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

CCG027008.3

Organism

Populus euphratica

Taxonomic ID

75702

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus

Family

G2-like

Protein Properties

Length: 1786aa MW: 201095 Da PI: 7.5397

Description

G2-like family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
CCG027008.3	genome	LZU	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	G2-like	102	3.9e-32	264	318	1	55
G2-like 1 kprlrWtpeLHerFveaveqLGGsekAtPktilelmkvkgLtlehvkSHLQkYRl 55 kpr+rWtpeLHe+Fveav++LGGse+AtPk +l+ mkv++Lt++hvkSHLQkYR+ CCG027008.3 264 KPRMRWTPELHEAFVEAVNNLGGSERATPKGVLKRMKVDSLTIYHVKSHLQKYRT 318 79****************************************************8 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
PROSITE profile	PS51294	12.961	261	321	IPR017930	Myb domain
SuperFamily	SSF46689	9.85E-17	262	318	IPR009057	Homeodomain-like
Gene3D	G3DSA:1.10.10.60	3.5E-29	263	320	IPR009057	Homeodomain-like
TIGRFAMs	TIGR01557	2.7E-23	264	318	IPR006447	Myb domain, plants
Pfam	PF00249	1.4E-8	266	317	IPR001005	SANT/Myb domain
Pfam	PF14379	1.3E-23	349	396	IPR025756	MYB-CC type transcription factor, LHEQLE-containing domain
Gene3D	G3DSA:3.30.40.10	2.5E-29	523	608	IPR013083	Zinc finger, RING/FYVE/PHD-type
SuperFamily	SSF57850	1.14E-33	524	604	No hit	No description
Pfam	PF14569	2.0E-36	529	601	IPR027934	Cellulose synthase, RING-type zinc finger
Pfam	PF03552	0	805	1365	IPR005150	Cellulose synthase
SuperFamily	SSF53448	1.58E-9	818	875	IPR029044	Nucleotide-diphospho-sugar transferases
SuperFamily	SSF53448	1.58E-9	973	1032	IPR029044	Nucleotide-diphospho-sugar transferases
SuperFamily	SSF53448	1.58E-9	1070	1129	IPR029044	Nucleotide-diphospho-sugar transferases
SuperFamily	SSF53448	1.58E-9	1225	1344	IPR029044	Nucleotide-diphospho-sugar transferases
Pfam	PF03552	3.8E-209	1387	1778	IPR005150	Cellulose synthase

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0030244	Biological Process	cellulose biosynthetic process
GO:0016020	Cellular Component	membrane
GO:0003677	Molecular Function	DNA binding
GO:0016760	Molecular Function	cellulose synthase (UDP-forming) activity

