ID   SPT5_CANGA              Reviewed;        1010 AA.
AC   Q6FRZ5;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Transcription elongation factor SPT5;
DE   AltName: Full=Chromatin elongation factor SPT5;
GN   Name=SPT5; OrderedLocusNames=CAGL0H04697g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380954; CAG59932.1; -; Genomic_DNA.
DR   RefSeq; XP_446999.1; XM_446999.1.
DR   AlphaFoldDB; Q6FRZ5; -.
DR   SMR; Q6FRZ5; -.
DR   STRING; 5478.XP_446999.1; -.
DR   PRIDE; Q6FRZ5; -.
DR   EnsemblFungi; CAG59932; CAG59932; CAGL0H04697g.
DR   GeneID; 2888499; -.
DR   KEGG; cgr:CAGL0H04697g; -.
DR   CGD; CAL0131556; CAGL0H04697g.
DR   VEuPathDB; FungiDB:CAGL0H04697g; -.
DR   eggNOG; KOG1999; Eukaryota.
DR   HOGENOM; CLU_003537_1_0_1; -.
DR   InParanoid; Q6FRZ5; -.
DR   OMA; VGYMNTP; -.
DR   Proteomes; UP000002428; Chromosome H.
DR   GO; GO:0032044; C:DSIF complex; IEA:EnsemblFungi.
DR   GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
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: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:0090262; P:regulation of transcription-coupled nucleotide-excision repair; IEA:EnsemblFungi.
DR   GO; GO:0000245; P:spliceosomal complex assembly; IEA:EnsemblFungi.
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; 4.
DR   SMART; SM00738; NGN; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
PE   3: Inferred from homology;
KW   mRNA processing; Nucleus; Reference proteome; Repeat; Transcription.
FT   CHAIN           1..1010
FT                   /note="Transcription elongation factor SPT5"
FT                   /id="PRO_0000238558"
FT   DOMAIN          333..360
FT                   /note="KOW 1"
FT   DOMAIN          536..563
FT                   /note="KOW 2"
FT   DOMAIN          750..777
FT                   /note="KOW 3"
FT   REGION          1..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..118
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..136
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..154
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        895..944
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        956..1010
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1010 AA;  109825 MW;  57BC37D4F86367E7 CRC64;
     MSDGSVEPVK ADDAVVDSSK RTHEEMSAEN TEPVSEQAHG TGSENGDGEN SLENSLEKDN
     AEKDNAESEK GSPSVTETAA DDDSSKTDGN GEENQDAEGL AEDYDEEDFD EDEDDEDEEP
     AAKRRQQERN RFLDIEAEVS EDEEDEEDEE DSELVREGFI THGEDEDDEE GVAGNRRGDR
     LHRQLDQDLN KSSEEDAQRL AKELRERYGR SSSKQYRAAA QDGYVPQRFL LPSVDTATIW
     GVRCRPGKEK ELVRKLLKKK FNLDRAMGKR KLKILSIFQR DNYTGRIYIE APKQSVIEKF
     CNGVPDIYIS QKLLIPVQEL PLLLKPSKSD DVALEEGSYV RVKRGIYKGD LAMVDQISEN
     NLEVMLKIVP RLDYGKFDEI DPVTQQRKSR RPTFAHRPAP QLFNPTMALR LDQANLYKRD
     DRHFTYKNED YIDGYLYKSF RIQHVETKNI QPTVEELARF GSKEGAVDLT AISQSIKKAQ
     AAKVSFQPGD RVEILNGEQR GSRGIVAKST TTIATVNLPE FPLKPLEFPV SALRKIFEPG
     DHVMVINGEH QGDAGLVLTI KQGQVTFMSN QTREEVTITA NNLSKSIDST PTSSEYSLHD
     IVELSAKNVA CIIQAGHDIF KVIDETGKVS TITKGSILSK INTSRSRLTT VDSSGNEIKI
     GDSIVEKIGA RREGQVLYIQ SQQIFVVSKK IVENAGVFVV NPVNVEAIAS KDNMLNNKLD
     LSKMNPDIIS KMGPPKSSMP SAAPVRTGRE VALGKTVRVR SAGYKGQLGI VKDVNGDKAT
     VELHSKNKHI TIDKRKLTYY NREGGEGITY DELVNRRGRL PQARMGPSYV SAPRHMASGA
     SGVVADNNGA LAGGMTPGWG AFDGGKTPAV NSHGAGTSGA TSAWGGASTW GGQGAGGSST
     WGGQGGATST WGGQGATSTW GGASAWGNKS SWGGASTWAA SGEANGGVST WGGGDRSTYG
     GASTWGNNAT GGTSTWGGNN QEQNNGGNRS AWKDQGNKSN YGGGSSWGNQ