ID A0A0G2EYZ0_9EURO Unreviewed; 1378 AA.
AC A0A0G2EYZ0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Transcription elongation factor Spt6 {ECO:0000256|PIRNR:PIRNR036947};
GN ORFNames=UCRPC4_g01129 {ECO:0000313|EMBL:KKY27329.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY27329.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY27329.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY27329.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY27329.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY27329.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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 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}.
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:KKY27329.1}.
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DR EMBL; LCWF01000025; KKY27329.1; -; Genomic_DNA.
DR OrthoDB; 170310at2759; -.
DR Proteomes; UP000053317; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:UniProtKB-UniRule.
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; 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; 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; 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 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 Elongation factor {ECO:0000313|EMBL:KKY27329.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036947};
KW Protein biosynthesis {ECO:0000313|EMBL:KKY27329.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999};
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 1070..1139
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..40
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 158623 MW; 9B7F8E158E3FF5F4 CRC64;
MSARDLVEGE ALLDDEEDDE DFDEETGEIR EGFIVDEEEE EEQQERRRER RKRRREERDR
EDEELDEEDL DLIGEKPEEP QESKFKRLKR GPRDARESRV SRGIDDIFDE SDEDEAPTRG
TAANEFDDFI EEDVFSDEER ERQREDEEVA RPARRGFGYG ITADTTGLDE QALDDMRRAF
GDGSDYYFAL EKEDQQEEID EEQGKHLDLK DVFEPSQLVE KMMTEEDQAI RNTDEPERCQ
IARKPYRHVT LTEEQFKEEG QWISNLMLPK RALKQELHEP FRRAVAKVLE LMVAEDFEVP
FIFHNRKDYL IHALKKPVGK NKEGEMEYEI EAAKLLNQSD LWEIFEQDLK FRAFIDKRNT
IQKTYDNLVS TSISPDEIFE SMLPAAVTME ELQDVQDYLY FQYSSQLKDL TASGAVETNG
DGVHRKKAVA KSLFERVRGG KAYNLVRAFG ISANGFAQNA LKQGVKNYTE DPSDRPDDMA
DSIVDTDFQT GSHALKAAKT MFVEELVTSP RMRNVIRQAF YTMGVVECYR TEKGLRKIDE
HHPYYDFKYL RNQELNQILG QPELYLKMLQ AENEGLIEVR VRLQNAEHFT KNLHKHIVSD
NFSEVADAWN RERIEVVDAA VTKLSKLMSR LVKENLRAEC ENLVARTCRE EFARRLDQAP
YQPKGMKKGI IPRVLAMSIG KGTYGRDSIV WAWVNEEGRV LENGKFVDLS PGDKERGLPD
GKDVVDFVEV VRRREPDVIG ISGFSPETRK LYTNLMALIK ERDLRGAEYT DENDREVKDP
LEVIIVNDEI ARLYQTSERA KLDHPSFAPL THYCVALAKY MQDPMKEYAA LGSDLASIMF
APGQQALDQK KLLHHLETVL VDHVNMCGVS LNDAISDMAT ANLLPYVAGL GHRKASHMLK
VINMNGGAVN NRSELIGIGA ERPAMGTKVW ANASSFLYLE YDAAEPESEY LDGTRIHPED
YDIARKMAAD ALELDEEDIQ AETDENGAGA IVRKLIKDDA QDRVNDLILE EYAEQLERNL
NQRKRATLEN IRAELIEPYE ELRQPFMTAL GTDEIFTMFT GETRDTLERG MIVPISIKRV
MNDHIDAKLD CGIDVYVGET ELSDRFDMSV KQMYSVHQTI QAKLLSLDRK NFTANCSLRE
EQLKRPYRKY NDRMHSEWDD RQEAADQKLL EEKTDGGGRA TRVIKHPLFR PFNSAQAEEY
LGSQNRGDVV IRPSSLGVDH LAVTWKVSDG VFQHIDVLEL DKENDFALGK TLKIGGRYTY
SDLDELIVLH VKAMAKKVDE MMTNEKYQNG SKADTDRWLT TYTEANPKRS VYAFCINPKY
PGYFYLCFKA GQHGKLQNWP VKVIPQGFEL QKNPYPSMRD LTNGFKLLYT NLQNGMRR
//
