Reviewed, UniProtKB/Swiss-Prot P41900 (T2FB_DROME)

Names and origin

Protein names

Recommended name:
    General transcription factor IIF subunit 2
    EC=3.6.1.-
Alternative name(s):
    Transcription initiation factor IIF subunit beta
      Short name=TFIIF-beta
    ATP-dependent helicase TfIIF-beta

Gene names

Name:	TfIIFbeta
Synonyms:	TFIIF30
ORF Names:	CG6538

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	277 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation. This subunit shows ATP-dependent DNA-helicase activity By similarity.
Subunit structure	Heterodimer of an alpha and a beta subunit.
Subcellular location	Nucleus.
Sequence similarities	Belongs to the TFIIF beta subunit family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription initiation from RNA polymerase II promoter Inferred from electronic annotation. Source: InterPro
Cellular component	transcription factor TFIIF complex Non-traceable author statement. Source: FlyBase
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: UniProtKB-KW general RNA polymerase II transcription factor activity Non-traceable author statement. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 277	277	General transcription factor IIF subunit 2		PRO_0000211239
Regions
	Nucleotide binding	43 – 50	8	ATP By similarity
Experimental info
	Sequence conflict	97 – 117	21	VFSHM…SAAQP → YSRTWHRPMARRTRLPRRHS in AAA81888. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P41900-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: ED128DE2815D21CA	FASTA	277	32,107
	10 20 30 40 50 60 MSKEDKEKTQ IIDKDLDLSN AGRGVWLVKV PKYIAQKWEK APTNMDVGKL RINKTPGQKA 70 80 90 100 110 120 QVSLSLTPAV LALDPEEKIP TEHILDVSQV TKQTLGVFSH MAPSDGKENS TTSAAQPDNE 130 140 150 160 170 180 KLYMEGRIVQ KLECRPIADN CYMKLKLESI RKASEPQRRV QPIDKIVQNF KPVKDHAHNI 190 200 210 220 230 240 EYRERKKAEG KKARDDKNAV MDMLFHAFEK HQYYNIKDLV KITNQPISYL KEILKDVCDY 250 260 270 NMKNPHKNMW ELKKEYRHYK TEEKKEEEHK SGSSDSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of cDNA encoding the small subunit of Drosophila transcription initiation factor TFIIF." Gong D.-W., Mortin M.A., Horikoshi M., Nakatani Y. Nucleic Acids Res. 23:1882-1886(1995) [PubMed: 7596813] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and function of the small subunit of TFIIF (RAP30) from Drosophila melanogaster." Frank D.J., Tyree C.M., George C.P., Kadonaga J.T. J. Biol. Chem. 270:6292-6297(1995) [PubMed: 7890767] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: Canton-S.
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U25188 mRNA. Translation: AAA86888.1. U02461 mRNA. Translation: AAA81888.1. AE014297 Genomic DNA. Translation: AAF54548.1. AY071514 mRNA. Translation: AAL49136.1.
PIR	S57336.
RefSeq	NP_524305.2.
UniGene	Dm.20167
3D structure databases
HSSP	HSSP built from PDB template 2BBY based on UniProtKB P13984.
ModBase	Search...
Protein-protein interaction databases
IntAct	P41900. 1 interaction.
Genome annotation databases
Ensembl	FBgn0010421. Drosophila melanogaster. [Contig view]
GeneID	41290.
KEGG	dme:Dmel_CG6538.
NMPDR	fig|7227.3.peg.12111.
Organism-specific databases
FlyBase	FBgn0010421. TfIIFbeta.
Phylogenomic databases
HOGENOM	P41900.
OMA	P41900. IDNDRGV.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-010956-MON.
Gene expression databases
GermOnline	CG6538. Drosophila melanogaster.
Family and domain databases
InterPro	IPR016640. TFIIF-beta_sub. IPR003196. TFIIF_beta. IPR011991. Wing_hlx_DNA_bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PANTHER	PTHR10445. TFIIF_beta. 1 hit.
Pfam	PF02270. TFIIF_beta. 1 hit. [Graphical view]
PIRSF	PIRSF015849. TFIIF-beta. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	823133.

Entry information

Entry name

T2FB_DROME

Accession

Primary (citable) accession number: P41900
Secondary accession number(s): Q9VGX4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project