ID G8BZ54_TETPH Unreviewed; 993 AA.
AC G8BZ54;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN Name=TPHA0K00480 {ECO:0000313|EMBL:CCE65182.1};
GN OrderedLocusNames=TPHA_0K00480 {ECO:0000313|EMBL:CCE65182.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65182.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE65182.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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; HE612866; CCE65182.1; -; Genomic_DNA.
DR RefSeq; XP_003687616.1; XM_003687568.1.
DR AlphaFoldDB; G8BZ54; -.
DR STRING; 1071381.G8BZ54; -.
DR GeneID; 11533325; -.
DR KEGG; tpf:TPHA_0K00480; -.
DR eggNOG; KOG1999; Eukaryota.
DR HOGENOM; CLU_003537_1_0_1; -.
DR OMA; PYPVGYM; -.
DR OrthoDB; 24955at2759; -.
DR Proteomes; UP000005666; Chromosome 11.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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 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; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 2.
DR SMART; SM01104; CTD; 1.
DR SMART; SM00739; KOW; 4.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 225..316
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 322..349
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 474..501
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 525..552
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 737..764
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 835..966
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..148
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 109287 MW; 993DD4D029ACB0BD CRC64;
MSEEQSGHEV PVKREDTSLP VEAEAAAVDP PIPADEASNE ASEEAAVLKR PLEEDSDTAE
QPNAKRENTG IAGDEQQEQH NEEDDNNEDY EEEEEEEEDE EEGENEEDEE DSMAPSKRQR
QERNRFLDIE AEVSDDEDED EDEEESELVK EGFITRGDEE EEGARRDDRL HRQLDQNLNK
TSEEDAQRLA KELRERYGRT SSKQYRDAAQ DGYIPQRFLL PSVDTATIWG VRVRPGKEKE
LVRKLLKKKL NLDRAMGNKK LKILSIFERD NFKGRIYIEA PKQSVIEKFC NGVPDIYVSQ
KILIPVQELP LLLKPTKSDD VTLEEGNYVR IKRGIYKGDL AIVDQISENN LEVMLKIVPR
LDYGKYDEID PITQQRKARR ATYANRPPSQ LFNPTLALRL DQANLYKRDD RHFTYKNEDY
VDGYLYKSYR IQHVETKNIQ PTVEELARFG SKDGSIDLAT ISQTIKKAQV ANIIFHPGDR
VEILNGEQRG SKGIIIKTTT DIATVRLPEI QLKPLEFPVS TLRKIFQPGD HVTVVNGDHQ
GDAGLVLAIK QGQVTFMSNQ TREEITITAN NLTKSMDSTP TSSEYSLHDI IELSAKTVAC
IIQAGHDLFK IIDETGKVST ITKGSILSKV NVARARVSTV DDKGNEIKIG DTIVEVIGAR
REGQVLYIQN QQIFAMSKKI IENAGVFVVS PSNVEAVSSK DNMLGGSIDL NKLNPEVISK
MGPPPVAKAQ QSRGGRDVAL GKTVRIRSAG YKGQLGIVKD VNGDTATIEL HSKNKNITVD
KKKLTFYNKE GGEGITYDEL VSRRGRVPQP RMGPSYVSAP RDMPRDISGP GQLSGGMTPG
WGGFDGGKTP AVNSGPSGNG GASAWGNTSS WGGSSSWGGR GAGGNTSAWG GSGATSTWGG
ASAWGNKSSW GGGSTWAQNG ENNGNASNWG GNKSSYGGAS TWGNSGRDGA ASAWRGNVTN
NNKNTNSDNN NNGNMSTWGN NEHSRNNSSW GGH
//
