SPT5_PYRFU
ID SPT5_PYRFU Reviewed; 152 AA.
AC Q8TZK1;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Transcription elongation factor Spt5 {ECO:0000255|HAMAP-Rule:MF_00950};
GN Name=spt5 {ECO:0000255|HAMAP-Rule:MF_00950}; OrderedLocusNames=PF1990;
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 (3.30 ANGSTROMS) IN COMPLEX WITH SPT4 AND RNAP,
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 [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH SPT4, FUNCTION,
RP 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_00950, ECO:0000269|PubMed:21187417,
CC ECO:0000269|PubMed:21386817}.
CC -!- SUBUNIT: Heterodimer composed of Spt4 and Spt5. Interacts with RNA
CC polymerase (RNAP) independently of nucleic acids. Forms a homodimer in
CC solution. {ECO:0000255|HAMAP-Rule:MF_00950,
CC ECO:0000269|PubMed:21187417, ECO:0000269|PubMed:21386817}.
CC -!- INTERACTION:
CC Q8TZK1; Q8U440: spt4; NbExp=3; IntAct=EBI-8606402, EBI-8606370;
CC -!- DOMAIN: Composed of only a NusG N-terminal (NGN) domain and a KOW
CC domain, similar to bacterial NusG. The NGN domain is the effector
CC domain of the complex that mediates the interaction with RNAP. The NGN
CC domain closes the RNAP active center cleft to lock nucleic acids and
CC render the elongation complex stable and processive. The KOW domain may
CC interact with RNA and/or other factors. {ECO:0000269|PubMed:21187417,
CC ECO:0000269|PubMed:21386817}.
CC -!- SIMILARITY: Belongs to the archaeal Spt5 family. {ECO:0000255|HAMAP-
CC Rule:MF_00950}.
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DR EMBL; AE009950; AAL82114.1; -; Genomic_DNA.
DR RefSeq; WP_011013134.1; NZ_CP023154.1.
DR PDB; 3P8B; X-ray; 1.80 A; B/D=1-152.
DR PDB; 3QQC; X-ray; 3.30 A; D=1-152.
DR PDBsum; 3P8B; -.
DR PDBsum; 3QQC; -.
DR AlphaFoldDB; Q8TZK1; -.
DR SMR; Q8TZK1; -.
DR DIP; DIP-59596N; -.
DR IntAct; Q8TZK1; 2.
DR MINT; Q8TZK1; -.
DR STRING; 186497.PF1990; -.
DR PRIDE; Q8TZK1; -.
DR EnsemblBacteria; AAL82114; AAL82114; PF1990.
DR GeneID; 41713813; -.
DR KEGG; pfu:PF1990; -.
DR PATRIC; fig|186497.12.peg.2066; -.
DR eggNOG; arCOG01920; Archaea.
DR HOGENOM; CLU_113589_0_0_2; -.
DR OMA; FSEIEHF; -.
DR OrthoDB; 91936at2157; -.
DR PhylomeDB; Q8TZK1; -.
DR EvolutionaryTrace; Q8TZK1; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.30.70.940; -; 1.
DR HAMAP; MF_00950; Spt5_arch; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR005825; Ribosomal_L24/26_CS.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR011590; Spt5_arc.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; PTHR11125; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR SMART; SM00739; KOW; 1.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR TIGRFAMs; TIGR00405; KOW_elon_Spt5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..152
FT /note="Transcription elongation factor Spt5"
FT /id="PRO_0000422136"
FT DOMAIN 94..124
FT /note="KOW"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00950"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3P8B"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:3P8B"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3P8B"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:3P8B"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:3P8B"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:3P8B"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3P8B"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3P8B"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:3P8B"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:3P8B"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:3P8B"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:3P8B"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:3P8B"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:3P8B"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:3P8B"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3P8B"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3P8B"
SQ SEQUENCE 152 AA; 16792 MW; B9321A520404A450 CRC64;
MAGKIFAVRV THGQEETTAK LIYSKVRTYN LPIYAILAPS RVKGYIFVEA PNKGVVDEAI
RGIRHARGVL PGEVPFKEIE HFLEEKPAVS GLEPGDLVEV IAGPFKGQKA KVVKIDESKD
EVVVQFIDAI VPIPVTIKGD YVRLISKLQK EE
