ID A0A1D6NSG8_MAIZE Unreviewed; 989 AA.
AC A0A1D6NSG8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Transcription elongation factor SPT5 {ECO:0000256|PIRNR:PIRNR036945};
GN ORFNames=ZEAMMB73_Zm00001d044971 {ECO:0000313|EMBL:AQL01214.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AQL01214.1};
RN [1] {ECO:0000313|EMBL:AQL01214.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQL01214.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000785; AQL01214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6NSG8; -.
DR ExpressionAtlas; A0A1D6NSG8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
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; cd06085; KOW_Spt5_5; 1.
DR CDD; cd06086; KOW_Spt5_6; 1.
DR CDD; cd09888; NGN_Euk; 1.
DR Gene3D; 2.30.30.30; -; 4.
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; IPR041978; KOW_Spt5_5.
DR InterPro; IPR041980; KOW_Spt5_6.
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; IPR005825; Ribosomal_uL24_CS.
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; PF03439; Spt5-NGN; 1.
DR Pfam; PF11942; Spt5_N; 1.
DR PIRSF; PIRSF036945; Spt5; 3.
DR SMART; SM00739; KOW; 5.
DR SMART; SM00738; NGN; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Elongation factor {ECO:0000313|EMBL:AQL01214.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036945};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein biosynthesis {ECO:0000313|EMBL:AQL01214.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036945}.
FT DOMAIN 188..274
FT /note="NusG-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00738"
FT DOMAIN 279..306
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 431..458
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 483..510
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 670..697
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT DOMAIN 937..964
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..37
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..126
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 989 AA; 109874 MW; 76B2F4750817BD7E CRC64;
MARRGHDDDD DEVDEEEEED AYDLDDDEDE DEEDDYEEET RRGKASRGGG GAKSGGGRKR
SREDNFIDDS AIEDEDDEDD DGGGRPRKKG GGGVRGFFDE EAQVDEDEEE EDEGEGEDDF
INDAGADLPD EDVVRGSRRH SIPMRDEEED IDEMERQVRE RYARSTHIEY GEEAAEVEQQ
ALLPSVKDPK LWMVKCAIGH ERETAICLMQ KFIDRSDLQI KSVVALDHLK NYIYVEAEKE
AHVKEACKGL RNIYASAKIT LVPIKEMADV LSVESKSVDL SRDSWVRMKL GIYKGDLAKV
VDVDNVRQRV DVKLIPRIDL QALASKLEGR DIVKKKAFVP PPRFFNIDEA REMHIRVERR
RDKESGEYFE WVDNLKFKDG FLYKSVSTKS IHKSNIQPTF DELEKFKKPG DDMNGDMASL
STLFANRKKG HFMKGDAVIV IKGDLKNLEG WVEKVEDETV HIRPKISDLP KTLAFNEKEL
CKYFKPGDHV KVISGVQEGA TGMVVKVEGH VLIILSDTTK EHIRVFADHV VESSEITTGI
TRIGDYELHD LVLLDNLSFG VIIRVEAEAF QVLKGVPDRP EVVLVKLREI KSKIERRSSA
KDRSNNIISA KDVVRVVEGA CKGMDTADAR LDALRSSASI LQSPGRLPPR GPNMNYGGRF
GGGRGGRGYD ALVGKCIKIK SGPYKGYRGR VKEVTGALVR VELDSLMKIV TVKRDDIADT
PTVATPFREP RYSLGGETPM HPSRTPHHAY QTPMRDPGAT PIHDGMRTPM RSRAWAPMSP
PRDNWEDGNP ATWGSSPAYQ CTIVTMRLFC IVWILTRMML FFPHSDLLAN APSPYVPSTP
VGQPMTPNSA SYLPGTPGGQ PMTPGNAGMD MLSPIIGGDG EVAWLLPDVL VNVLRGGDDG
PGVVREVLGD GSCRVALGSS GNGDVVTVLA NEVEVIRPKK SDRIKILNGN FRGYTGKLIG
IDGSDGIVRL DETYEVKILD MVILAKLAT
//