ID A0A0A0LKK6_CUCSA Unreviewed; 1625 AA.
AC A0A0A0LKK6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Transcription elongation factor spt6 {ECO:0000256|PIRNR:PIRNR036947};
GN ORFNames=Csa_2G075460 {ECO:0000313|EMBL:KGN61287.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN61287.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN61287.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
CC -!- FUNCTION: Plays a role in maintenance of chromatin structure during RNA
CC polymerase II transcription elongation thereby repressing transcription
CC initiation from cryptic promoters. Mediates the reassembly of
CC nucleosomes onto the promoters of at least a selected set of genes
CC during repression; the nucleosome reassembly is essential for
CC transcriptional repression. {ECO:0000256|ARBA:ARBA00025022}.
CC -!- FUNCTION: Transcription elongation factor that enhances transcription
CC elongation by RNA polymerase II (RNAPII).
CC {ECO:0000256|PIRNR:PIRNR036947}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR036947}.
CC -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000256|ARBA:ARBA00009253,
CC ECO:0000256|PIRNR:PIRNR036947}.
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DR EMBL; CM002923; KGN61287.1; -; Genomic_DNA.
DR RefSeq; XP_011649014.1; XM_011650712.1.
DR STRING; 3659.A0A0A0LKK6; -.
DR EnsemblPlants; KGN61287; KGN61287; Csa_2G075460.
DR GeneID; 101219281; -.
DR Gramene; KGN61287; KGN61287; Csa_2G075460.
DR KEGG; csv:101219281; -.
DR eggNOG; KOG1856; Eukaryota.
DR OMA; LCNGFKT; -.
DR OrthoDB; 170310at2759; -.
DR Proteomes; UP000029981; Chromosome 2.
DR GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:UniProtKB-UniRule.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0140673; P:transcription elongation-coupled chromatin remodeling; IEA:InterPro.
DR CDD; cd09928; SH2_Cterm_SPT6_like; 1.
DR CDD; cd09918; SH2_Nterm_SPT6_like; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 1.10.10.650; RuvA domain 2-like; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR Gene3D; 1.10.10.2740; Spt6, Death-like domain; 1.
DR Gene3D; 1.10.150.850; Spt6, helix-hairpin-helix domain; 1.
DR Gene3D; 1.10.3500.10; Tex N-terminal region-like; 1.
DR Gene3D; 3.30.420.140; YqgF/RNase H-like domain; 1.
DR InterPro; IPR041692; HHH_9.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR049540; Spt6-like_S1.
DR InterPro; IPR028083; Spt6_acidic_N_dom.
DR InterPro; IPR042066; Spt6_death-like.
DR InterPro; IPR032706; Spt6_HHH.
DR InterPro; IPR028088; Spt6_HTH_DNA-bd_dom.
DR InterPro; IPR035420; Spt6_SH2.
DR InterPro; IPR035018; Spt6_SH2_C.
DR InterPro; IPR035019; Spt6_SH2_N.
DR InterPro; IPR028231; Spt6_YqgF.
DR InterPro; IPR023323; Tex-like_dom_sf.
DR InterPro; IPR023319; Tex-like_HTH_dom_sf.
DR InterPro; IPR017072; TF_Spt6.
DR InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR InterPro; IPR037027; YqgF/RNaseH-like_dom_sf.
DR PANTHER; PTHR10145; TRANSCRIPTION ELONGATION FACTOR SPT6; 1.
DR PANTHER; PTHR10145:SF6; TRANSCRIPTION ELONGATION FACTOR SPT6; 1.
DR Pfam; PF14635; HHH_7; 1.
DR Pfam; PF17674; HHH_9; 1.
DR Pfam; PF14641; HTH_44; 1.
DR Pfam; PF14633; SH2_2; 1.
DR Pfam; PF14632; SPT6_acidic; 1.
DR Pfam; PF21710; Spt6_S1; 1.
DR Pfam; PF14639; YqgF; 1.
DR PIRSF; PIRSF036947; Spt6; 1.
DR SMART; SM00316; S1; 1.
DR SMART; SM00732; YqgFc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 2.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF158832; Tex N-terminal region-like; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036947};
KW Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR036947};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR036947}.
