SPT5_DEBHA
ID SPT5_DEBHA Reviewed; 967 AA.
AC Q6BZG0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Transcription elongation factor SPT5;
DE AltName: Full=Chromatin elongation factor SPT5;
GN Name=SPT5; OrderedLocusNames=DEHA2A01628g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382133; CAG84361.2; -; Genomic_DNA.
DR RefSeq; XP_456409.2; XM_456409.1.
DR AlphaFoldDB; Q6BZG0; -.
DR SMR; Q6BZG0; -.
DR STRING; 4959.XP_456409.2; -.
DR EnsemblFungi; CAG84361; CAG84361; DEHA2A01628g.
DR GeneID; 2899625; -.
DR KEGG; dha:DEHA2A01628g; -.
DR VEuPathDB; FungiDB:DEHA2A01628g; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_0_1; -.
DR InParanoid; Q6BZG0; -.
DR OMA; VGYMNTP; -.
DR OrthoDB; 828863at2759; -.
DR Proteomes; UP000000599; Chromosome A.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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 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; IPR022581; Spt5_N.
DR InterPro; IPR017071; TF_Spt5_eukaryote.
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 Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 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..967
FT /note="Transcription elongation factor SPT5"
FT /id="PRO_0000238560"
FT DOMAIN 552..585
FT /note="KOW"
FT REGION 1..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..121
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 914..958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 967 AA; 106327 MW; 4723BEDA621DD67E CRC64;
MSEEENRITT SSDDVIKHEH PDNSTAGGAY EVQDRDQNDI DEEEEEKEEN KRSAEEEYSI
GSKRSLEDSE EGESKVPTEN DQALINNSGE GAEQQDNGDE ANDDENDDEN DEDEDEDEDE
EEVSSNKRKR RRGANQFIDI EAEVDDEEED EMDEDDEEAE LLREQFIADD SRVETMDGKD
SAGEHQDDRL HRQFDRRRQE AEDQDAEVLA ETLKQRYRKT HTVYRGDTTA SGTVSQKLLM
PSINDPAIYA IRCTPGREKD LVRKLYEKKR TLARSNPLEI LTVFQRDSFK GYIYIEAKKP
EAIERALTGM VNIYAKQRLL VPVREYPDLL KQVKSSDVEI VPGIYVRITR GKYKNDLAIV
DNLSENGLDV RCKLVPRLDY GKNDDFDKDG KRIRSKTKPI PRLFSEQEAR MYDGEYLQSG
RGPRAFIYRG EEYNEGFLFK DFKLQFIQTK DVHPKLEELD RFQTGDPEED GLDLAAIAAS
LKNKNNSEGA GRSSAFQPGD KVEIRRGEQA KTIGKVLSTS LNEITILVTD SGDPKFVNQR
LTVPANDLRK LFSAGDHVRV IEGKHSDETG LVIKIDNDSV ILLSDQTKQD VRVFANYLIK
ATDASSNTDV TGGKYDLNDL VQLNVSTVGV IVKAEKSSFE VLTSEGRLMS VNPAGIASKL
ELSRREQIAT DRNGSTVKIG DTVKEVLGDK KREGAILHIY KNSLFIKSNE ILENLGVFVT
NCMNVSTITT KDSIVSKSLG PDLNRMNPNL KLPNPIANAG LKTRVGGRDK LIYKDVLVNS
GNYKGLMGKV TEADEVYARI ELHTKSKKIK VTKNSLSVLV RGEAIPYLRF IGASSGPGNS
NPSGNFGGAS FNQPAKTPAF SSGGKSSWGS GGATPSVGGG ATAWGSGGAQ SSWGGGKTPA
YNSGNASTWG GNAGGASAWG NNNGNASTWG SNSKNGGSST WGGNSTWGNS NKGGKSSWGN
GSAWGGK
