SPT5_KLULA
ID SPT5_KLULA Reviewed; 1036 AA.
AC Q6CWW9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Transcription elongation factor SPT5;
DE AltName: Full=Chromatin elongation factor SPT5;
GN Name=SPT5; OrderedLocusNames=KLLA0B00891g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: The SPT4-SPT5 complex mediates both activation and inhibition
CC of transcription elongation, and plays a role in pre-mRNA processing.
CC This complex seems to be important for the stability of the RNA
CC polymerase II elongation machinery on the chromatin template but not
CC for the inherent ability of this machinery to translocate down the gene
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the SPT4-SPT5 complex. Interacts with RNA
CC polymerase II (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000305}.
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DR EMBL; CR382122; CAH01963.1; -; Genomic_DNA.
DR RefSeq; XP_451570.1; XM_451570.1.
DR AlphaFoldDB; Q6CWW9; -.
DR SMR; Q6CWW9; -.
DR STRING; 28985.XP_451570.1; -.
DR PRIDE; Q6CWW9; -.
DR EnsemblFungi; CAH01963; CAH01963; KLLA0_B00891g.
DR GeneID; 2897291; -.
DR KEGG; kla:KLLA0_B00891g; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_0_1; -.
DR InParanoid; Q6CWW9; -.
DR OMA; VGYMNTP; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0032044; C:DSIF complex; IEA:EnsemblFungi.
DR GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
DR GO; GO:0001042; F:RNA polymerase I core binding; IEA:EnsemblFungi.
DR GO; GO:0001179; F:RNA polymerase I general transcription initiation factor binding; IEA:EnsemblFungi.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IEA:EnsemblFungi.
DR GO; GO:0019843; F:rRNA binding; IEA:EnsemblFungi.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:EnsemblFungi.
DR GO; GO:0070990; F:snRNP binding; IEA:EnsemblFungi.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0030619; F:U1 snRNA binding; IEA:EnsemblFungi.
DR GO; GO:0030620; F:U2 snRNA binding; IEA:EnsemblFungi.
DR GO; GO:0030621; F:U4 snRNA binding; IEA:EnsemblFungi.
DR GO; GO:0030623; F:U5 snRNA binding; IEA:EnsemblFungi.
DR GO; GO:0017070; F:U6 snRNA binding; IEA:EnsemblFungi.
DR GO; GO:0008298; P:intracellular mRNA localization; IEA:EnsemblFungi.
DR GO; GO:2001208; P:negative regulation of transcription elongation by RNA polymerase I; IEA:EnsemblFungi.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:EnsemblFungi.
DR GO; GO:2001209; P:positive regulation of transcription elongation from RNA polymerase I promoter; IEA:EnsemblFungi.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:2000232; P:regulation of rRNA processing; IEA:EnsemblFungi.
DR GO; GO:0090262; P:regulation of transcription-coupled nucleotide-excision repair; IEA:EnsemblFungi.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:EnsemblFungi.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd06081; KOW_Spt5_1; 1.
DR CDD; cd06082; KOW_Spt5_2; 1.
DR CDD; cd06083; KOW_Spt5_3; 1.
DR CDD; cd06084; KOW_Spt5_4; 1.
DR CDD; cd06085; KOW_Spt5_5; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 3.
DR Gene3D; 3.30.70.940; -; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR041973; KOW_Spt5_1.
DR InterPro; IPR041975; KOW_Spt5_2.
DR InterPro; IPR041976; KOW_Spt5_3.
DR InterPro; IPR041977; KOW_Spt5_4.
DR InterPro; IPR041978; KOW_Spt5_5.
DR InterPro; IPR005100; NGN-domain.
DR InterPro; IPR006645; NGN_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR005825; Ribosomal_L24/26_CS.
DR InterPro; IPR039659; SPT5.
DR InterPro; IPR024945; Spt5_C_dom.
DR InterPro; IPR022581; Spt5_N.
DR InterPro; IPR017071; TF_Spt5_eukaryote.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11125; PTHR11125; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 1.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 5.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
PE 3: Inferred from homology;
KW mRNA processing; Nucleus; Reference proteome; Transcription.
FT CHAIN 1..1036
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000238563"
FT REGION 1..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..162
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1036 AA; 112772 MW; EDB1E98B1EB1E0CB CRC64;
MSGTAEESDK AEAVSVPETV SGSVESQDKE HNSTSSSSDS TDVVGGKKRT IDEVDGSSEN
NSASVDQLKD APTDSKPKTE ATEDSPIRGN QGNNQENSQE NKDDEDDEDD NDDDDNDDDD
DEDEDVESYR KKQRRERNRF LDIEAEVSED EDDEEDEEDS ELVREGFITR GDEEDEEDRG
GRVDDRLHRE LDQNLQKTAD EDMHKIAEDF KKRYGRDSSK DYRVQTQGGY VPQRFMLPSV
DTAIIWSVRC RPGKEKELVR KLLNKKFNLD KSMGSKKLKI LSIFQRDNYT GRIYIEAPKQ
SVIEKFVNGV PDVYSNQKLL IPVQELPLLL KPTKSDEVRL DVGSYVRIKR GIYKNDLAVI
DQISQNNLEA LLKIVPRLDY GKNDEIDPDT NQRKAKRATF ASRPPPQLFN PTMALRLDQA
NLFKRDDRHF TYRKEDYVDG YLFKSFKIQY LDTKNIQPTV EELSRFGSKE GDVDLAAIAQ
TMKKAQASKA MFQPGDRVEV LTGEQRGSRG VVTRSSKDVI SVKLSGFSDK SLEFPIASLR
KIFELGDHVT VIAGEHEGNA GLVLLVQNGQ VTFVSDQTRE NLTISANNLS KSMDSTPTSS
EYALHDIVEL SAKNVACVIQ AGHDIFKIID DSGKVATVTK GSILAKINVA RAKVAAVDGN
GREIKIGDVV REKIGSRREG QVLYVQNQHI FIRSKTITEN AGVFVVNPMN VEAVASKENL
MSSALDLSKI NPNIASKMGP PQTTQQTRLV GRDVALNKTV RIRSAGYKGQ LGIVKDVNGD
KATIELHSKN KHITIDKRKL TYFSHEGGEG ITYDELVSRR GRTPHTRLGP SYVSAPRHMA
AGGAVATNTP QQLPGGMTPG WNAFDGGKTP AVGQNGGTSS WGGASTWGGQ GPGGASAWGG
AAGNTSTWGG QGATSTWGGA STWGNKSSYG GASSWAASGE SGAASAWGGG NKSSYGGTST
WGGNQGGVSA WGGSGNKSQR SKNTGGSSTW GNNQSQHNSG ERSAWGNASQ HNNSGNRSAW
GNQDARGGGS TWGGNN
