ID J3KH82_COCIM Unreviewed; 1425 AA.
AC J3KH82;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Transcription elongation factor Spt6 {ECO:0000256|PIRNR:PIRNR036947};
GN ORFNames=CIMG_00540 {ECO:0000313|EMBL:EAS35186.3};
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410 {ECO:0000313|EMBL:EAS35186.3, ECO:0000313|Proteomes:UP000001261};
RN [1] {ECO:0000313|Proteomes:UP000001261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2] {ECO:0000313|Proteomes:UP000001261}
RP GENOME REANNOTATION.
RC STRAIN=RS {ECO:0000313|Proteomes:UP000001261};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; GG704911; EAS35186.3; -; Genomic_DNA.
DR RefSeq; XP_001246769.1; XM_001246768.2.
DR STRING; 246410.J3KH82; -.
DR GeneID; 4566614; -.
DR KEGG; cim:CIMG_00540; -.
DR VEuPathDB; FungiDB:CIMG_00540; -.
DR InParanoid; J3KH82; -.
DR OMA; LCNGFKT; -.
DR OrthoDB; 170310at2759; -.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR003029; S1_domain.
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; 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; SM00316; S1; 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.
PE 3: Inferred from homology;
KW Elongation factor {ECO:0000313|EMBL:EAS35186.3};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036947};
KW Protein biosynthesis {ECO:0000313|EMBL:EAS35186.3};
KW Reference proteome {ECO:0000313|Proteomes:UP000001261};
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 1113..1184
FT /note="S1 motif"
FT /evidence="ECO:0000259|SMART:SM00316"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1425 AA; 164119 MW; F08281B4AFBD107B CRC64;
MSAAELLENE ALLDDEENDE DYDEETGEVA RGTADRNGHY DDSSEEEEDE DEDAARAVRE
GFIVDEDEEE EERSERRREK KKRRREERAL EDEDLDEEDI YLIGENNPDF EPPVSYESKF
KRLKRGHKGD RDRAVSQGIN DIFNSDEEED EVDRYRMGAR DRRGLHDDLD DFIEEDVFSD
EERERMREDE EIARPVKKGI SGLAVTEATG LDEAALEDMR AAFGDGTDYL FALEMEEDED
EEERGDEEKP LDLKDVFEPS QLAEKMMTEE DNEIRFTDEP ERYQIARKPY KHVILSEEQF
KEEAIWISNL MLLKKRLEPD LREPFQRAIV KVLEFMVTDD WEVPFIFQHR KDYLIHAAKV
PMSPSAPNPD GQDYVIRAEK LLNMTDLWDI FEYDLKFRAL VDKRNILQRT YDNLKNVANV
KDEVFEQMLP AVVTMEELQD LQDYIYFEYS SELKDVAMVN GNGENGAVHQ RRKAATKTFY
ERIRNSKAYG LVRAFGITPD GFAQNAMKEA KRHHIDDPTE LPEDMADGLL DTHFANGLHA
LKAAKTMFAE QLIMSPKVRK ELRRAFYMNG VIDCFRTEKG LKKIDEHHPY YEFKYLRNQQ
LSDIARRPEL FLRMLKAEEE GLVDVNVRFQ NFDNYKKRLY RDIQSDNFSE VADAWNKARK
EVLDMALARL DKIMSRGVKE NIKTECENHV AKECREAFSL RLDQAPYKPK GMILGTIPRV
LTLSAGAGII GKDPIYWAWV EEDGRVLENG KFTDLTLGDP DRMISDGRDV NSLIDLVERR
KPDVIGISGM SPETRKLYKQ LAELIDAKNL RSSPYTNDND DEVSDPLEVV IVNDEVARLY
HTSDKARSEH PGLHPLTIYC VSLAKYLQNP MKEYASLGRD IVSIQFKPGQ QLISQEKLLK
QLESALVDMV NLCGVDINEA VNDPATANLL TYVSGLGPRK ASQLLKIINM NGGVVNNRME
LLGVNAQYPA MGVKVWNNCA SFLYIDYDTA DPDTDYLDNT RVHPEDYDIG RKMAADALEL
DEEDIKAETD ENGPGAIVRK LVKEDAQEKV NDLILEEYAE QLEKNLNQRK RATLETIRAE
LQQPYEELRK QFVFLSTDAI FTMFTGETAD TLAEGMVVPV TIKRITDDHI DGKLDCGVDV
LIPEMELTDR YDIPVRSLYS IHQTVPAKLL YLNRKAFIAN ASLREDQVIR PYRREFDHMR
DEWDDKQEHQ DQEAMKEETK TSTRTLRVIK HPLFRPFNGP QAEEFLASQS RGDAVIRPSS
KGPDHLAVTW KVSDGVYQHI DVLELDKENE FSVGKILKIG GKYSYSDLDE LIVNHVKAMA
RKVDDMTIHE KYQSGSKEAT ERWLTTYTTA NPTRSAYAFC IDPKHPGYFH LCFKAGQNAS
MNSWPVKVIP QGYELQRNPY PDMMALCNGF KTMYANVLAG KKGRR
//
