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SPT6_ASPFU
ID   SPT6_ASPFU              Reviewed;        1420 AA.
AC   Q4WWH6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Transcription elongation factor spt6;
DE   AltName: Full=Chromatin elongation factor spt6;
GN   Name=spt6; ORFNames=AFUA_3G05890;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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; AAHF01000002; EAL92977.1; -; Genomic_DNA.
DR   RefSeq; XP_755015.1; XM_749922.1.
DR   AlphaFoldDB; Q4WWH6; -.
DR   SMR; Q4WWH6; -.
DR   STRING; 746128.CADAFUBP00004232; -.
DR   PRIDE; Q4WWH6; -.
DR   EnsemblFungi; EAL92977; EAL92977; AFUA_3G05890.
DR   GeneID; 3512651; -.
DR   KEGG; afm:AFUA_3G05890; -.
DR   VEuPathDB; FungiDB:Afu3g05890; -.
DR   eggNOG; KOG1856; Eukaryota.
DR   HOGENOM; CLU_001680_0_1_1; -.
DR   InParanoid; Q4WWH6; -.
DR   OMA; LCNGFKT; -.
DR   OrthoDB; 56990at2759; -.
DR   Proteomes; UP000002530; Chromosome 3.
DR   GO; GO:0000791; C:euchromatin; IEA:EnsemblFungi.
DR   GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR   GO; GO:0008023; C:transcription elongation factor complex; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0031491; F:nucleosome binding; IBA:GO_Central.
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; IBA:GO_Central.
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:0034728; P:nucleosome organization; IBA:GO_Central.
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; IBA:GO_Central.
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   GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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; IPR041692; HHH_9.
DR   InterPro; IPR012340; NA-bd_OB-fold.
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; IPR037027; YqgF/RNaseH-like_dom_sf.
DR   PANTHER; PTHR10145; PTHR10145; 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; PF14639; YqgF; 1.
DR   PIRSF; PIRSF036947; Spt6; 1.
DR   SUPFAM; SSF47781; SSF47781; 2.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; SH2 domain; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1420
FT                   /note="Transcription elongation factor spt6"
FT                   /id="PRO_0000238569"
FT   DOMAIN          1230..1330
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1186..1208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..30
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1187..1208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1420 AA;  163634 MW;  52E823BDD8C3E24A CRC64;
     MSARDFVEGE AVLDDEENEN EEEQEEDYDG EVHEGAGTMN HYNDSSEEEE EDDDDEEAAR
     AIREGFIVDE DEEIEERAER RREKRKRRRE EREREDEHLD EEDLELIGEL NPAFQSAAAT
     ESKFKRLKRG HKDHRQASQG IDDIFNSDED EEAAGDYGRP SHRRPMHDEM KDFIEEDVFT
     DDELERERED LEIARPAKRG VTGLGATDAA GLDENALEDM RAAFGDGNEY LFALEMEEQE
     EEQEEDQEKH LDLKDVFEPS QLAERMLTEE DNQIRLLDEP ERHQLARKPY RNLVLTEEQF
     REEAAWIANL MLLKKRIEPE LREPFQRSVA KVLEFLVTDD WEVPFIFQHR KDYMIHATKV
     PVAGAPADGD TSQYTIKAEK LLNMTDLWDI FDHDLKFRAL VEKRNTIQKT YDNLQSLFNV
     NDSVVQDMLS TAVTMEELQD VQDYVHFQYA SQLRDINLMN GEANGDTHRR KATGRSFFER
     VRNGKAYGLV RAFGITADAF AQNALKEGRR QYTEDPAERP EEMADSFIDN DFSNASHVLK
     AAKALFAEEI VMSPKMRKVI RQAYYMNGAV DCFRTEKGLR RIDEQHPYYE FKYLRNQQLS
     DIARQPELYL RMLKAEEEGL VEVKVRFENF DHFRQRLYPD IESDNYSEIA DAWNRTRREV
     LDMALGKLER LINRSVKENI RQECENHVAK ECREAFSQRL DQAPYKPKGM VLGTVPRVLA
     MSTGTGIVGR DPIHWAYVEE DGRVLENGKF VDLSIGDRDR SIPDGKDVEA LIELLERRRP
     DVIGVSGMSP ETRKLYKLLT ELVEKKDLRG ATYTDERDEE ISDPLEVVIV NDEVARLYQH
     SERAKKDHPS FGPLTHYCVA LAKYLQSPLK EYASLGRDIV SIQFKRGQQL VAQELLLKQL
     ETALVDMVNL VGVDINEAVT DPATANLLPY VCGLGPRKAA HLLKIVNMNG GVVNNRVELL
     GVNAQYPAMG VKVWNNCASF LFIDFENADP DADPLDNTRV HPEDYDIARK MAADALELDE
     EDIKAETDEN GPGAIVRKLF RDEAQDRVND LILEEYAEQL EKNLNQRKRA TLETIRAELQ
     QPYEELRKQF ALLSTDDVFT MLTGETSDTL AEGMVVPISI KRITDDHIDG KLDCGVDVLV
     PESELTDRYD IPVRALYSLH QTLPAKVLFL NKKNFLCNVS LREEQVSRPT PRPRDHMRGE
     WDDRQEAKDR EMLQEKTQSG GRVMRVIKHP LFRPFNSTQA EEFLGSQSRG DVVIRPSSKG
     PDHLAVTWKV ADGIFQHIDV LELDKENEFS VGRTLKVGGR YTYSDLDDLI FNHVKAMAKK
     VDEMMLHEKY QEGSKDATYS WLNTYTKANP RRSAYAFCID PKHPGYFQLC FKAGENAQLH
     SWPVKVIPQG YELQRNPYPD MRALCNGFKL LFTNMQAGKR
 
 
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