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

Achn352311

Organism

Actinidia chinensis

Taxonomic ID

3625

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; asterids; Ericales; Actinidiaceae; Actinidia

Family

LBD

Protein Properties

Length: 676aa MW: 75433 Da PI: 8.0396

Description

LBD family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
Achn352311	genome	IKGC	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	DUF260	79.5	5.4e-25	503	580	24	101
DUF260 24 aeqpkkfanvhklFGasnvlkllkalpeeeredamsslvyeAearardPvyGavgvilklqqqleqlkaelallkeel 101 a+ p++fa++hk+FGasnv+kll ++p +r +a+ +++yeA+ar+rdPvyG+v++i++lqqq+++l+a+l ++k++l Achn352311 503 AQGPAQFAAIHKVFGASNVSKLLLHVPVPDRCEAVVTITYEAQARMRDPVYGCVAHIFALQQQVACLQAQLMQVKAQL 580 45599******************************************************************9999875 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
Gene3D	G3DSA:3.30.1740.10	2.8E-4	53	89	IPR001510	Zinc finger, PARP-type
SuperFamily	SSF57716	1.05E-19	97	189	No hit	No description
Gene3D	G3DSA:3.30.1740.10	1.3E-23	97	196	IPR001510	Zinc finger, PARP-type
PROSITE profile	PS50064	16.046	101	173	IPR001510	Zinc finger, PARP-type
SMART	SM01336	5.8E-23	104	178	IPR001510	Zinc finger, PARP-type
Pfam	PF00645	1.9E-16	104	175	IPR001510	Zinc finger, PARP-type
SuperFamily	SSF142921	1.15E-9	266	315	IPR008893	WGR domain
Pfam	PF05406	2.5E-7	269	316	IPR008893	WGR domain
Gene3D	G3DSA:1.20.142.10	4.7E-25	314	443	IPR004102	Poly(ADP-ribose) polymerase, regulatory domain
PROSITE profile	PS51060	19.329	333	461	IPR004102	Poly(ADP-ribose) polymerase, regulatory domain
Pfam	PF02877	7.6E-23	334	443	IPR004102	Poly(ADP-ribose) polymerase, regulatory domain
SuperFamily	SSF47587	1.83E-20	335	443	IPR004102	Poly(ADP-ribose) polymerase, regulatory domain
Pfam	PF00644	1.2E-10	441	504	IPR012317	Poly(ADP-ribose) polymerase, catalytic domain
SuperFamily	SSF56399	1.63E-9	442	506	No hit	No description
Gene3D	G3DSA:3.90.228.10	1.2E-12	444	504	IPR012317	Poly(ADP-ribose) polymerase, catalytic domain
PROSITE profile	PS50891	12.875	477	580	IPR004883	Lateral organ boundaries, LOB
Pfam	PF03195	5.4E-24	502	577	IPR004883	Lateral organ boundaries, LOB

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0006471	Biological Process	protein ADP-ribosylation
GO:0003677	Molecular Function	DNA binding
GO:0003950	Molecular Function	NAD+ ADP-ribosyltransferase activity
GO:0008270	Molecular Function	zinc ion binding

Sequence ? help Back to Top
Protein Sequence Length: 676 aa Download sequence Send to blast
MEGIGKGDSR STRNFCPRNL STIFQKDFHS ISSSNSSSSS KNYIYSDALI NDCTEESAFE 60 AANLDDVEGI ELLRWEDQQK IRKYVEVGGP QYTPSAAVME YGIEVSQTSR ATCRHCNQKI 120 MKGEVRISTK PDGQGARGLA WHHANCFMEL FPTTQVENVS GWNNLSAADQ AAILALVKNP 180 PSSRKDIKVE QQEDKESLQQ PASKGGSKRK KAVSYDQKAK LAKCESGAFM REGDMQDEWK 240 NQIEGAGGQV HTKIKKDTNC LVVSGLLDDK NAEMKAASYY ILQIIQEDKG SCCYVFRKWG 300 RVGNKKIGGI KLDEMDYGVN KEVSKKKNLN DAGSLLAPPL KELIKMLFNV EAYRICFIYI 360 QFCRSAMMEF EINMSEMPLG KLSKSNIQKG FEALTEIQNL VTSNVHDPSY KESLIIDASN 420 RFFTVIPSIH PHVIRDEDDL KSKYMDKPPQ GKHSTKGLGL KIPQQSEHAK WRDEVVVPCG 480 KPVASNIKAS ELMYNEYIVY NTAQGPAQFA AIHKVFGASN VSKLLLHVPV PDRCEAVVTI 540 TYEAQARMRD PVYGCVAHIF ALQQQVACLQ AQLMQVKAQL AQNLIDTRQV ENQIWPGNMV 600 AMPNFPTYAN PTCMSLSSIC PQSSLESIGR GNVDGLGGQE RERREEFCFQ TCTKKRPSQT 660 DFGELQALAL RMMRN*

