SPT4_PYRFU
ID SPT4_PYRFU Reviewed; 61 AA.
AC Q8U440;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transcription elongation factor Spt4 {ECO:0000255|HAMAP-Rule:MF_00949};
GN Name=spt4 {ECO:0000255|HAMAP-Rule:MF_00949}; OrderedLocusNames=PF0255;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 2-61.
RX PubMed=15858261; DOI=10.1107/s0907444905003239;
RA Liu Z.J., Lin D., Tempel W., Praissman J.L., Rose J.P., Wang B.C.;
RT "Parameter-space screening: a powerful tool for high-throughput crystal
RT structure determination.";
RL Acta Crystallogr. D 61:520-527(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) IN COMPLEX WITH SPT5; RNAP AND ZINC,
RP FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=21386817; DOI=10.1038/emboj.2011.64;
RA Martinez-Rucobo F.W., Sainsbury S., Cheung A.C., Cramer P.;
RT "Architecture of the RNA polymerase-Spt4/5 complex and basis of universal
RT transcription processivity.";
RL EMBO J. 30:1302-1310(2011).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH SPT5 AND ZINC,
RP FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=21187417; DOI=10.1073/pnas.1013828108;
RA Klein B.J., Bose D., Baker K.J., Yusoff Z.M., Zhang X., Murakami K.S.;
RT "RNA polymerase and transcription elongation factor Spt4/5 complex
RT structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:546-550(2011).
CC -!- FUNCTION: Stimulates transcription elongation. {ECO:0000255|HAMAP-
CC Rule:MF_00949, ECO:0000269|PubMed:21187417,
CC ECO:0000269|PubMed:21386817}.
CC -!- SUBUNIT: Heterodimer composed of Spt4 and Spt5. {ECO:0000255|HAMAP-
CC Rule:MF_00949, ECO:0000269|PubMed:21187417,
CC ECO:0000269|PubMed:21386817}.
CC -!- INTERACTION:
CC Q8U440; Q8TZK1: spt5; NbExp=3; IntAct=EBI-8606370, EBI-8606402;
CC -!- DOMAIN: Contains a N-terminal zinc-binding domain and a C-terminal NGN-
CC binding domain. {ECO:0000269|PubMed:21187417,
CC ECO:0000269|PubMed:21386817}.
CC -!- SIMILARITY: Belongs to the archaeal Spt4 family. {ECO:0000255|HAMAP-
CC Rule:MF_00949}.
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DR EMBL; AE009950; AAL80379.1; -; Genomic_DNA.
DR RefSeq; WP_011011370.1; NZ_CP023154.1.
DR PDB; 1RYQ; X-ray; 1.38 A; A=2-61.
DR PDB; 3P8B; X-ray; 1.80 A; A/C=1-61.
DR PDB; 3QQC; X-ray; 3.30 A; E=1-61.
DR PDBsum; 1RYQ; -.
DR PDBsum; 3P8B; -.
DR PDBsum; 3QQC; -.
DR AlphaFoldDB; Q8U440; -.
DR SMR; Q8U440; -.
DR DIP; DIP-59595N; -.
DR IntAct; Q8U440; 2.
DR MINT; Q8U440; -.
DR STRING; 186497.PF0255; -.
DR PRIDE; Q8U440; -.
DR EnsemblBacteria; AAL80379; AAL80379; PF0255.
DR GeneID; 41712045; -.
DR KEGG; pfu:PF0255; -.
DR PATRIC; fig|186497.12.peg.267; -.
DR eggNOG; arCOG04077; Archaea.
DR HOGENOM; CLU_199467_0_0_2; -.
DR OMA; VCRECHR; -.
DR OrthoDB; 119723at2157; -.
DR PhylomeDB; Q8U440; -.
DR EvolutionaryTrace; Q8U440; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 2.20.28.90; -; 1.
DR HAMAP; MF_00949; Spt4_arch; 1.
DR InterPro; IPR029040; RPABC4/Spt4.
DR InterPro; IPR022800; Spt4/RpoE2_Znf.
DR InterPro; IPR007178; Spt4_arch.
DR InterPro; IPR038589; Spt4_dom_sf.
DR PANTHER; PTHR40704; PTHR40704; 1.
DR Pfam; PF06093; Spt4; 1.
DR SMART; SM01389; Spt4; 1.
DR SUPFAM; SSF63393; SSF63393; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..61
FT /note="Transcription elongation factor Spt4"
FT /id="PRO_0000422131"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00949,
FT ECO:0000269|PubMed:21187417, ECO:0000269|PubMed:21386817"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00949,
FT ECO:0000269|PubMed:21187417, ECO:0000269|PubMed:21386817"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00949,
FT ECO:0000269|PubMed:21187417, ECO:0000269|PubMed:21386817"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00949,
FT ECO:0000269|PubMed:21187417, ECO:0000269|PubMed:21386817"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:1RYQ"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:1RYQ"
FT STRAND 11..17
FT /evidence="ECO:0007829|PDB:1RYQ"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1RYQ"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1RYQ"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1RYQ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1RYQ"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:1RYQ"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:1RYQ"
SQ SEQUENCE 61 AA; 6953 MW; CA46E8DBF597B8ED CRC64;
MSEKACRHCH YITSEDRCPV CGSRDLSEEW FDLVIIVDVE NSEIAKKIGA KVPGKYAIRV
R
