Reviewed, UniProtKB/Swiss-Prot P07273 (TFS2_YEAST)

Names and origin

Protein names

Recommended name:
    Transcription elongation factor S-II
Alternative name(s):
    DNA strand transfer protein alpha
      Short name=STP-alpha
    DNA strand transferase 1
    Pyrimidine pathway regulatory protein 2

Gene names

Name:	DST1
Synonyms:	PPR2
Ordered Locus Names:	YGL043W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus. Can promote the transfer of one strand of a double-stranded DNA molecule to a homologous single strand and thus may be involved in recombination.
Subcellular location	Nucleus.
Miscellaneous	S-II binds to RNA-polymerase II in the absence of transcription. Present with 6260 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the TFS-II family. Contains 1 TFIIS central domain. Contains 1 TFIIS N-terminal domain. Contains 1 TFIIS-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	RNA elongation from RNA polymerase II promoter Inferred from direct assay. Source: SGD regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: InterPro transcription initiation from RNA polymerase II promoter Inferred from direct assay. Source: SGD
Cellular component	nucleoplasm Inferred from physical interaction. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II transcription factor activity Inferred from electronic annotation. Source: InterPro positive transcription elongation factor activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct translation elongation factor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATG26	Q06321	1	EBI-19168,EBI-37737
RPB9	P27999	1	EBI-19168,EBI-15798

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 309

309

Transcription elongation factor S-II

PRO_0000121443

Regions

Domain

5 – 79

75

TFIIS N-terminal

Domain

148 – 264

117

TFIIS central

Zinc finger

267 – 307

41

TFIIS-type

Amino acid modifications

Modified residue

115

1

Phosphoserine Ref.9

Modified residue

116

1

Phosphoserine Ref.9

Modified residue

118

1

Phosphoserine Ref.9

Experimental info

Sequence conflict

35

1

V → F in AAA88734. Ref.1

Sequence conflict

35

1

V → F in AAA34580. Ref.1

Sequence conflict

74 – 77

4

DAIN → AQLI in AAA88734. Ref.1

Sequence conflict

74 – 77

4

DAIN → AQLI in AAA34580. Ref.1

Sequence conflict

82

1

S → C in AAA88734. Ref.1

Sequence conflict

82

1

S → C in AAA34580. Ref.1

Sequence conflict

85

1

A → P in AAA88734. Ref.1

Sequence conflict

85

1

A → P in AAA34580. Ref.1

Secondary structure

1

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309

Helix Strand Turn

Details...