Sequence ? help Back to Top

Protein Sequence Length: 676 aa Download sequence Send to blast

MEGIGKGDSR STRNFCPRNL STIFQKDFHS ISSSNSSSSS KNYIYSDALI NDCTEESAFE  60
AANLDDVEGI ELLRWEDQQK IRKYVEVGGP QYTPSAAVME YGIEVSQTSR ATCRHCNQKI  120
MKGEVRISTK PDGQGARGLA WHHANCFMEL FPTTQVENVS GWNNLSAADQ AAILALVKNP  180
PSSRKDIKVE QQEDKESLQQ PASKGGSKRK KAVSYDQKAK LAKCESGAFM REGDMQDEWK  240
NQIEGAGGQV HTKIKKDTNC LVVSGLLDDK NAEMKAASYY ILQIIQEDKG SCCYVFRKWG  300
RVGNKKIGGI KLDEMDYGVN KEVSKKKNLN DAGSLLAPPL KELIKMLFNV EAYRICFIYI  360
QFCRSAMMEF EINMSEMPLG KLSKSNIQKG FEALTEIQNL VTSNVHDPSY KESLIIDASN  420
RFFTVIPSIH PHVIRDEDDL KSKYMDKPPQ GKHSTKGLGL KIPQQSEHAK WRDEVVVPCG  480
KPVASNIKAS ELMYNEYIVY NTAQGPAQFA AIHKVFGASN VSKLLLHVPV PDRCEAVVTI  540
TYEAQARMRD PVYGCVAHIF ALQQQVACLQ AQLMQVKAQL AQNLIDTRQV ENQIWPGNMV  600
AMPNFPTYAN PTCMSLSSIC PQSSLESIGR GNVDGLGGQE RERREEFCFQ TCTKKRPSQT  660
DFGELQALAL RMMRN*

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
4dqy_C	2e-21	278	427	52	225	Poly [ADP-ribose] polymerase 1
4dqy_F	2e-21	278	427	52	225	Poly [ADP-ribose] polymerase 1
Search in ModeBase

Functional Description ? help Back to Top
Source	Description
UniProt	Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (By similarity). {ECO:0000250\|UniProtKB:P09874}.

Regulation -- Description ? help Back to Top
Source	Description
UniProt	INDUCTION: By ionising radiation (IR)-induced DNA damage. {ECO:0000269\|PubMed:11523787}.

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
Swissprot	Q9ZP54	8e-62	PARP1_ARATH; Poly [ADP-ribose] polymerase 1

Orthologous Group ? help Back to Top
Lineage	Orthologous Group ID	Taxa Number	Gene Number
Asterids	OGEA43	24	669

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT2G42430.1	8e-33	lateral organ boundaries-domain 16

