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

GSMUA_Achr2P12930_001

Organism

Musa acuminata

Taxonomic ID

4641

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; Liliopsida; Petrosaviidae; commelinids; Zingiberales; Musaceae; Musa

Family

NF-YA

Protein Properties

Length: 1307aa MW: 140517 Da PI: 7.3365

Description

NF-YA family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
GSMUA_Achr2P12930_001	genome	CIRAD	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	CBFB_NFYA	84	2.4e-26	106	161	2	58
CBFB_NFYA 2 eplYVNaKQyqrIlkRRqkRakleeekkldeksrkpylheSRhkhAlrRpRgsgGrF 58 p+YVNaKQ+++I++RR++Rak+e+e++l +k rkpy+h SRh hA rR+R +gGrF GSMUA_Achr2P12930_001 106 GPIYVNAKQFNAIIRRRKARAKAEKENNL-IKVRKPYMHVSRHLHAARRARDCGGRF 161 69*************************.************************9 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
SMART	SM00521	2.1E-30	103	164	IPR001289	Nuclear transcription factor Y subunit A
PROSITE profile	PS51152	31.682	104	164	IPR001289	Nuclear transcription factor Y subunit A
Pfam	PF02045	5.4E-24	107	161	IPR001289	Nuclear transcription factor Y subunit A
PROSITE pattern	PS00686	0	109	129	IPR018362	CCAAT-binding factor, conserved site
Gene3D	G3DSA:2.120.10.80	2.4E-40	329	617	IPR015915	Kelch-type beta propeller
SuperFamily	SSF117281	6.8E-38	334	617	No hit	No description
Pfam	PF13415	3.3E-5	429	476	No hit	No description
Pfam	PF07646	3.2E-5	521	567	IPR011498	Kelch repeat type 2
CDD	cd07419	0	956	1258	No hit	No description
SuperFamily	SSF56300	2.89E-94	961	1267	IPR029052	Metallo-dependent phosphatase-like
Gene3D	G3DSA:3.60.21.10	6.3E-110	964	1283	IPR029052	Metallo-dependent phosphatase-like
SMART	SM00156	1.7E-105	976	1260	IPR006186	Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
Pfam	PF00149	1.8E-32	1004	1211	IPR004843	Calcineurin-like phosphoesterase domain, apaH type
PRINTS	PR00114	2.1E-60	1004	1031	IPR006186	Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
PRINTS	PR00114	2.1E-60	1039	1066	IPR006186	Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
PRINTS	PR00114	2.1E-60	1072	1096	IPR006186	Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
PROSITE pattern	PS00125	0	1073	1078	IPR006186	Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
PRINTS	PR00114	2.1E-60	1110	1136	IPR006186	Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
PRINTS	PR00114	2.1E-60	1140	1167	IPR006186	Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
PRINTS	PR00114	2.1E-60	1200	1220	IPR006186	Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
PRINTS	PR00114	2.1E-60	1222	1238	IPR006186	Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0006355	Biological Process	regulation of transcription, DNA-templated
GO:0016602	Cellular Component	CCAAT-binding factor complex
GO:0003677	Molecular Function	DNA binding
GO:0003700	Molecular Function	transcription factor activity, sequence-specific DNA binding
GO:0005515	Molecular Function	protein binding
GO:0016787	Molecular Function	hydrolase activity

