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Database: UniProt
Entry: SPT6_GIBZE
LinkDB: SPT6_GIBZE
Original site: SPT6_GIBZE 
ID   SPT6_GIBZE              Reviewed;        1408 AA.
AC   Q4HYQ4; A0A0E0RVD1; V6RPP5;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Transcription elongation factor SPT6;
DE   AltName: Full=Chromatin elongation factor SPT6;
GN   Name=SPT6; ORFNames=FGRRES_09904, FGSG_09904;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000305}.
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DR   EMBL; DS231669; ESU16548.1; -; Genomic_DNA.
DR   EMBL; HG970332; CEF75206.1; -; Genomic_DNA.
DR   RefSeq; XP_011318810.1; XM_011320508.1.
DR   AlphaFoldDB; Q4HYQ4; -.
DR   SMR; Q4HYQ4; -.
DR   STRING; 229533.Q4HYQ4; -.
DR   GeneID; 23556830; -.
DR   KEGG; fgr:FGSG_09904; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G06803; -.
DR   eggNOG; KOG1856; Eukaryota.
DR   HOGENOM; CLU_001680_0_1_1; -.
DR   InParanoid; Q4HYQ4; -.
DR   OrthoDB; 170310at2759; -.
DR   PHI-base; PHI:1601; -.
DR   Proteomes; UP000070720; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 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.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; SH2 domain; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1408
FT                   /note="Transcription elongation factor SPT6"
FT                   /id="PRO_0000238576"
FT   DOMAIN          1101..1168
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          1213..1314
FT                   /note="SH2"
FT   REGION          1..199
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"
SQ   SEQUENCE   1408 AA;  162213 MW;  8CB31D52E5DFE1BF CRC64;
     MSNSMRDLIS GEAELDDEEE DESFDERGGQ RRHKNAVEDS SEEEEDDDDE EEARKVREGF
     IVDEDEDEDE GGESDADVRP LHKRKREHRD REEEAQLDED DLDLIGEQFG ERPKPTTQSK
     FKRLKRGTRD EDRGNQRRGL DDIFSDEEDD AGEQRAYNNR SSYRQADEFD DFIEEDFPDD
     PEELEQQRED AEVARPRDRV IGNIADTANL DKDALDDMEA IFGNGEDYDW ALQMEEEEED
     REREEQAIEL KDVFEPSQLK EKLLTDEDNE IRFTDEPERF QIDRKTFKSL QLTAEQFKEE
     ARWITNQLWP KKGLASDLQS PFGKAVGKVL EFFIVDEVEV PYVFQHRKDY LLHTRKTRNP
     NRDDPDAPEY VISADKLLNQ DDLWKILELD IKFRSFVDKR NALEKTVDNL KGMEIHDAMV
     DEMIPEATTM EELQDLQDYL HFQYGQQLKD LAALAGNLSL TKRPGSKSNL LERVRQGKAY
     GFVRAYGISA DQLAKNALRH GKKVTPDDDA QYPMDLADSL IDDVFSTGDQ VISAARQMYS
     EELFASPRMR KHFRNSYYQA AEISCRRTEK GLRRIDDSHP YYEIKYLQNQ AIADLVHQPE
     LFLKMMKAEE EGLVTIKLDM PARYDFRQHL YQEFESENFS DRAEQWREER KKVLDLAYPK
     LEKIIAKNVK EVIRTFCQDE VLKMCREEYA KRLDQAPYKP KGMILGTTPR VLVLSNGMSD
     PARDPICWAW VEEDGRVIEQ GKLGNLARDE RQREEFEELV KRRRPDVIGV SGWSAETTKL
     VRDLEGLVNE KGLMGPEFED PDTNDYRTEP LEVVVVNDEV ARLYKDSPRA LAEHPSLNPI
     TRYCVALARY MQNPMKEYAA LGKDVSSLSY HPCQNLLPAD KLAKYLDSAM VDMVNLCGVD
     INEAMNDTYT ANLLPYVSGL GPRKATSVIK AINANGGAVG TRDELVGDPD SGKLPVVGPR
     VWNNCASFLF IEYEATNPSS DPLDNTRVHP EDYELGRKMA ADALELDEED VKGETDENGP
     GAIVRKLFKM DEQDKVNELV LEEYAEQLER NYSQRKRATL ETIRAELQAP YEELRRNFAL
     LSASEIFTMF TGETKHTLCE GMIVPVNVRV VKDDFAIVKL DCGIEGRVEG HEVSHRSSIK
     EVLSSGQTSQ AKILDINYKD FMAKLSMRED ALRIPYKRPI NLGRDGWDYV LEAADKEELR
     EKDKTTGRTQ RVVKHPNFKP FNGLQAEEYL GSQPNGEVVI RPSSKGNDHL AVTWKVADGV
     FQHIDVLEMQ KETEFAVGKL LRVGGKYTYT DLDELIVEHV KAMARKVEEL MRHDKYQNRS
     RGETEKWLTT YIDANPNRST YAFCIDTKHP GYFWLCFKAS RAAKVIALPV RAIPQGFELK
     GYQYPDMRAL CNGFKLRYQN EFSKMGQR
//
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