Publications ? help Back to Top
Doucet-Chabeaud G,Godon C,Brutesco C,de Murcia G,Kazmaier M Ionising radiation induces the expression of PARP-1 and PARP-2 genes in Arabidopsis. Mol. Genet. Genomics, 2001. 265(6): p. 954-63 [PMID:11523787] De Block M,Verduyn C,De Brouwer D,Cornelissen M Poly(ADP-ribose) polymerase in plants affects energy homeostasis, cell death and stress tolerance. Plant J., 2005. 41(1): p. 95-106 [PMID:15610352] Vanderauwera S, et al. Silencing of poly(ADP-ribose) polymerase in plants alters abiotic stress signal transduction. Proc. Natl. Acad. Sci. U.S.A., 2007. 104(38): p. 15150-5 [PMID:17823244] Pellny TK, et al. Pyridine nucleotide cycling and control of intracellular redox state in relation to poly (ADP-ribose) polymerase activity and nuclear localization of glutathione during exponential growth of Arabidopsis cells in culture. Mol Plant, 2009. 2(3): p. 442-56 [PMID:19825628] Zhu Y, et al. Arabidopsis homologues of the histone chaperone ASF1 are crucial for chromatin replication and cell proliferation in plant development. Plant J., 2011. 66(3): p. 443-55 [PMID:21251110] Wang H,Liang Q,Cao K,Ge X Endogenous protein mono-ADP-ribosylation in Arabidopsis thaliana. Planta, 2011. 233(6): p. 1287-92 [PMID:21519881] Heyndrickx KS,Vandepoele K Systematic identification of functional plant modules through the integration of complementary data sources. Plant Physiol., 2012. 159(3): p. 884-901 [PMID:22589469] Jia Q,den Dulk-Ras A,Shen H,Hooykaas PJ,de Pater S Poly(ADP-ribose)polymerases are involved in microhomology mediated back-up non-homologous end joining in Arabidopsis thaliana. Plant Mol. Biol., 2013. 82(4-5): p. 339-51 [PMID:23625359] Boltz KA,Jasti M,Townley JM,Shippen DE Analysis of poly(ADP-Ribose) polymerases in Arabidopsis telomere biology. PLoS ONE, 2014. 9(2): p. e88872 [PMID:24551184] Bianchi AR,De Maio A Synthesis and degradation of poly(ADP-ribose) in plants. Front Biosci (Landmark Ed), 2014. 19: p. 1436-44 [PMID:24896363] Song J,Keppler BD,Wise RR,Bent AF PARP2 Is the Predominant Poly(ADP-Ribose) Polymerase in Arabidopsis DNA Damage and Immune Responses. PLoS Genet., 2015. 11(5): p. e1005200 [PMID:25950582] Pham PA, et al. Analysis of knockout mutants reveals non-redundant functions of poly(ADP-ribose)polymerase isoforms in Arabidopsis. Plant Mol. Biol., 2015. 89(4-5): p. 319-38 [PMID:26428915] Zhang H, et al. Arabidopsis PARG1 is the key factor promoting cell survival among the enzymes regulating post-translational poly(ADP-ribosyl)ation. Sci Rep, 2015. 5: p. 15892 [PMID:26516022] Shen H,Strunks GD,Klemann BJ,Hooykaas PJ,de Pater S CRISPR/Cas9-Induced Double-Strand Break Repair in Arabidopsis Nonhomologous End-Joining Mutants. G3 (Bethesda), 2017. 7(1): p. 193-202 [PMID:27866150] 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] Rissel D, et al. No Silver Bullet - Canonical Poly(ADP-Ribose) Polymerases (PARPs) Are No Universal Factors of Abiotic and Biotic Stress Resistance of Arabidopsis thaliana. Front Plant Sci, 2017. 8: p. 59 [PMID:28220129] Rissel D,Heym PP,Peiter E A yeast growth assay to characterize plant poly(ADP-ribose) polymerase (PARP) proteins and inhibitors. Anal. Biochem., 2017. 527: p. 20-23 [PMID:28408182] Varas J,Santos JL,Pradillo M The Absence of the Arabidopsis Chaperone Complex CAF-1 Produces Mitotic Chromosome Abnormalities and Changes in the Expression Profiles of Genes Involved in DNA Repair. Front Plant Sci, 2017. 8: p. 525 [PMID:28443118] Ryu TH,Kim JK,Kim JI,Kim JH Transcriptome-based biological dosimetry of gamma radiation in Arabidopsis using DNA damage response genes. J Environ Radioact, 2018. 181: p. 94-101 [PMID:29128690]