Sequence ? help Back to Top
Protein Sequence Length: 1307 aa Download sequence Send to blast
MNHLEDPSQG PRLGFGIPEK GGNNTAKFTI FPDSKELGGE PKTQQHFGHF SLQSLLPENS 60 GFKGVGQSVV CPSQSYVDQF YGLYATYGAQ AMHGRMLLPM DTTAEGPIYV NAKQFNAIIR 120 RRKARAKAEK ENNLIKVRKP YMHVSRHLHA ARRARDCGGR FFNTKKEVIA QAGNTGHKVN 180 DVVPRLPAAS PSSEVLQSDS LNLNSARAAA MEVDSTMSTE SGHDPAAGNH TGNPNEPSSS 240 PSAPGAVPPA EAQPVAAGPR PAPGYSVVNA VIERKEDGPG CRCGHTLTAV AAVGEEGTPG 300 YIGPRLILFG GATALEGNSA APASPTGSAG IRLAGATADV HCYDVLSNKW TRVTPLGEPP 360 SPRAAHVATA VGTMVVIQGG IGPAGLSAED LHVLDLTQQR PRWHRVVVQG PGPGARYGHV 420 MALVGQRFLL TIGGNDGKRP LADVWALDTA AKPYEWRKLE PEGEGPPPCM YATASARSDG 480 LLLLCGGRDA NGVPLSSAYG LAKHRDGRWE WAIAPGVSPS PRYQHAAVFV NARLHVSGGA 540 LGGGRMVEDS SSIAVLDTAA GVWCDTKSVV TSPRPGRYSV DAAGGDASVE LTRRCRHAAA 600 AVGDLIFIYG GLRGATYLLP SLRHVKSICL VTVKIFKYLF KVSIKNIMHF SYLNHSYICF 660 ILCNIFMFVV ASINSSLNRT RKEEMTMIKD GFTPIALFLN INVYELFIIL NRSISLLVDP 720 YGNTWSVLLD DLLVAEDLAA AETTNSASHA AAVAAASNVQ VGRSAGRYMF SDERSRQSSP 780 EAVPDGAVAL GTPVAPPVNG DMFADISTEN ALFQGSRRLS KGVEYLVEAS AAEAEAISAA 840 LAAAKARQVN GEVEQLPDQA HGSEATLGGK QVCNLSKASD SSLPNNGTPT GVRLHHRAVV 900 VAAETGGALG GMVRQLSIDQ FENEGRRVSY GTPESATAAR KLLDRQMSIN SVPKKVIAHL 960 LKPRGWKPPV RRQFFLDCNE IADLCDSAER IFTSEPSVLQ IKAPVKIFGD LHGQFGDLMR 1020 LFDEYGAPST AGDIAYIDYL FLGDYVDRGQ HSLETIALLL ALKVEHPHNV HLIRGNHEAA 1080 DINALFGFRT ECIERMGERD GIWTWHRINR LFNWLPLAAL IEKKIICMHG GIGRSINHVE 1140 QIENLQRPIT METGSVVLMD LLWSDPTEND SVEGLRPNAR GPGLVTFGPD RVMEFCNNND 1200 LQLIVRAHEC VMDGFERFAQ GHLITLFSAT NYCGTANNAG AILVLGRDLV VVPKLIHPIP 1260 PAVSSPEASP EHHIEDTWMQ ELNANRPPTP TRGRPQVASD RGSLAWI

Sequence ? help Back to Top

Protein Sequence Length: 1307 aa Download sequence Send to blast

MNHLEDPSQG PRLGFGIPEK GGNNTAKFTI FPDSKELGGE PKTQQHFGHF SLQSLLPENS  60
GFKGVGQSVV CPSQSYVDQF YGLYATYGAQ AMHGRMLLPM DTTAEGPIYV NAKQFNAIIR  120
RRKARAKAEK ENNLIKVRKP YMHVSRHLHA ARRARDCGGR FFNTKKEVIA QAGNTGHKVN  180
DVVPRLPAAS PSSEVLQSDS LNLNSARAAA MEVDSTMSTE SGHDPAAGNH TGNPNEPSSS  240
PSAPGAVPPA EAQPVAAGPR PAPGYSVVNA VIERKEDGPG CRCGHTLTAV AAVGEEGTPG  300
YIGPRLILFG GATALEGNSA APASPTGSAG IRLAGATADV HCYDVLSNKW TRVTPLGEPP  360
SPRAAHVATA VGTMVVIQGG IGPAGLSAED LHVLDLTQQR PRWHRVVVQG PGPGARYGHV  420
MALVGQRFLL TIGGNDGKRP LADVWALDTA AKPYEWRKLE PEGEGPPPCM YATASARSDG  480
LLLLCGGRDA NGVPLSSAYG LAKHRDGRWE WAIAPGVSPS PRYQHAAVFV NARLHVSGGA  540
LGGGRMVEDS SSIAVLDTAA GVWCDTKSVV TSPRPGRYSV DAAGGDASVE LTRRCRHAAA  600
AVGDLIFIYG GLRGATYLLP SLRHVKSICL VTVKIFKYLF KVSIKNIMHF SYLNHSYICF  660
ILCNIFMFVV ASINSSLNRT RKEEMTMIKD GFTPIALFLN INVYELFIIL NRSISLLVDP  720
YGNTWSVLLD DLLVAEDLAA AETTNSASHA AAVAAASNVQ VGRSAGRYMF SDERSRQSSP  780
EAVPDGAVAL GTPVAPPVNG DMFADISTEN ALFQGSRRLS KGVEYLVEAS AAEAEAISAA  840
LAAAKARQVN GEVEQLPDQA HGSEATLGGK QVCNLSKASD SSLPNNGTPT GVRLHHRAVV  900
VAAETGGALG GMVRQLSIDQ FENEGRRVSY GTPESATAAR KLLDRQMSIN SVPKKVIAHL  960
LKPRGWKPPV RRQFFLDCNE IADLCDSAER IFTSEPSVLQ IKAPVKIFGD LHGQFGDLMR  1020
LFDEYGAPST AGDIAYIDYL FLGDYVDRGQ HSLETIALLL ALKVEHPHNV HLIRGNHEAA  1080
DINALFGFRT ECIERMGERD GIWTWHRINR LFNWLPLAAL IEKKIICMHG GIGRSINHVE  1140
QIENLQRPIT METGSVVLMD LLWSDPTEND SVEGLRPNAR GPGLVTFGPD RVMEFCNNND  1200
LQLIVRAHEC VMDGFERFAQ GHLITLFSAT NYCGTANNAG AILVLGRDLV VVPKLIHPIP  1260
PAVSSPEASP EHHIEDTWMQ ELNANRPPTP TRGRPQVASD RGSLAWI

