SPT6_CANGA
ID SPT6_CANGA Reviewed; 1449 AA.
AC Q6FLB1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Transcription elongation factor SPT6;
DE AltName: Full=Chromatin elongation factor SPT6;
GN Name=SPT6; OrderedLocusNames=CAGL0L04774g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380958; CAG61953.1; -; Genomic_DNA.
DR RefSeq; XP_448983.1; XM_448983.1.
DR PDB; 3GXW; X-ray; 1.90 A; A/B/C/D=1250-1348.
DR PDB; 3GXX; X-ray; 2.40 A; A/B/C/D=1250-1348.
DR PDB; 3PJP; X-ray; 1.60 A; A/B=1250-1444.
DR PDB; 6QTC; NMR; -; A=1249-1444.
DR PDBsum; 3GXW; -.
DR PDBsum; 3GXX; -.
DR PDBsum; 3PJP; -.
DR PDBsum; 6QTC; -.
DR AlphaFoldDB; Q6FLB1; -.
DR BMRB; Q6FLB1; -.
DR SMR; Q6FLB1; -.
DR STRING; 5478.XP_448983.1; -.
DR EnsemblFungi; CAG61953; CAG61953; CAGL0L04774g.
DR GeneID; 2890706; -.
DR KEGG; cgr:CAGL0L04774g; -.
DR CGD; CAL0135088; CAGL0L04774g.
DR VEuPathDB; FungiDB:CAGL0L04774g; -.
DR eggNOG; KOG1856; Eukaryota.
DR HOGENOM; CLU_001680_0_1_1; -.
DR InParanoid; Q6FLB1; -.
DR OMA; LCNGFKT; -.
DR EvolutionaryTrace; Q6FLB1; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0000791; C:euchromatin; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0031491; F:nucleosome binding; IEA:EnsemblFungi.
DR GO; GO:0001073; F:transcription antitermination factor activity, DNA binding; IEA:EnsemblFungi.
DR GO; GO:0000433; P:carbon catabolite repression of transcription from RNA polymerase II promoter by glucose; IEA:EnsemblFungi.
DR GO; GO:0140673; P:co-transcriptional chromatin reassembly; IEA:EnsemblFungi.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0006334; P:nucleosome assembly; IEA:EnsemblFungi.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:EnsemblFungi.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IEA:EnsemblFungi.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0000414; P:regulation of histone H3-K36 methylation; IEA:EnsemblFungi.
DR GO; GO:0031440; P:regulation of mRNA 3'-end processing; IEA:EnsemblFungi.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:EnsemblFungi.
DR GO; GO:0001178; P:regulation of transcriptional start site selection at RNA polymerase II promoter; IEA:EnsemblFungi.
DR CDD; cd09928; SH2_Cterm_SPT6_like; 1.
DR CDD; cd09918; SH2_Nterm_SPT6_like; 1.
DR Gene3D; 1.10.10.2740; -; 1.
DR Gene3D; 1.10.10.650; -; 1.
DR Gene3D; 1.10.3500.10; -; 1.
DR Gene3D; 3.30.420.140; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
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; PTHR10145; 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; PF14639; YqgF; 1.
DR PIRSF; PIRSF036947; Spt6; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00732; YqgFc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; SH2 domain; Transcription;
KW Transcription regulation.
