SPT5_ASHGO
ID SPT5_ASHGO Reviewed; 958 AA.
AC Q759T6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Transcription elongation factor SPT5;
DE AltName: Full=Chromatin elongation factor SPT5;
GN Name=SPT5; OrderedLocusNames=ADR187W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 635-650 AND 660.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS52107.2; -; Genomic_DNA.
DR RefSeq; NP_984283.2; NM_209636.2.
DR AlphaFoldDB; Q759T6; -.
DR SMR; Q759T6; -.
DR STRING; 33169.AAS52107; -.
DR EnsemblFungi; AAS52107; AAS52107; AGOS_ADR187W.
DR GeneID; 4620445; -.
DR KEGG; ago:AGOS_ADR187W; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_0_1; -.
DR InParanoid; Q759T6; -.
DR OMA; VGYMNTP; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0032044; C:DSIF complex; IBA:GO_Central.
DR GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
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: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:0060195; P:negative regulation of antisense RNA transcription; 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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; 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..958
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000238554"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..70
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..887
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 958 AA; 103695 MW; 113EC32DF7A18BE9 CRC64;
MSEREASEPI SEQGVSDNGD TFAAEGSQMK RRLSEVDGES RGAVDDALEG SNSDGDEDED
EDEDEDEDED GEGPHKKQRR ERNRFLDIEA EVSDDEEDDE DDEDSELVRE GFITHGDEDE
EEDDAQGSKD DRLHRQLDQD LQKSSEEDAQ KLAKELRERY GRSSSKQYRA AAQDGYVPQR
FMLPSVDTAT VWGVRCRPGK EKDLVKKLLK KKFNLDKSMG SKKLKILSIF QRDSFSGRIY
IEAPKQSVIE KFCNGVPDIY VNQKLLIPVQ ELPLLLKPSK SDDVRLEPGS YVRIKRGIYK
GDLAVVEQLS DNNLECMLKV VPRLDYGKND EVDPDTQQKK AKKVSFAQRP PPQLFNPTMA
LRMDQANLYK RDEKHFTYRN EDYIDGYLIK VFKIQYLKTA NIHPTVEELA RFGSKDGAVD
LTTISQTIKK AQASKAMFQP GDRVEILNGE QRGSKGYVTR TSTDIISVSL TGFNAKPLGF
PVSSLRKIFE PGDHVSVMSG DHQGDAGLVL IVKNGQVTFV SDQTRENLTI SANNLTKSMD
STPTSSDYAL HDIVELSAKN VACVIQAGHD IFKVLDDSGK VSTVTKGSIL KKINTTRSRI
AAVDGNGKEI KIGDTVVEKV GARREGQVLY VQSHQIFIVS KKIVENAGVF VVNPMNVEAV
ASRENLIASK LDLTKMNPEI AAKMGPPSQT AQPVSVGRDV ALNKTVRIRS AGYKGQLGIV
KDVNGDMATV ELHSKNKHIT VDKRKLTYFN HEGGDGITYD ELVSRRGRMP HARLGPSYVS
APRTMATGAP GAAPALSGGM TPGWSYFDGG KTPAVGSHGA GAASAWGGAS SWGGQGGGAT
STWGGQPGNV STWGGQTGAT STWGGASTWG NKSTWGGAST WASGGENGAA STWGGGDRSA
YGGASTWGAA GGASAWGGNK SHHRPDGSNS TWGTAPQGNR SAWGDQPAGS GSSWGGAR