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
1it6_A	8e-78	956	1293	12	315	SERINE/THREONINE PROTEIN PHOSPHATASE 1 GAMMA (PP1-GAMMA) CATALYTIC SUBUNIT
1it6_B	8e-78	956	1293	12	315	SERINE/THREONINE PROTEIN PHOSPHATASE 1 GAMMA (PP1-GAMMA) CATALYTIC SUBUNIT
1jk7_A	8e-78	956	1293	12	315	SERINE/THREONINE PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT
2bcd_A	8e-78	956	1293	12	315	Serine/threonine protein phosphatase PP1-gamma catalytic subunit
2bdx_A	8e-78	956	1293	12	315	Serine/threonine protein phosphatase PP1-gamma catalytic subunit
2o8a_A	1e-77	956	1293	18	321	Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
2o8a_B	1e-77	956	1293	18	321	Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
2o8g_A	1e-77	956	1293	18	321	Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
2o8g_B	1e-77	956	1293	18	321	Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
4ut2_A	8e-78	956	1293	12	315	SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT
4ut2_B	8e-78	956	1293	12	315	SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT
4ut3_A	8e-78	956	1293	12	315	SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT
4ut3_B	8e-78	956	1293	12	315	SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT
4v0u_D	8e-78	956	1293	12	315	SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT
4v0u_F	8e-78	956	1293	12	315	SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT
4v0u_H	8e-78	956	1293	12	315	SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT
4v0u_J	8e-78	956	1293	12	315	SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT
4v0u_N	8e-78	956	1293	12	315	SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC SUBUNIT
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Functional Description ? help Back to Top
Source	Description
UniProt	Phosphatase involved in elongation process, probably by acting as a regulator of brassinolide signaling. {ECO:0000269\|PubMed:14977918}.

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_009388972.1	0.0	PREDICTED: serine/threonine-protein phosphatase BSL2 homolog
Swissprot	Q9SHS7	0.0	BSL3_ARATH; Serine/threonine-protein phosphatase BSL3
TrEMBL	M0S7I4	0.0	M0S7I4_MUSAM; Serine/threonine-protein phosphatase
STRING	GSMUA_Achr2P12930_001	0.0	(Musa acuminata)

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT5G06510.3	3e-23	nuclear factor Y, subunit A10

Publications ? help Back to Top
Kerk D, et al. The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis. Plant Physiol., 2002. 129(2): p. 908-25 [PMID:12068129] Farkas I,Dombrádi V,Miskei M,Szabados L,Koncz C Arabidopsis PPP family of serine/threonine phosphatases. Trends Plant Sci., 2007. 12(4): p. 169-76 [PMID:17368080] Kerk D,Templeton G,Moorhead GB Evolutionary radiation pattern of novel protein phosphatases revealed by analysis of protein data from the completely sequenced genomes of humans, green algae, and higher plants. Plant Physiol., 2008. 146(2): p. 351-67 [PMID:18156295] Maselli GA, et al. Revisiting the evolutionary history and roles of protein phosphatases with Kelch-like domains in plants. Plant Physiol., 2014. 164(3): p. 1527-41 [PMID:24492333]