ID S9X139_SCHCR Unreviewed; 963 AA.
AC S9X139;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=SPOG_00660 {ECO:0000313|EMBL:EPY50802.1};
OS Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS NBRC 106824 / NRRL Y48691) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY50802.1, ECO:0000313|Proteomes:UP000015464};
RN [1] {ECO:0000313|EMBL:EPY50802.1, ECO:0000313|Proteomes:UP000015464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC {ECO:0000313|Proteomes:UP000015464};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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
CC gene. {ECO:0000256|ARBA:ARBA00024691, ECO:0000256|PIRNR:PIRNR036945}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR036945}.
CC -!- SIMILARITY: Belongs to the SPT5 family. {ECO:0000256|ARBA:ARBA00006956,
CC ECO:0000256|PIRNR:PIRNR036945}.
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DR EMBL; KE546992; EPY50802.1; -; Genomic_DNA.
DR RefSeq; XP_013024289.1; XM_013168835.1.
DR AlphaFoldDB; S9X139; -.
DR STRING; 653667.S9X139; -.
DR EnsemblFungi; EPY50802; EPY50802; SPOG_00660.
DR GeneID; 25034992; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_1_1; -.
DR OMA; PYPVGYM; -.
DR OrthoDB; 24955at2759; -.
DR Proteomes; UP000015464; Unassembled WGS sequence.
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:0003711; F:transcription elongation factor activity; IEA:EnsemblFungi.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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 by RNA polymerase I; IEA:EnsemblFungi.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; 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:0140673; P:transcription elongation-coupled chromatin remodeling; 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; NusG, N-terminal domain; 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-like_dom.
DR InterPro; IPR036735; NGN_dom_sf.
DR InterPro; IPR039385; NGN_Euk.
DR InterPro; IPR014722; Rib_uL2_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; SUPPRESSOR OF TY 5; 1.
DR PANTHER; PTHR11125:SF7; TRANSCRIPTION ELONGATION FACTOR SPT5; 1.
DR Pfam; PF12815; CTD; 1.
DR Pfam; PF00467; KOW; 2.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 2.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 5.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:EPY50802.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Protein biosynthesis {ECO:0000313|EMBL:EPY50802.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 219..308
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 313..340
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 451..478
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 500..527
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 619..644
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 707..734
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 831..963
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT REGION 1..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 911..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..146
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..935
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 106051 MW; B42CAAB3BB4C3F43 CRC64;
MDGNVGNADL GEERYPPGGT VHEESTEQTS PNASRRNDDT NDSLVDSKEQ ENVSDDEDEQ
GQKEDAVQGD RNGEKNEEEN DAVDEEAEED EEEEDEEELE EEEEEEEEAG GGRRKRARHE
RRNQFLDIEA EVDEDEEELD DEEDEIGRED GFIEEEVGGA DYVSDDRRHR ELDRQRQELQ
SVDAERLAEE YREKYGRSQT VISDTSNVPQ RLLLPSVNDP NVWAVRCKVG KEKDIVFTIM
RKAMDLQYTS MPLEIISAFQ RDSLVGYVYV EARKQSHVLA ALNGILNVYT NNMILVPIKE
MPDLLKVQKQ TVELLPGAYV RIKRGKYAGD LAQVDNLSEN GLTARVRIVP RVDYSNSLKR
SKSITRPQSR LFNESEAYKS NPTKFYRRGP RTFVFNNEEF EDGFLVKDIR ISSLVTEGVN
PTLDEVSKFS PSNEDLDLSS LALSVKNDHA EFQFGDVVEV FVGEQAGVGG VVETVHGTVV
TIISNDGLRL DVPSRGLRKR FRHGDYVKVI AGKYKDDTGM VVRISKDEVT FLSDTMMTEL
TVFSRDLGEA GSAQAINSAY DLHDLVQLDV NTVGCVFSVE RDTYRVVDQH GGVRTAKASQ
ITMRHSNRRG VATDRNGTEI RVGDKVKEVG GENKEGTILH IYRAFVFLHN REIMENNGVF
VARSRNVATV AAKGARISTD LTKMNPALNN GPSLPPVANI KRTIGRDKAI GATVRIRKGP
MKGLLGVIKD TTDANARVEL HTGNKIVPVP KENLLYTTKN GDLITYTEFI ERSRGIRPGS
IGNVDGPSVP SWAQGARTPA YANGGQTQSW YSGSKTPAWS SGAKTPAWNA GGKTPAWNSG
NKTPAWNAGS KTPAWNSGNK TPAWNAGAKT PAWNSGGKTP AWNAGTKTPA WNAGGKTPSW
NSSAASNVVG QGPAYGGFSE TTWDTDDNNG SWTAPTPGGW AAPTPGGWNE DEGNSPNYVP
PSP
//