Sequence ? help Back to Top
Protein Sequence Length: 1786 aa Download sequence Send to blast
MEGRPAFSIQ RAGAKQLGNL GVSGTLSSSL PVVPTPLEET YPKLPGCQQV SMERELMTRP 60 LVHASHLPSN NGVVGHLFSS SASFSTDLQY SSVTPREKHS RNTSFISQSS ANEGALLMSQ 120 SSPSALLQST TTSHYINENS ASWCPESPPG FLDFPTNTTV QTNQIESNSC AGVMASEEFG 180 KRNDWQEWAD QLITDDDALT TNWNELLADT SIVDMEPKMA YQVSKPSSNI PVQHSQGHLK 240 LPSPSAEIHP VLTPTSSANS APTKPRMRWT PELHEAFVEA VNNLGGSERA TPKGVLKRMK 300 VDSLTIYHVK SHLQKYRTAR YRPESSEGSS EKRLTSIDEI SSLDLKTGIE ITEALRLQME 360 VQKRLHEQLE IQRNLQLRIE EQGRHLQMMF EKQCKSGIDV DKLKAASSAS ENPSTLSSDA 420 IQDSPAKNDL ETPQLDCGKT PTDTIYANPA LEGGSQDLNR KHKVGVDWSV TAGRCMMLSL 480 QNQGVRNKLG CKTEPGLVFF LLLSMAGLVT GSSQTLHAKD ELRPPTRQSA TSKKCRVCGD 540 EIGVKEDGEV FVACHVCGFP VCRPCYEYER SEGNQSCPQC NTRYKRHRGC PRVPGDNDDD 600 DANFDDFDDE FQIKHHDHDE SNQKNVFSHT EIEHYNEQEM HPIRPAFSSA GSVAGKDLEG 660 EKEGYSNAEW QERVEKWKFR QEKRGLVSKD DGGNDQGEED EYLMAEARQP LWRKIPIPSS 720 RINPYRIVIV LRLIILCFFF RFRILTPAYD AYALWLISVI CEVWFGLSWI LDQFPKWNPI 780 ERETYLDRLS MRFEREGEPN RLGPVDVFVS TVDPLKEPPI ITANTVLSIL SVDYPVDKVS 840 CYVSDDGASM LLFDSLAETA EFARRWVPFC KKHNIEPRAP EFYFTQKIDY LKDKVHPNFV 900 KERRAMKREY EEFKVRINAL VSKAQKKPEE GWVMQDGTPW PGNITRDHPG MIQVYLGSEG 960 ALDVEGKELP RLVYVSREKR PGYNHHKKAG AMNALIRVSA VLTNAPFMLN LDCDHYINNS 1020 KAVREAMCFL MDPQLGKKLC YVQFPQRFDG IDRHDRYANR NVVFFDINMK GLDGIQGPVY 1080 VGTGCVFNRQ SLYGYDPPVS EKRPKMTCDC WPSWCCCCCG GSRKKSKKKG QRSLLGGLYP 1140 MKKKMMGKKY TRKASGPVFD LEEIEEGLEG YEELEKSSLM SQKSFEKRFG QSPVFIASTL 1200 MENGGLPEGT NSQSHIKEAI HVISCGYEEK TEWGKEVGWI YGSVTEDILT GFKMHCRGWR 1260 SVYCSPQRPA FKGSAPINLS DRLHQVLRWA LGSIEIFLSH HCPLWYGYGG KLKLLERLAY 1320 INTIVYPFTS IPLLAYCTIP AVCLLTGKFI IPTLNNLASI WFLALSKKKG QRSLLGGLYP 1380 MKKKMMGKKY TRKPSGPVFD LEEIEEGLEG YEELEKSSLM SQKSFEKRFG QSPVFIASTL 1440 MENGGLPEGT NSQSHIKEAI HVISCGYEEK TEWGKEVGWI YGSVTEDILT GFKMHCRGWR 1500 SVYCSPQRPA FKGSAPINLS DRLHQVLRWA LGSIEIFLSH HCPLWYGYGG KLKLLERLAY 1560 INTIVYPFTS IPLLAYCTIP AVCLLTGKFI IPTLNNLASI WFLALFISII ATSVLELRWS 1620 GVSIQDLWRN EQFWVIGGVS AHLFAVFQGL LKVLGGVDTN FTVTSKSADD TEFGELYLFK 1680 WTTLLIPPTT LIILNMVGVV AGVSDAINNG YGSWGPLFGK LFFAFWVIVH LYPFLKGLMG 1740 RQNRTPTIVV LWSILLASIF SLIWVRIDPF LPKQTGPILK QCGVEC

