919] Horvath BM, et al. Arabidopsis RETINOBLASTOMA RELATED directly regulates DNA damage responses through functions beyond cell cycle control. EMBO J., 2017. 36(9): p. 1261-1278 [PMID:28320736] Sjogren CA,Larsen PB SUV2, which encodes an ATR-related cell cycle checkpoint and putative plant ATRIP, is required for aluminium-dependent root growth inhibition in Arabidopsis. Plant Cell Environ., 2017. 40(9): p. 1849-1860 [PMID:28556304] Yoshiyama KO,Kaminoyama K,Sakamoto T,Kimura S Increased Phosphorylation of Ser-Gln Sites on SUPPRESSOR OF GAMMA RESPONSE1 Strengthens the DNA Damage Response in Arabidopsis thaliana. Plant Cell, 2017. 29(12): p. 3255-3268 [PMID:29208704] Johnson RA, et al. SUPPRESSOR OF GAMMA RESPONSE1 Links DNA Damage Response to Organ Regeneration. Plant Physiol., 2018. 176(2): p. 1665-1675 [PMID:29222192] Ogita N, et al. Identifying the target genes of SUPPRESSOR OF GAMMA RESPONSE 1, a master transcription factor controlling DNA damage response in Arabidopsis. Plant J., 2018. 94(3): p. 439-453 [PMID:29430765] Cao X, et al. Roles of MSH2 and MSH6 in cadmium-induced G2/M checkpoint arrest in Arabidopsis roots. Chemosphere, 2018. 201: p. 586-594 [PMID:29533809]