FT CHAIN 1..1449
FT /note="Transcription elongation factor SPT6"
FT /id="PRO_0000238572"
FT DOMAIN 1256..1353
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..49
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 1252..1254
FT /evidence="ECO:0007829|PDB:3GXW"
FT HELIX 1263..1270
FT /evidence="ECO:0007829|PDB:3PJP"
FT STRAND 1278..1282
FT /evidence="ECO:0007829|PDB:3PJP"
FT STRAND 1284..1287
FT /evidence="ECO:0007829|PDB:3GXX"
FT STRAND 1289..1297
FT /evidence="ECO:0007829|PDB:3PJP"
FT STRAND 1300..1310
FT /evidence="ECO:0007829|PDB:3PJP"
FT STRAND 1319..1323
FT /evidence="ECO:0007829|PDB:3PJP"
FT STRAND 1326..1330
FT /evidence="ECO:0007829|PDB:3PJP"
FT HELIX 1331..1337
FT /evidence="ECO:0007829|PDB:3PJP"
FT HELIX 1339..1350
FT /evidence="ECO:0007829|PDB:3PJP"
FT HELIX 1360..1373
FT /evidence="ECO:0007829|PDB:3PJP"
FT STRAND 1379..1384
FT /evidence="ECO:0007829|PDB:3PJP"
FT STRAND 1386..1388
FT /evidence="ECO:0007829|PDB:6QTC"
FT STRAND 1391..1399
FT /evidence="ECO:0007829|PDB:3PJP"
FT STRAND 1404..1411
FT /evidence="ECO:0007829|PDB:3PJP"
FT STRAND 1413..1418
FT /evidence="ECO:0007829|PDB:3PJP"
FT STRAND 1421..1425
FT /evidence="ECO:0007829|PDB:3PJP"
FT HELIX 1426..1436
FT /evidence="ECO:0007829|PDB:3PJP"
FT HELIX 1440..1442
FT /evidence="ECO:0007829|PDB:3PJP"
SQ SEQUENCE 1449 AA; 168864 MW; 47C7AB8A854F3AB6 CRC64;
MSDQESASLR EEKNEIINGM GSGAPSDEEE GEDVFDSSEE EEEDDEDEAR KISEGFIVND
EDEDEDEDDE NVADKKKKRR HKRRAREEED DRLSEDDLDL LMENAGVKRP TTEGSSGGKL
KRLKRVGDEV ESGAADREQE SSQEKESSRL NDFFSDDEDE EPYDEENRER SRGSREYDRG
ESNHQGDNRK SGMLDELDDF IEEDEFSDED EETRQQRLLE RKMMREQRMK APTKITGLSS
DKIDEMYDVF GDGHDYDWAL EIENEELEGG DINEQSEEFD EETGMTKSSK KKISLQDIYD
LQDLKKNLMT DEDMLIRKTD IPERYQELRS GLVNHGNLSD NDQELEKNWI SEKIAVDKNF
SADYDLTEFK EAVGNAIKFI TKENLEVPFI YAYRRNYISS RERDGFLLTE DDLWEIVHLD
IEFQSIINKR DYVKRFYSEL GISDPLVDEY FKNQSTGSVA ELNSLQDIYN YLEFKYAQEI
NDNLQKESDK SGKKHLKNSN YEKFKSSALY KVIEAVGVSA DQIGNNISSQ HQIHIPKDHE
ALKPLELIEL VLNENAGDLQ VFLSNIKLAM DTIQKYYSWE ISKNTKVREK VRADFYRYYL
VDVVLTTKGK REIQRGSLYE DIKYAINRTP LHFRREPEIF LKMLEAESLN LMTLKLHMSS
QKQYVDHLFQ IALETTNTSD LAIEWNNFRK AAFTQAIEKI FNDIAQEIKD DLEKTCQKLV
CKVVRHKFMT KLDQAPYVPD LKDPKLPKIL TLTCGQGRFG SDAIIAAYVN RKGEFVRDFK
ITENPFDRSN PDKFEEVFED IVQTCQITAI GINGPNPKTQ KLFKKLIEVI HKKNLVDSKG
THIPIIYVED EIAIRYQNSE RAAQEFPNKP PYVKYCIALA RYMHSPLMEY ANLSPEELKS
LSIHPFQSFL SPEYLNRAIE TAFVDIVNLV GVEVNKATDN SYYASVLRFV SGFGKRKAID
FLESLQRLNE PLLARQQLIT HNILHKVIFM NSAGFLYISW SKKRQRYEDL EHDQLDSTRI
HPEDYHLATK VAADALEYDP DTIAEKEENG TMSEFIEFLR EDPNRRSKLE SLNLESYAEE
LEKNTGQRKL NNLNTIVLEL LDGFEELRND FHIMQSEEVF SSLTGETDKT LFKGCVIPVR
VERFWHNDIV CVTNSEVECI VNAQRHLGAQ VRRPPNEIYE LNKTYPAKVI FIDYPNITAE
VSLLEHDVKN EYNPLTYSKD PAIWDLKQEL EDSEEEKKVT MAESRAKRTH RVINHPYYFP
FNGKQAEDYL RSKERGDFVI RQSSRGDDHL AITWKLDKDL FQHVDIQELE KENPLALGKV
LVVEGQRYHD LDQIIVEYLQ NKIRLLNELT SNEKFKAGTK KEVVKFIEDY SKVNPKKSVY
YFSLNYENPG WFYLIFKLNA ESKLYIWNVK LTHTGFFLVN YNYPTVIQLC NGFKTLLKSS
NTRNRSGYR