Sequence ? help Back to Top

Protein Sequence Length: 1786 aa Download sequence Send to blast

MEGRPAFSIQ RAGAKQLGNL GVSGTLSSSL PVVPTPLEET YPKLPGCQQV SMERELMTRP  60
LVHASHLPSN NGVVGHLFSS SASFSTDLQY SSVTPREKHS RNTSFISQSS ANEGALLMSQ  120
SSPSALLQST TTSHYINENS ASWCPESPPG FLDFPTNTTV QTNQIESNSC AGVMASEEFG  180
KRNDWQEWAD QLITDDDALT TNWNELLADT SIVDMEPKMA YQVSKPSSNI PVQHSQGHLK  240
LPSPSAEIHP VLTPTSSANS APTKPRMRWT PELHEAFVEA VNNLGGSERA TPKGVLKRMK  300
VDSLTIYHVK SHLQKYRTAR YRPESSEGSS EKRLTSIDEI SSLDLKTGIE ITEALRLQME  360
VQKRLHEQLE IQRNLQLRIE EQGRHLQMMF EKQCKSGIDV DKLKAASSAS ENPSTLSSDA  420
IQDSPAKNDL ETPQLDCGKT PTDTIYANPA LEGGSQDLNR KHKVGVDWSV TAGRCMMLSL  480
QNQGVRNKLG CKTEPGLVFF LLLSMAGLVT GSSQTLHAKD ELRPPTRQSA TSKKCRVCGD  540
EIGVKEDGEV FVACHVCGFP VCRPCYEYER SEGNQSCPQC NTRYKRHRGC PRVPGDNDDD  600
DANFDDFDDE FQIKHHDHDE SNQKNVFSHT EIEHYNEQEM HPIRPAFSSA GSVAGKDLEG  660
EKEGYSNAEW QERVEKWKFR QEKRGLVSKD DGGNDQGEED EYLMAEARQP LWRKIPIPSS  720
RINPYRIVIV LRLIILCFFF RFRILTPAYD AYALWLISVI CEVWFGLSWI LDQFPKWNPI  780
ERETYLDRLS MRFEREGEPN RLGPVDVFVS TVDPLKEPPI ITANTVLSIL SVDYPVDKVS  840
CYVSDDGASM LLFDSLAETA EFARRWVPFC KKHNIEPRAP EFYFTQKIDY LKDKVHPNFV  900
KERRAMKREY EEFKVRINAL VSKAQKKPEE GWVMQDGTPW PGNITRDHPG MIQVYLGSEG  960
ALDVEGKELP RLVYVSREKR PGYNHHKKAG AMNALIRVSA VLTNAPFMLN LDCDHYINNS  1020
KAVREAMCFL MDPQLGKKLC YVQFPQRFDG IDRHDRYANR NVVFFDINMK GLDGIQGPVY  1080
VGTGCVFNRQ SLYGYDPPVS EKRPKMTCDC WPSWCCCCCG GSRKKSKKKG QRSLLGGLYP  1140
MKKKMMGKKY TRKASGPVFD LEEIEEGLEG YEELEKSSLM SQKSFEKRFG QSPVFIASTL  1200
MENGGLPEGT NSQSHIKEAI HVISCGYEEK TEWGKEVGWI YGSVTEDILT GFKMHCRGWR  1260
SVYCSPQRPA FKGSAPINLS DRLHQVLRWA LGSIEIFLSH HCPLWYGYGG KLKLLERLAY  1320
INTIVYPFTS IPLLAYCTIP AVCLLTGKFI IPTLNNLASI WFLALSKKKG QRSLLGGLYP  1380
MKKKMMGKKY TRKPSGPVFD LEEIEEGLEG YEELEKSSLM SQKSFEKRFG QSPVFIASTL  1440
MENGGLPEGT NSQSHIKEAI HVISCGYEEK TEWGKEVGWI YGSVTEDILT GFKMHCRGWR  1500
SVYCSPQRPA FKGSAPINLS DRLHQVLRWA LGSIEIFLSH HCPLWYGYGG KLKLLERLAY  1560
INTIVYPFTS IPLLAYCTIP AVCLLTGKFI IPTLNNLASI WFLALFISII ATSVLELRWS  1620
GVSIQDLWRN EQFWVIGGVS AHLFAVFQGL LKVLGGVDTN FTVTSKSADD TEFGELYLFK  1680
WTTLLIPPTT LIILNMVGVV AGVSDAINNG YGSWGPLFGK LFFAFWVIVH LYPFLKGLMG  1740
RQNRTPTIVV LWSILLASIF SLIWVRIDPF LPKQTGPILK QCGVEC