FT DOMAIN 1107..1178
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1436..1625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..61
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..186
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1625 AA; 183199 MW; 5031DA2AB5DE1345 CRC64;
MRLDTDEDDR EPLDGDDVDG HNMGDEEDEE DEEGEDEYEK DGFIVDDVEE EDEEDVEERE
DSDDERQKKK KRKKKEEYVL DEDDYELLED NNISIQRPKG SKKFKRLKKA RRDNLEPSGF
SDDEDFVESS RGGRTAEEKL KRSLFGDDEA PLEDIAEEEE QPEEEEDADI GDEDEMADFI
VDEEEDEDGA PIRRKKLKKK KSRQAPGVSS TALQEAHEIF GDVDELLQLR KRELDTQEWR
EKRLEDEFEP IVISEKYMTE KDDQIREIDI PERMQISEES TGSPPTDDAS LDDEASWIHG
HIANGVSSLS SNASGQDLSV TKDDILRYLD LVHVQKLDIP FISMYRKEEI LSLLKDTEHE
AGDDQDKNDK APTLRWHKLL WAIQDLDKKW LLLQKRKKAL QSYYKNRYLE EIRTAEHVTR
TTLNRQLFDS VNRSLEAAES EREVDDVDSK FNLHFPPGEV GVDEGQFKRP KRKSLYSICS
KAGLWEVAGK FGYSSEQFGL QLSLEKMRND ELEDPKETPE EMASNFTCAM FESPQAVLKG
ARHMAAIEIS CEPCVRKHVR SYFMDYAVIS TSPTADGNVA IDSFHQFSVV KWLREKPLNR
FEDAQWLLIQ KAEEEKLLNV TLKLPEKHLN KLISDFNEYY LSDGVSKSAQ LWNEQRKLIL
QDALSGFLLP SMEKEARSLM TSKAKKWLLM EYGKNLWSKV SIGPYQHKEN DISSDEEAAP
RVMACCWGPG KPATTFVMLD SSGEVLDVLY TGSLTLRSQN VNDQQRKKND QERVLKFMTD
HQPHVVVLGA VNLSCTRLKD DIYEIIFKMV EENPRDVGHE MDGLSIVYGD ESLPRLYENS
RISSDQLQGQ SGIVKRAVAL GRYLQNPLAM VATLCGPGRE ILSWKLNPLE NFLTPDEKYG
MVEQVMVDVT NQVGLDTNLA ISHEWLFSPL QFIAGLGPRK AASLQRSLVR AGSIFTRKDF
VTAHGLGKKV FVNAVGFLRV RRSGLAASSS QFIDLLDDTR IHPESYALAQ ELAKDVFDED
VKGDANDDED AEMAIEHVRD RPHLLRTLDV DEYAKSKKRE DKIETFLDIK RELMQGFQDW
RKQYEEPSQD EEFYMISGET EDTLAEGRIV QATVRKVLGQ KAICGLESGL TGMLMKEDYA
DDSRDISDLS DRLREGDIVT CKIKSIQKNR YQVFLVCKES EMRSNRHQIT QNLDPYYHED
RSSLQSEQEK SRKEKELAKK HFKPRMIVHP RFQNITADEA MELLSDKDPG ESIVRPSSRG
PSFLTLTLKI YDGVYAHKDI VEGGKEHKDI TSLLRIGKTL KIGEDTFEDL DEVMDRYVDP
LVAHLKAMLS YRKFRRGTKA EVDELMKIEK SEYPMRIIYG FGISHEHPGT FILTYIRSTN
PHHEYIGLYP KGFKFRKRMF EDIDRLVAYF QRHIDDPQHD SAPSIRSVAA MVPMRSPATG
GSSAASAGSP WGGSSHEGGW RSQSFDRDRS STPGSRTGRN DNRNSSGRDG HPSGLPRPYG
GRGRGRGSYN NNRGNNDRSD SGYDGSRWDS SSKDGDDGLS NFPGAKIHNS PGKEAFPGGW
SSGGGGGGNG WNESSGGGGG GGGGGGSGSG GGGSGSGGGG WGGTGGNSKG NWSGSGGSNS
GGWGS
//