Helix

3 – 16

14

Helix

21 – 30

10

Turn

31 – 33

3

Turn

38 – 39

2

Helix

40 – 52

13

Turn

59 – 60

2

Helix

61 – 76

16

Turn

134 – 137

4

Turn

145 – 148

4

Helix

149 – 163

15

Helix

171 – 178

8

Turn

179 – 183

5

Turn

187 – 191

5

Helix

192 – 206

15

Turn

207 – 208

2

Turn

214 – 216

3

Helix

217 – 220

4

Helix

228 – 231

4

Turn

232 – 236

5

Sequences

	Sequence		Length	Mass (Da)
	P07273-1 [UniParc]. Last modified October 1, 1996. Version 4. Checksum: D133938319C015FF	FASTA	309	34,843
	10 20 30 40 50 60 MDSKEVLVHV KNLEKNKSND AAVLEILHVL DKEFVPTEKL LRETKVGVEV NKFKKSTNVE 70 80 90 100 110 120 ISKLVKKMIS SWKDAINKNK RSRQAQQHHQ DHAPGNAEDK TTVGESVNGV QQPASSQSDA 130 140 150 160 170 180 MKQDKYVSTK PRNSKNDGVD TAIYHHKLRD QVLKALYDVL AKESEHPPQS ILHTAKAIES 190 200 210 220 230 240 EMNKVNNCDT NEAAYKARYR IIYSNVISKN NPDLKHKIAN GDITPEFLAT CDAKDLAPAP 250 260 270 280 290 300 LKQKIEEIAK QNLYNAQGAT IERSVTDRFT CGKCKEKKVS YYQLQTRSAD EPLTTFCTCE ACGNRWKFS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation, DNA sequence, and regulation of a Saccharomyces cerevisiae gene that encodes DNA strand transfer protein alpha." Clark A.B., Dykstra C.C., Sugino A. Mol. Cell. Biol. 11:2576-2582(1991) [PubMed: 1850099] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-30.
[2]	"Purification, gene cloning, and gene disruption of the transcription elongation factor S-II in Saccharomyces cerevisiae." Nakanishi T., Nakano A., Sekimizu K., Natori S. J. Biol. Chem. 267:13200-13204(1992) [PubMed: 1618824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes." Feuermann M., de Montigny J., Potier S., Souciet J.-L. Yeast 13:861-869(1997) [PubMed: 9234674] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Complete sequence of a eukaryotic regulatory gene." Hubert J.-C., Guyonvarch A., Kammerer B., Exinger F., Liljelund P., Lacroute F. EMBO J. 2:2071-2073(1983) [PubMed: 6139279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 182-309.
[6]	"Homologue of TFIIS in yeast." Davies C.J., Trgovchich J., Hutchison C.A. III Nature 345:298-298(1990) [PubMed: 1971423] [Abstract] Cited for: SIMILARITY TO S-II.
[7]	"TFIIS and strand-transfer proteins." Kipling D., Kearsey S.E. Nature 353:509-509(1991) [PubMed: 1922360] [Abstract] Cited for: IDENTITY OF PPR2 AND DST1.
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-116 AND SER-118, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M36724 Genomic DNA. Translation: AAA88734.1.
D12478 Genomic DNA. Translation: BAA02046.1.
M60770 Genomic DNA. Translation: AAA34580.1.
Z72565 Genomic DNA. Translation: CAA96744.1.
X00047 Genomic DNA. Translation: CAA24928.1.

PIR

A42921.

RefSeq

NP_011472.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ENW	NMR	-	A	131-240	[»]
1EO0	NMR	-	A	1-77	[»]
1PQV	X-ray	3.80	S	1-309	[»]
1Y1V	X-ray	3.80	S	131-309	[»]
1Y1Y	X-ray	4.00	S	131-309	[»]
3GTM	X-ray	3.80	S	145-309	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2307N.

IntAct

P07273. 2 interactions.

STRING

P07273.

Proteomic databases

PeptideAtlas

P07273.

Genome annotation databases

Ensembl

YGL043W; YGL043W; YGL043W; Saccharomyces cerevisiae. [Genome view]

GeneID

852839.

KEGG

sce:YGL043W.

NMPDR

fig|4932.3.peg.2577.

Organism-specific databases

CYGD

YGL043w.

SGD

S000003011. DST1.

Phylogenomic databases

HOGENOM

HBG716813.

OrthoDB

EOG9D80PG.

Gene expression databases

ArrayExpress

P07273.

Genevestigator

P07273.

GermOnline

YGL043W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR016492. TF_IIS.
IPR003617. TFIIS/CRSP70_N_sub.
IPR010990. TFIIS/elonginA/CRSP70_N.
IPR003618. TFIIS_centre.
IPR017923. TFIIS_N.
IPR014754. TFIIS_N_fun-typ.
IPR017890. TFS2M.
IPR006289. TFSII.
IPR001222. Znf_TFIIS.
[Graphical view]

Gene3D

G3DSA:1.10.472.30. TFIIS_centre. 1 hit.
G3DSA:1.20.930.10. TFIIS_N_fun-typ. 1 hit.

Pfam

PF08711. TFIIS. 1 hit.
PF01096. TFIIS_C. 1 hit.
PF07500. TFIIS_M. 1 hit.
[Graphical view]

PIRSF

PIRSF006704. TF_IIS. 1 hit.

SMART

SM00510. TFS2M. 1 hit.
SM00509. TFS2N. 1 hit.
SM00440. ZnF_C2C2. 1 hit.
[Graphical view]

PROSITE

PS51321. TFIIS_CENTRAL. 1 hit.
PS51319. TFIIS_N. 1 hit.
PS00466. ZF_TFIIS_1. 1 hit.
PS51133. ZF_TFIIS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

972417.

Entry information

Entry name

TFS2_YEAST

Accession

Primary (citable) accession number: P07273
Secondary accession number(s): P24535

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	October 1, 1996
Last modified:	December 15, 2009
This is version 110 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)