ID A0A2H3CAL3_9AGAR Unreviewed; 1402 AA.
AC A0A2H3CAL3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Transcription elongation factor Spt6 {ECO:0000256|ARBA:ARBA00020248, ECO:0000256|PIRNR:PIRNR036947};
GN ORFNames=ARMSODRAFT_873256 {ECO:0000313|EMBL:PBK78364.1};
OS Armillaria solidipes.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Armillaria.
OX NCBI_TaxID=1076256 {ECO:0000313|EMBL:PBK78364.1, ECO:0000313|Proteomes:UP000218334};
RN [1] {ECO:0000313|Proteomes:UP000218334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=28-4 {ECO:0000313|Proteomes:UP000218334};
RX PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA Gueldener U., Muensterkoetter M., Nagy L.G.;
RT "Genome expansion and lineage-specific genetic innovations in the forest
RT pathogenic fungi Armillaria.";
RL Nat. Ecol. Evol. 1:1931-1941(2017).
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; KZ293415; PBK78364.1; -; Genomic_DNA.
DR STRING; 1076256.A0A2H3CAL3; -.
DR OrthoDB; 170310at2759; -.
DR Proteomes; UP000218334; 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; IPR041692; HHH_9.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR010994; RuvA_2-like.
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; 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:PBK78364.1};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036947};
KW Protein biosynthesis {ECO:0000313|EMBL:PBK78364.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218334};
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 1219..1310
FT /note="SH2"
FT /evidence="ECO:0000259|SMART:SM00252"
FT REGION 1..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..34
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..171
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1402 AA; 160551 MW; 65C8B722AC4CFDF1 CRC64;
MNSSEHGDDD EGEGDVIMPG ASDDSSEEDE DDPEEERKIK QGFIVDSDEE EEEKQRRKKR
RKRHHRPEEE EMLEDDDLDL LEENTGTSFK RNRLKRLVRH GSDSPPAASS SRRAVVESSD
DDLDDDDGLP RIQDIHKIWD DDRRGEEDDE DADGDMDDFI EYEDEDEGGA MDEQAREARR
KERKRQELER RKKAREIRPE LAGIDANAWE EIHDVFGDGH DYDWALAADD EYDYDEEQTK
PDIKYQDVFE PTDIRARMLT EDDDLIRAQD IPERMQLATS SISSNSSLSL HTPLTPDDIN
GAALWVSQRL SSRKTQEFFS PIGKHQELKG ALVLAVTFAL RQLFIEEYEV PYIWTHKRDH
ISHFDVNDVR ARFELLSLSE LWKIYSLGQK YRSLVERRNT LTAAYQRLQV GDKYFEEEVL
PQIDGIEVVA DATEWLNMKY KNKKPDEAFR FHDDEVTDTT KKHKMPSRVS IYEVTKKSIV
SRLAQGFGIQ PHEVVLNFVA MNHVHFIEDQ DLNPLAYAER FADPDPARAL PAEELLRQAR
MIIATELGKD PLLRNHIRQA FKEDGQVSVL PTERGKTKID EHHPYFNFKY LLNKPGREMM
WSSQFLHMIA AENAHLVTIS IFLPADAYSA FERRLNDAFA SDSFSESAKA WNEERARIVQ
EVLTQHLIPA GVKWMREYLR DEVEDFLAAG CAAGLGKRLD VAPYFTPKMS FGDTASVLAL
SWGKGDPQRD PISIVFMDEA GRMRESTKID NLFDQEQKDE FFDLIKRRKP DVIVIGGFTM
ATAKLSYRVK EILKHGTLIE ESEPEPDLDI PVIYIRDETA RIYQHSSRAA EEFNALSQTA
RYCVGMARYA QNPLNEYAAL GSDIAAVTFD EDDQHLVPRE KLLIALERTL VDVTNKVGVD
INRAAADSYY GLLLPFVCGL GPRKAQVLIQ KIASQGGNLV NRNQFIKGGL LTTKIFLNAA
GFLRIHQEPE SKSMRNRHDD DNAPDPLDDT RIHPEDYELA RKMATDALEL DEEDIHDEHP
SHVVTMIMRD PDNEKKLSEL NLDEFAVSLF NANQELKRHT LNVIREELLK PFAEQRNHWP
VLEPWDVLTM LSGENPRTLR VGLIVSVLVQ RVKTNIAHVR LDSGIEGIVQ PEFMMDNGGH
LLPNMAVPGV IIEVKLSLET DQFMVELSTR QSDVGGGDSA FRRVRPDEQW DHQQHDKDQE
VLARKKRAEG AKNRRVIKHP NFHNFNTAQA ENYLDKQQRG DVVIRPSSKG ANHLAVTWKV
DDKLYQHIDV TEPNADPTGQ TVGSQLIVDA SHRYADLDEL IVNHVQAMAR RVEELMAHDR
FKQGSEDDLH LFLKQQLAAN PAKSMYGFTL NRKRPGHFSL CFLANKQSNV QTWPVRVTPE
AYYLFEAAAV GVPELCDAFK VR
//
