ID A0A1B8B837_FUSPO Unreviewed; 1493 AA.
AC A0A1B8B837;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Transcription elongation factor Spt6 {ECO:0000256|ARBA:ARBA00020248, ECO:0000256|PIRNR:PIRNR036947};
GN ORFNames=FPOA_02834 {ECO:0000313|EMBL:OBS28899.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS28899.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS28899.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS28899.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-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}.
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:OBS28899.1}.
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DR EMBL; LYXU01000001; OBS28899.1; -; Genomic_DNA.
DR STRING; 36050.A0A1B8B837; -.
DR OMA; LCNGFKT; -.
DR Proteomes; UP000091967; 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; cd00164; S1_like; 1.
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; IPR006861; HABP4_PAIRBP1-bd.
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; PF04774; HABP4_PAI-RBP1; 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.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036947};
KW Reference proteome {ECO:0000313|Proteomes:UP000091967};
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 1101..1168
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 1..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1493 AA; 171457 MW; 9C9A77A17DBD95B7 CRC64;
MSNSMRDLIS GEAELDDEEE DESFDERGGQ RRHKNAVEDS SEEEEDDDDE EEARKVREGF
IVDEDEDEDE GGDSDADVRP LHKRKREHRD REEEAQLDED DLDLIGEQFG ERPKPQTQSK
FKRLKRGTRD EDRGNQRRGL DDIFSDEEDD AGEQRAYNNR SSYRQADEFD DFIEEDFPDD
PEELEQQRED AEVARPRDRV IGNIADTANL DKDALDDMEA IFGNGEDYDW ALQMEEEEED
REREEQAIEL KDVFEPSQLK EKLLTDEDNE IRFTDEPERF QLDRKTFKSL QLTAEQFKEE
ARWITNQLWP KKGLASDLQS PFGKAVGKVL EFFIVDEVEV PYVFQHRKDY LLHTRKTRNP
NRDDPDAPEY VISADKLLNQ DDLWKILELD IKFRSFVDKR NALEKTVDNL KGMEIHDAMV
DEMIPEATTM EELQDLQDYL HFQYGPQLKD LAAMAGNLSL TKRPGSKSNL LERVRQGKAY
SFVRAYGISA DQLAKNALRH GKKVTPDDDA QYPMDLADSL IDDVFSTGDQ VISAARQMYS
EELFASPRMR KHFRNSYYQA AEISCRRTEK GLRRIDDSHP YYEIKYLQNQ AIADLVHQPE
LFLKMMKAEE EGLVTIKLDM PARYDFRQHL YQEFESENFS DRAEQWREER KKVLDLAYPK
LEKIIAKNVK EVIRTFCQDE VLKMCREEYA KRLDQAPYKP KGMILGTTPR VLVLSSGMSD
PARDPICWAW VEEDGRVIEQ GKLGNLARDE RQREEFEELV KRRRPDVIGV SGWSAETTKL
VRDLESLVNE KGLMGPEFED PDTNDYRTEP LEVVVVNDEV ARLYKDSPRA LAEHPSLNPI
TRYCVALARY MQNPMKEYAA LGKDVASLSY HPCQNLLPAD KLAKYLDSAM VDMVNLCGVD
INEAMNDTYT ANLLPYVSGL GPRKATSVIK AINANGGAVG TRDELVGDPD SGKLPVVGPR
VWNNCASFLF IEYEATNPSS DPLDNTRVHP EDYELGRKMA ADALELDEED VKAETDENGP
GAIVRKLFKQ DEQDKVNELV LEEYAEQLER NYSQRKRATL ETIRAELQAP YEELRRNFAL
LSPSEIFTMF TGETKHTLCE GMIVPVNVRV VKDDFAIVKL DCGIEGRVEG HEVSHRSSIK
EVLSSGQTAQ AKILDINYKD FMAKLSMRDD ALRVPYKRPI NLGRDGWDYV LEAADKEELR
EKDKTTGRTQ RVVKHPNFKP FNGLQAEEYL GSQPSGEVII RPSSKGNDHL AVTWKVADGV
FQHIDVLEMQ KETEFAVGKL LRVGGKYTYT DLDELIVEHV KAMARKVEEL MRHDKYQNRS
RGETEKWLTT YIDANPTRST YAFCIDTKHP GYFWLCFKAS RAAKPTKMTR SHKANDRDHK
GIAEGTMLPT ETVPRFFGKN GFADVDPKKM KKDGSGRGNW GTVNDDIAGE QFTFTNTRRR
SNSSSFSHVA DFKTKFEVNE PEPVFEESLH GPEEEDHEDL TKTDSSESGR SSS
//
