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

Gh_A08G2528

Organism

Gossypium hirsutum

Taxonomic ID

3635

Taxonomic Lineage

cellular organisms; Eukaryota; Viridiplantae; Streptophyta; Streptophytina; Embryophyta; Tracheophyta; Euphyllophyta; Spermatophyta; Magnoliophyta; Mesangiospermae; eudicotyledons; Gunneridae; Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium

Family

SRS

Protein Properties

Length: 989aa MW: 105854 Da PI: 8.1448

Description

SRS family protein

Gene Model

Gene Model ID	Type	Source	Coding Sequence
Gh_A08G2528	genome	NAU-NBI	View CDS

Signature Domain? help Back to Top

No.	Domain	Score	E-value	Start	End	HMM Start	HMM End
1	DUF702	217.2	3.6e-67	212	372	3	153
DUF702 3 sgtasCqdCGnqakkdCaheRCRtCCksrgfdCathvkstWvpaakrrerqqqlaaasskaaasa.aeaaskrkrelkskkqsalsstklssaeskke 99 s +a+CqdCGnqakkdC+h+RCRtCCksrgfdC thvkstWvpaa+rrerq + aaa++ a s+ +++ +k++r +++++++s+t++s+++++++ Gh_A08G2528 212 SSGATCQDCGNQAKKDCTHRRCRTCCKSRGFDCPTHVKSTWVPAARRRERQLMSAAATTAGAGSSgSTSGAKKPRL-VTSQTTTTSHTSTSNTTPPRS 308 56789********************************************9999998887777746666777776.588999999******** PP DUF702 100 letss..........lPeevsseavfrcvrvssvddgeeelaYqtavsigGhvfkGiLydqGle 153 ++tss lP +v+++avf+cvrv++v+ ge+e+aYq++v+igGhvfkG+LydqG+e Gh_A08G2528 309 FDTSSshqdvgfketLPGQVRAPAVFKCVRVTAVEGGEDEYAYQAVVKIGGHVFKGFLYDQGVE 372 999*******************************************************98 PP

Protein Features ? help Back to Top

Database	Entry ID	E-value	Start	End	InterPro ID	Description
Pfam	PF05142	1.5E-61	214	372	IPR007818	Protein of unknown function DUF702
TIGRFAMs	TIGR01623	4.8E-27	216	258	IPR006510	Zinc finger, lateral root primordium type 1
TIGRFAMs	TIGR01624	3.9E-28	324	371	IPR006511	Lateral Root Primordium type 1, C-terminal
SuperFamily	SSF51338	7.95E-33	505	556	IPR011059	Metal-dependent hydrolase, composite domain
Gene3D	G3DSA:2.30.40.10	4.5E-31	505	571	IPR011059	Metal-dependent hydrolase, composite domain
TIGRFAMs	TIGR02033	2.4E-196	506	956	IPR011778	Hydantoinase/dihydropyrimidinase
CDD	cd01314	0	506	952	No hit	No description
Pfam	PF01979	1.3E-24	553	939	IPR006680	Amidohydrolase-related
SuperFamily	SSF51556	1.6E-96	557	885	IPR032466	Metal-dependent hydrolase
Gene3D	G3DSA:3.20.20.140	1.6E-113	572	878	No hit	No description
Gene3D	G3DSA:2.30.40.10	7.9E-11	879	960	IPR011059	Metal-dependent hydrolase, composite domain
SuperFamily	SSF51338	7.95E-33	885	956	IPR011059	Metal-dependent hydrolase, composite domain

Gene Ontology ? help Back to Top
GO Term	GO Category	GO Description
GO:0005737	Cellular Component	cytoplasm
GO:0016810	Molecular Function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds

Sequence ? help Back to Top
Protein Sequence Length: 989 aa Download sequence Send to blast
MFYGRNIYFC YFFVVAIVAT TRGQLPSDTG GAFADWATSS STAIRAGPDD LLSLGFNPNA 60 ASTAATAAAP AQWPPSARPI NYGLAGPEMG MVGLRDFVVV APAASFNHHH HHHHHHHTQD 120 PIMVNEQING PSSAAAAATA LGVGVIPLLT ASPCLPPQNV EDTGKFSGMQ LWQNQSSSHY 180 LKKPASLLDN NPSMMAGDGG GMGGGSGGSG SSSGATCQDC GNQAKKDCTH RRCRTCCKSR 240 GFDCPTHVKS TWVPAARRRE RQLMSAAATT AGAGSSGSTS GAKKPRLVTS QTTTTSHTST 300 SNTTPPRSFD TSSSHQDVGF KETLPGQVRA PAVFKCVRVT AVEGGEDEYA YQAVVKIGGH 360 VFKGFLYDQG VEGRDGFPNI SELHLGGGGR NAGSSSSPVL DPSDVYAATG GGFLGGGLGY 420 GFLQDVLQVT CENRDCRCGN RVWLLTIRYS VRCCKFIRIL SSYASLLTNA DQNKAAGMLL 480 RICEVGTGNG GSIGGTSPLP ASLSKLLIKG GTVVNAHRQE RADVYVEDGI IVAVKPNIKV 540 GDEVTVLDAT GRYVMPGGID PHTHLDAEFM GTVAVDDFFS GQAAALAGGT TMHIDFVHPV 600 NGSLMSGFEA YEKKASKSCM DYGFHMVIRH WDESVSKEME IMVKEKGIKS FKFFMAYKGT 660 FMVDDAVLLR GMKRCKSLGA LAMVHAENGD AVFEGQKRMI ERGITGPEGH ALSRPPMLEA 720 EATGRAIRLA SFVNTPLYVV HVMSIDAMEE IAKARKTGQK VIGEPVVSGL VLDDSKLWDP 780 DFITAAKYVM SPPIRESGHN KALQAALSTG VLQLVGTDHC TFNSSQKAFG IDDFRKIPNG 840 VNGIEERMHL VWDTMVESGQ ISVTDFVRIT STECARIFNI YPRKGAILVG SDADIIIFNP 900 NSSFEINPRS HHSRTNTNVY EGRKGKGKVE VTISRGRIVW KDDELKVAPG SGKYIPMPPF 960 GFLFDGIEKI DAKLVSSFKA PVHRFKSDV