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
5jnp_A	9e-69	848	973	3	128	Probable cellulose synthase A catalytic subunit 8 [UDP-forming]
5jnp_B	9e-69	848	973	3	128	Probable cellulose synthase A catalytic subunit 8 [UDP-forming]
Search in ModeBase

Functional Description ? help Back to Top
Source	Description
UniProt	Catalytic subunit of cellulose synthase terminal complexes ('rosettes'), required for beta-1,4-glucan microfibril crystallization, a major mechanism of the cell wall formation. Involved in the secondary cell wall formation. Required for the xylem cell wall thickening. {ECO:0000269\|PubMed:12538856, ECO:0000269\|PubMed:17351116}.

Annotation -- Nucleotide ? help Back to Top
Source	Hit ID	E-value	Description
GenBank	AY573571	0.0	AY573571.1 Populus tremula x Populus tremuloides cellulose synthase (CesA1) mRNA, complete cds.

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_002301856.2	0.0	cellulose synthase A catalytic subunit 4 [UDP-forming]
Swissprot	Q84JA6	0.0	CESA4_ARATH; Cellulose synthase A catalytic subunit 4 [UDP-forming]
TrEMBL	W9RB71	0.0	W9RB71_9ROSA; Cellulose synthase
STRING	XP_010091789.1	0.0	(Morus notabilis)

Orthologous Group ? help Back to Top
Lineage	Orthologous Group ID	Taxa Number	Gene Number
Fabids	OGEF1512	34	98

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT4G28610.1	1e-103	phosphate starvation response 1

