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Database: UniProt
Entry: A0A136J1M3_9PEZI
LinkDB: A0A136J1M3_9PEZI
Original site: A0A136J1M3_9PEZI 
ID   A0A136J1M3_9PEZI        Unreviewed;      1419 AA.
AC   A0A136J1M3;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Transcription elongation factor Spt6 {ECO:0000256|ARBA:ARBA00020248, ECO:0000256|PIRNR:PIRNR036947};
GN   ORFNames=Micbo1qcDRAFT_69685 {ECO:0000313|EMBL:KXJ91140.1};
OS   Microdochium bolleyi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Microdochiaceae; Microdochium.
OX   NCBI_TaxID=196109 {ECO:0000313|EMBL:KXJ91140.1, ECO:0000313|Proteomes:UP000070501};
RN   [1] {ECO:0000313|Proteomes:UP000070501}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J235TASD1 {ECO:0000313|Proteomes:UP000070501};
RG   DOE Joint Genome Institute;
RA   David A.S., May G., Haridas S., Lim J., Wang M., Labutti K., Lipzen A.,
RA   Barry K., Grigoriev I.V.;
RT   "Draft genome sequence of Microdochium bolleyi, a fungal endophyte of
RT   beachgrass.";
RL   Submitted (FEB-2016) 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}.
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DR   EMBL; KQ964251; KXJ91140.1; -; Genomic_DNA.
DR   STRING; 196109.A0A136J1M3; -.
DR   InParanoid; A0A136J1M3; -.
DR   OrthoDB; 170310at2759; -.
DR   Proteomes; UP000070501; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 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; IPR000980; SH2.
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; 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; SM00252; SH2; 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.
DR   PROSITE; PS50001; SH2; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036947};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070501};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
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          1108..1177
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          1225..1323
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          1..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..58
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1419 AA;  164020 MW;  B24AA669CC81851D CRC64;
     MSNSMRDLVI GEAELDDDED DESFDEETGE ARQRERKRNG EMDDSSDDED DDDDEEEAAK
     IREGFIVDED EEEEEDEDPE ERRQRRKRKR RQEREEDAQL DEEDLDLIGE TIPDADRNQA
     SQKNYKRLKR GHQEEKARGS ERRGLDDMFD DEEEELDERP YGRPSHRAAV DEFDDFIEED
     FPEDEDERMR QMEDLEVARP RERQIAGGVL DTAGLDKDAL EDMAAIFGNG EEYAWALDME
     EEEEERQKGE QTLELKDVFE PSQLAEKLLT EADNEIRFTD EPERFQLDRK PFKHLQISAD
     QFREESEWIM NLMWPQKQLS SDLHSPFHKA IGKVLEYFVV EELEVPYVFQ HRKDYLIHAR
     KNRNPDYQTD SDAPQFIINA EKLLTQDDLW RILELDIQFR SLIEKRNALE KTYDNLRGIT
     EGIDEMIPEM IPQAATIGEL QDIQDFVQFQ YAAQLKDLAS MNGTSKETKR PGTKASLFDR
     VRKSKAYRFV KAYGISPDRL AQNALREGKK VLADDEQMLP IDLADALTDS DFPTGEQVLK
     QGRQMYSEEM FMSPRMRKHF RIHFYQMGEV SCHRTEKGLR RIDEAHPFYE IKYLVNQSIS
     DLARHPERFL KMMKAEEEGL IEVRLRLMNE REFKRQLLAE FKSDNYSELA DAWNEERRQV
     LDLAFPKLER LIAKGVKDSL RTACQDELLK VCREEYSKRL DQAPYKPKGM VLGTAPRVLA
     LSNGMGDPGR EPVFWVWVDE DGRIAETGQL GNLSRDEAQR DLFVDIVERR KPDVIGVSGF
     SADTQRLVRD IEALVSEKKL EGAEYTDPDS DDYRSDLLEV VVVNDEVARL YKDSPRAQAE
     NPTLNQVARY CVGLAKYLQN PMKEYAALGK DVASLLFHPS QHLLPPEKFL KHLDTAMVDM
     VNLYGVDINE AVSDSYTANL LPYVAGLGPR KATSVIKAIN TNGGIVNSRD ELVGDPDNNK
     LPVVGPRVWN NCASFLFIEY DATNPTSEPL DNTRVHPEDY ELGRKMAADA LELDEEDVKA
     ETDENGPGAI VRKLFRDDEQ EKVNELILEE YAEQLEKNYS QRKRATLETI RAELQAPYEE
     IRRPFATLQT DQIFTMFTGE TKESLAEGMI ISINIRVVKD DFAIAKLDCG IEGRIDAQEV
     SYRPGTSMRD VIHMGQTVQA KILELNRKDF MTKLSLREDE LRKPYRKYND HDRDAWDFRL
     ESDDQEALRE KDKATGRAQR MIKHPYFKTF NSAQAEEYLG SRAQGDVVVR PSSKGNDHLT
     ITWKVADGVF QHIDVLELQK DSEFALGKQL RIGGKYTYTD LDELIESHVK AMAKKVNELM
     NHEKFKQGSL ADLEKWLTSY SNANATQSIY LFGINPKHPG YFSLCFKVNK AAPIMKWHVK
     VVPQAFEMMG SQYPDMRALC NGFKLRLNNE LSKMQQGRR
//
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