ID A0A109FI11_9BASI Unreviewed; 1012 AA.
AC A0A109FI11;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=RHOSPDRAFT_17389 {ECO:0000313|EMBL:KWU44835.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44835.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU44835.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU44835.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ954476; KWU44835.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109FI11; -.
DR STRING; 1305733.A0A109FI11; -.
DR OrthoDB; 24955at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; 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 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; 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; PF00467; KOW; 1.
DR Pfam; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 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 Elongation factor {ECO:0000313|EMBL:KWU44835.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Protein biosynthesis {ECO:0000313|EMBL:KWU44835.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 142..236
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 241..268
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 400..427
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 454..481
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 667..694
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 47..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 106995 MW; 550D4E28BBCCA31A CRC64;
MIVRGRNGSV RSLVFWTACP HLSLPETPLI RFGFPQRRRR GGAQFLDIEA DVDEDEDEEE
EEGEEGFVAN GADDGDDADF AQGDFDGDAS HRRLDRRRMA QKDKEAAELA AELNQRYRRN
KYTTDGAEDW APKAMLMPSE KDPRIWGIKC KTGRERDLIL SISRKAVALE AADNGIPLAI
ISAFQRDSLK GFIYIEARSE QDVRTAVHGL VGLYMNGPNG IFLVDVEEMP DLLRTKQKRV
DLQPGGWVRF KRGKYAGDLA QILAPSENGD EIAVKFIPRI DLAPKDDALG VGPDGRKRKK
GATMPLAFRP PQRLFNAEEI AKIYGQKEVQ KRGNVLIFKG DEYHDGFCEK DVRVSSLNVE
DVTPTIDELT RFQGDAAAEA GGALDLSQIA DAARTLSKTI LQPGDHVDIF EGDQKGVYGT
VDSVTNEVVV VTPHADLDLE GTKIEVPARS VRKRFKEGDH VKVMQGANAD ETGLVVKVEG
DVVTFLSDLS STEVSVFAKD VREAAEVGSG INVIAGYELH DLVQLDPQTA GVIIKMERDQ
FRVLDQTGSV RALKPNQLSG KVQTRFAVAT DKDGFDIKPG ENNNSGIERR GKVLHVYRSM
FAFLHSRDIT ENGGVFVSYA RNLESTAPRP NKPSGGMGMN PDRLNMMGGG PAVPKVQVAT
GVQMGRDHRI NRRVAITRGT YKGNHGVIKD VTGNSARVEL HSISKTVTVS IETLKERTDA
GELIPLMDRP GGGGGATPAY AGAGAYGRTP HYAGGAAAAA PGMGATPNPY GAPSSSRTPY
GAGFAGGKTP DPRHLAGGRT PAYGTGAGIA SGGRTPAYGA KNGYAAASAP TPGGNLQGAA
PTPAASGSGA AAWADDDWGD QTSVQQGAPT PAPGRDNGPD YNGAPTPYAG APTPAAGGAP
TPGAYLGAPT PGFSGAPTPS AYPSGPTPGA SGSYGAAAQT PGGGAAGGYY QTPYAGAATN
AAEPLEEREM MAAADAVAVP HPSEWVVENV KIVVKESAFQ GGRLTGQHGK LN
//