Publications ? help Back to Top
Holland N, et al. A comparative analysis of the plant cellulose synthase (CesA) gene family. Plant Physiol., 2000. 123(4): p. 1313-24 [PMID:10938350] Richmond T Higher plant cellulose synthases. Genome Biol., 2000. 1(4): p. REVIEWS3001 [PMID:11178255] Beeckman T, et al. Genetic complexity of cellulose synthase a gene function in Arabidopsis embryogenesis. Plant Physiol., 2002. 130(4): p. 1883-93 [PMID:12481071] Taylor NG,Howells RM,Huttly AK,Vickers K,Turner SR Interactions among three distinct CesA proteins essential for cellulose synthesis. Proc. Natl. Acad. Sci. U.S.A., 2003. 100(3): p. 1450-5 [PMID:12538856] Gardiner JC,Taylor NG,Turner SR Control of cellulose synthase complex localization in developing xylem. Plant Cell, 2003. 15(8): p. 1740-8 [PMID:12897249] Nühse TS,Stensballe A,Jensen ON,Peck SC Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell, 2004. 16(9): p. 2394-405 [PMID:15308754] Sibout R, et al. CINNAMYL ALCOHOL DEHYDROGENASE-C and -D are the primary genes involved in lignin biosynthesis in the floral stem of Arabidopsis. Plant Cell, 2005. 17(7): p. 2059-76 [PMID:15937231] Brembu T,Winge P,Bones AM The small GTPase AtRAC2/ROP7 is specifically expressed during late stages of xylem differentiation in Arabidopsis. J. Exp. Bot., 2005. 56(419): p. 2465-76 [PMID:16061508] Somerville C Cellulose synthesis in higher plants. Annu. Rev. Cell Dev. Biol., 2006. 22: p. 53-78 [PMID:16824006] Roberts AW,Bushoven JT The cellulose synthase (CESA) gene superfamily of the moss Physcomitrella patens. Plant Mol. Biol., 2007. 63(2): p. 207-19 [PMID:17006591] Bosca S, et al. Interactions between MUR10/CesA7-dependent secondary cellulose biosynthesis and primary cell wall structure. Plant Physiol., 2006. 142(4): p. 1353-63 [PMID:17041031] Taylor NG Identification of cellulose synthase AtCesA7 (IRX3) in vivo phosphorylation sites--a potential role in regulating protein degradation. Plant Mol. Biol., 2007. 64(1-2): p. 161-71 [PMID:17427041] Srinivasasainagendra V,Page GP,Mehta T,Coulibaly I,Loraine AE CressExpress: a tool for large-scale mining of expression data from Arabidopsis. Plant Physiol., 2008. 147(3): p. 1004-16 [PMID:18467456] Mutwil M,Obro J,Willats WG,Persson S GeneCAT--novel webtools that combine BLAST and co-expression analyses. Nucleic Acids Res., 2008. 36(Web Server issue): p. W320-6 [PMID:18480120] Atanassov II,Pittman JK,Turner SR Elucidating the mechanisms of assembly and subunit interaction of the cellulose synthase complex of Arabidopsis secondary cell walls. J. Biol. Chem., 2009. 284(6): p. 3833-41 [PMID:19056734] Minic Z, et al. Transcriptomic analysis of Arabidopsis developing stems: a close-up on cell wall genes. BMC Plant Biol., 2009. 9: p. 6 [PMID:19149885] Timmers J, et al. Interactions between membrane-bound cellulose synthases involved in the synthesis of the secondary cell wall. FEBS Lett., 2009. 583(6): p. 978-82 [PMID:19258017] Betancur L, et al. Phylogenetically distinct cellulose synthase genes support secondary wall thickening in arabidopsis shoot trichomes and cotton fiber. J Integr Plant Biol, 2010. 52(2): p. 205-20 [PMID:20377682] 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] Carroll A, et al. Complexes with mixed primary and secondary cellulose synthases are functional in Arabidopsis plants. Plant Physiol., 2012. 160(2): p. 726-37 [PMID:22926318] Li S,Lei L,Gu Y Functional analysis of complexes with mixed primary and secondary cellulose synthases. Plant Signal Behav, 2013. 8(3): p. e23179 [PMID:23299322] Handakumbura PP, et al. Perturbation of Brachypodium distachyon CELLULOSE SYNTHASE A4 or 7 results in abnormal cell walls. BMC Plant Biol., 2013. 13: p. 131 [PMID:24024469] Hill JL,Hammudi MB,Tien M The Arabidopsis cellulose synthase complex: a proposed hexamer of CESA trimers in an equimolar stoichiometry. Plant Cell, 2014. 26(12): p. 4834-42 [PMID:25490917] Taylor-Teeples M, et al. An Arabidopsis gene regulatory network for secondary cell wall synthesis. Nature, 2015. 517(7536): p. 571-5 [PMID:25533953] Sun X, et al. A R2R3-MYB transcription factor that is specifically expressed in cotton (Gossypium hirsutum) fibers affects secondary cell wall biosynthesis and deposition in transgenic Arabidopsis. Physiol Plant, 2015. 154(3): p. 420-32 [PMID:25534543] Zhang Y, et al. Golgi-localized STELLO proteins regulate the assembly and trafficking of cellulose synthase complexes in Arabidopsis. Nat Commun, 2016. 7: p. 11656 [PMID:27277162] Kumar M, et al. S-Acylation of the cellulose synthase complex is essential for its plasma membrane localization. Science, 2016. 353(6295): p. 166-9 [PMID:27387950] Kumar M, et al. Exploiting CELLULOSE SYNTHASE (CESA) Class Specificity to Probe Cellulose Microfibril Biosynthesis. Plant Physiol., 2018. 177(1): p. 151-167 [PMID:29523715] Pear JR,Kawagoe Y,Schreckengost WE,Delmer DP,Stalker DM Higher plants contain homologs of the bacterial celA genes encoding the catalytic subunit of cellulose synthase. Proc. Natl. Acad. Sci. U.S.A., 1996. 93(22): p. 12637-42 [PMID:8901635]