Sequence ? help Back to Top

Protein Sequence Length: 989 aa Download sequence Send to blast

MFYGRNIYFC YFFVVAIVAT TRGQLPSDTG GAFADWATSS STAIRAGPDD LLSLGFNPNA  60
ASTAATAAAP AQWPPSARPI NYGLAGPEMG MVGLRDFVVV APAASFNHHH HHHHHHHTQD  120
PIMVNEQING PSSAAAAATA LGVGVIPLLT ASPCLPPQNV EDTGKFSGMQ LWQNQSSSHY  180
LKKPASLLDN NPSMMAGDGG GMGGGSGGSG SSSGATCQDC GNQAKKDCTH RRCRTCCKSR  240
GFDCPTHVKS TWVPAARRRE RQLMSAAATT AGAGSSGSTS GAKKPRLVTS QTTTTSHTST  300
SNTTPPRSFD TSSSHQDVGF KETLPGQVRA PAVFKCVRVT AVEGGEDEYA YQAVVKIGGH  360
VFKGFLYDQG VEGRDGFPNI SELHLGGGGR NAGSSSSPVL DPSDVYAATG GGFLGGGLGY  420
GFLQDVLQVT CENRDCRCGN RVWLLTIRYS VRCCKFIRIL SSYASLLTNA DQNKAAGMLL  480
RICEVGTGNG GSIGGTSPLP ASLSKLLIKG GTVVNAHRQE RADVYVEDGI IVAVKPNIKV  540
GDEVTVLDAT GRYVMPGGID PHTHLDAEFM GTVAVDDFFS GQAAALAGGT TMHIDFVHPV  600
NGSLMSGFEA YEKKASKSCM DYGFHMVIRH WDESVSKEME IMVKEKGIKS FKFFMAYKGT  660
FMVDDAVLLR GMKRCKSLGA LAMVHAENGD AVFEGQKRMI ERGITGPEGH ALSRPPMLEA  720
EATGRAIRLA SFVNTPLYVV HVMSIDAMEE IAKARKTGQK VIGEPVVSGL VLDDSKLWDP  780
DFITAAKYVM SPPIRESGHN KALQAALSTG VLQLVGTDHC TFNSSQKAFG IDDFRKIPNG  840
VNGIEERMHL VWDTMVESGQ ISVTDFVRIT STECARIFNI YPRKGAILVG SDADIIIFNP  900
NSSFEINPRS HHSRTNTNVY EGRKGKGKVE VTISRGRIVW KDDELKVAPG SGKYIPMPPF  960
GFLFDGIEKI DAKLVSSFKA PVHRFKSDV

3D Structure ? help Back to Top

PDB ID	Evalue	Query Start	Query End	Hit Start	Hit End	Description
2ftw_A	1e-166	506	971	10	478	dihydropyrimidine amidohydrolase
Search in ModeBase

Expression -- UniGene ? help Back to Top
UniGene ID	E-value	Expressed in
Ghi.20099	0.0	boll\| ovule

Expression -- Description ? help Back to Top
Source	Description
Uniprot	DEVELOPMENTAL STAGE: Up-regulated between days 3 and 12 after germination and during senescence. {ECO:0000269\|PubMed:19413687}.

Functional Description ? help Back to Top
Source	Description
UniProt	Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil to N-carbamoyl-alanine and of 5,6-dihydrothymine to N-carbamoyl-amino isobutyrate. Involved in the recycling of nitrogen from nucleobases to general nitrogen metabolism. {ECO:0000269\|PubMed:12626710, ECO:0000269\|PubMed:19413687}.

Regulation -- Description ? help Back to Top
Source	Description
UniProt	INDUCTION: Up-regulated by nitrogen limitation. {ECO:0000269\|PubMed:19413687}.

Annotation -- Nucleotide ? help Back to Top
Source	Hit ID	E-value	Description
GenBank	GQ393523	1e-137	GQ393523.1 Gossypium hirsutum cultivar Deltapine 33 B clone MONCS0488 SSR marker CGR5515 genomic sequence.

Annotation -- Protein ? help Back to Top
Source	Hit ID	E-value	Description
Refseq	XP_016727001.1	0.0	PREDICTED: dihydropyrimidinase-like isoform X1
Swissprot	Q9FMP3	0.0	DPYS_ARATH; Dihydropyrimidinase
TrEMBL	A0A2P5XLJ3	0.0	A0A2P5XLJ3_GOSBA; Uncharacterized protein
STRING	EOY32878	0.0	(Theobroma cacao)

Best hit in Arabidopsis thaliana ? help Back to Top
Hit ID	E-value	Description
AT5G12330.4	2e-82	Lateral root primordium (LRP) protein-related

Publications ? help Back to Top
Gojkovic Z, et al. Dihydropyrimidine amidohydrolases and dihydroorotases share the same origin and several enzymatic properties. Nucleic Acids Res., 2003. 31(6): p. 1683-92 [PMID:12626710] Zrenner R, et al. A functional analysis of the pyrimidine catabolic pathway in Arabidopsis. New Phytol., 2009. 183(1): p. 117-32 [PMID:19413687] Marchand CH, et al. Thioredoxin targets in Arabidopsis roots. Proteomics, 2010. 10(13): p. 2418-28 [PMID:20405473]