ID A0A072PT93_9EURO Unreviewed; 1076 AA.
AC A0A072PT93;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 18-JUN-2025, entry version 42.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|ARBA:ARBA00020181, ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=A1O9_01077 {ECO:0000313|EMBL:KEF63101.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF63101.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF63101.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF63101.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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 -!- SUBUNIT: Component of the SPT4-SPT5 complex. Interacts with RNA
CC polymerase II. {ECO:0000256|ARBA:ARBA00025870}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEF63101.1}.
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DR EMBL; AMGV01000001; KEF63101.1; -; Genomic_DNA.
DR RefSeq; XP_013265691.1; XM_013410237.1.
DR AlphaFoldDB; A0A072PT93; -.
DR STRING; 1182545.A0A072PT93; -.
DR GeneID; 25276025; -.
DR VEuPathDB; FungiDB:A1O9_01077; -.
DR HOGENOM; CLU_003537_1_1_1; -.
DR OrthoDB; 28901at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0032044; C:DSIF complex; IEA:EnsemblFungi.
DR GO; GO:0140463; F:chromatin-protein adaptor activity; IEA:EnsemblFungi.
DR GO; GO:0003729; F:mRNA binding; IEA:TreeGrafter.
DR GO; GO:0003711; F:transcription elongation factor activity; IEA:EnsemblFungi.
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 FunFam; 2.30.30.30:FF:000029; Transcription elongation factor SPT5; 1.
DR FunFam; 3.30.70.940:FF:000005; Transcription elongation factor SPT5; 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; PF23042; KOW1_SPT5; 1.
DR Pfam; PF23284; KOW2_Spt5; 1.
DR Pfam; PF23291; KOW4_SPT5; 1.
DR Pfam; PF23290; KOW5_SPT5; 1.
DR Pfam; PF23037; KOWx_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; 5.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Reference proteome {ECO:0000313|Proteomes:UP000027920};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 222..314
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 318..345
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 484..511
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 537..565
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 660..685
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 751..778
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 851..1008
FT /note="Spt5 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01104"
FT REGION 1..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..20
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..960
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1055
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 117135 MW; AFE573AC7831E19A CRC64;
MASASWLNQD FGDDDEESDN EFNPATGGVS DDERNEDSKP SPPNRRSSSP RRSSASPKNS
KREIEDEDED DNTAENGAHD RGNEDDAKGD VDDEEGDEDE DEEEDEDEEI TNRPRKRRRR
GLNQFFEEEA EVDEDDDELE ADEEDLGPEF IQDTHPDDDL PPEADHDDRR HRELDRQRQL
EASMDAEKQA AAYRERYGRR TNAALSNSSF VPQNLLMPDV NDPSIWGVKC KPGKEKEIIV
RLNKKYSESL RSRNPMRVCS FFERGDGPMA GYIFVEARRK IDVDDALNGV SDVYPRGKMN
LVPVKEMPDL LRVTKTKELE VGGYVRIKRG IYTGDLAMIE EVESNGLDVN VRLVPRLTYG
MEEDQGRPGA DVKRKRPNAF NVPTINLANR PPQRLFNENE AKKRHDRFLQ QNRGLSKRNW
IYKGDTYIDG FLVKDFKLQH LITENVNPRL DEITKLTRTA DDGSEHLDLE TLAHSLRNTT
GDGSYLPGDE IEVYEGEQRG TIGRVEAVTG NIISIMVSEG ELTGQLVEVP VKGLRKRFRE
GDNVKIVGGS KYRDEVGMVL RIKDDKVTVL TNTSNEEITV FSKDLREATD AGGGGAGSSK
FDVQELVQID ATTVGIVVRA DRESVRILDQ NGSVATRIPS QISKIDTRKN TVATDKNGAE
IRVGDVVKES GGEAKSGTIL HLHRGYVFAH NKLGIENSGL WVNRCSNVIT TAAKGGRITA
PTTDLTKMNP ALQMRNRPDA SMAPPQRPGR DPLQGRLVHI NKGNYKGHRA IVKDTTVTEA
RLELQTKNKV INVPKSQLSI IDTNTQNKTR YDDWIRNRGG PPAMRTGQGI PGSRVPDSGF
GGRTPMVPAD GGRTPAWGTA SRTPAWSGPG GSGLDSGRTP AWKGASGSQT SYGGGGMTSY
GGAGNFGTNT GSRTPAWASG AKTPYGSSGG DGFGNSNSGF DAFGAGSRTP AYNPSSSRTP
AWSGPGNAAS APTPGARPYD APTPAVSAPT PAPFGDDAYT PYLAAPTPGA GQDAPTPAPN
FSKNANKEPL KHNRLAAFDA PTPAASAPTP YASGAFDAPT PAAGGPRYVD DDEDDD
//
