ID   SPT6H_CAEEL             Reviewed;        1521 AA.
AC   P34703; Q7JMP9;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Suppressor of Ty 6 homolog;
DE   AltName: Full=Abnormal embryogenesis protein 5;
GN   Name=emb-5; ORFNames=T04A8.14;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ALA-859.
RC   STRAIN=Bristol N2;
RX   PubMed=8391108; DOI=10.1007/bf00276929;
RA   Nishiwaki K., Sano T., Miwa J.;
RT   "emb-5, a gene required for the correct timing of gut precursor cell
RT   division during gastrulation in Caenorhabditis elegans, encodes a protein
RT   similar to the yeast nuclear protein SPT6.";
RL   Mol. Gen. Genet. 239:313-322(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH GLP-1 AND LIN-12.
RX   PubMed=8658178; DOI=10.1126/science.273.5271.112;
RA   Hubbard E.J.A., Dong Q., Greenwald I.;
RT   "Evidence for physical and functional association between EMB-5 and LIN-12
RT   in Caenorhabditis elegans.";
RL   Science 273:112-115(1996).
CC   -!- FUNCTION: May regulate transcriptional elongation by RNA polymerase II.
CC       Required for several aspects of morphogenesis of C.elegans, including
CC       regulation of division in the germline and gut and specification of
CC       ventral-uterine precursor cell fate. {ECO:0000269|PubMed:8658178}.
CC   -!- SUBUNIT: Interacts with glp-1 and lin-12. {ECO:0000269|PubMed:8658178}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Abundant in embryos, and less abundant in larvae.
CC   -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000305}.
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DR   EMBL; D14635; BAA03484.1; -; Genomic_DNA.
DR   EMBL; Z35663; CAA84737.1; -; Genomic_DNA.
DR   EMBL; Z35719; CAA84737.1; JOINED; Genomic_DNA.
DR   PIR; S35241; S35241.
DR   RefSeq; NP_497969.1; NM_065568.3.
DR   AlphaFoldDB; P34703; -.
DR   SMR; P34703; -.
DR   BioGRID; 40856; 23.
DR   STRING; 6239.T04A8.14; -.
DR   iPTMnet; P34703; -.
DR   EPD; P34703; -.
DR   PaxDb; P34703; -.
DR   PeptideAtlas; P34703; -.
DR   PRIDE; P34703; -.
DR   EnsemblMetazoa; T04A8.14.1; T04A8.14.1; WBGene00001259.
DR   GeneID; 175621; -.
DR   KEGG; cel:CELE_T04A8.14; -.
DR   UCSC; T04A8.14; c. elegans.
DR   CTD; 175621; -.
DR   WormBase; T04A8.14; CE13120; WBGene00001259; emb-5.
DR   eggNOG; KOG1856; Eukaryota.
DR   GeneTree; ENSGT00510000047446; -.
DR   HOGENOM; CLU_001680_4_0_1; -.
DR   InParanoid; P34703; -.
DR   OMA; LCNGFKT; -.
DR   OrthoDB; 56990at2759; -.
DR   PhylomeDB; P34703; -.
DR   Reactome; R-CEL-112382; Formation of RNA Pol II elongation complex.
DR   Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-CEL-75955; RNA Polymerase II Transcription Elongation.
DR   SignaLink; P34703; -.
DR   PRO; PR:P34703; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00001259; Expressed in germ line (C elegans) and 4 other tissues.
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:0042789; P:mRNA transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR   GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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; 2.40.50.140; -; 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; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
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; PF17674; HHH_9; 1.
DR   Pfam; PF14641; HTH_44; 1.
DR   Pfam; PF00575; S1; 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; SM00316; S1; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00732; YqgFc; 1.
DR   SUPFAM; SSF47781; SSF47781; 2.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50126; S1; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..1521
FT                   /note="Suppressor of Ty 6 homolog"
FT                   /id="PRO_0000072169"
FT   DOMAIN          1183..1252
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   DOMAIN          1300..1389
FT                   /note="SH2"
FT   REGION          1..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           26..42
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        12..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..236
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         859
FT                   /note="A->E: In HC61; temperature-sensitive."
FT                   /evidence="ECO:0000269|PubMed:8391108"
SQ   SEQUENCE   1521 AA;  175816 MW;  97855CAC28EE08F7 CRC64;
     MDFIDNQAEE SDASSGHSDD EEPQSKKMKM AKEKSKRKKK MVASSDEDED DDDDEEENRK
     EMQGFIADDD DEEEDAKSEK SEKSRHSGED ELDDEDLDLI NENYDIRETK KQNRVQLGDS
     SDEDEPIRRP NHEDDDLLSE RGSDDGDRRK DRGRGDRGGY GSESERSEDD FIEDDGDAPR
     RHRKRHRGDE NLPEGAEDDA RDVFGVEDFN LDEFYDDDDG EDGLEDEEEE IIEDDGEGGE
     IKIRRKKDTT KKSTLLESIE PSEIDRGFLL PGDKKIAKED LPERFQLRRT PVTEADDDEL
     ESEALWIIKY AFEEGTVTNQ ADLDQDDKLD CIMNLDPSVY EDRKKAVIKS IKKVLQFIRV
     RSNSFEPTFI GFYRKEDIDN LLTMNNLWRV YDFDEKWCHL SEKKNKIYDL MRRMREYQEL
     SDDLTAKRRP ISDADLMDTK YAETLEQLTD IHANFQLLYG ALLDDMIRWE KGRLTGEEEE
     QEYRVKFKSS IRNDKYQMCV ENGIGELAGR FGLTAKQFSE NLNWKKHDIE QDPMLPLEAA
     EEYVCPAFSD SDMVLNGAKF MLAKEISRQP QVRHSVRQEF RQSAHFWIKP TKKGRDTIDQ
     THPLYDKRYI KSKPVRSLTA EEFLFYHKAK EDGLVDVLIM YESEEDQDSN NYLVNKYLSD
     SIFQKDEYTE NVEQWNSVRD ECVNMAITEM LVPYMRDELY NTILEEAKTA VAKKCRKEFA
     SRISRSGYLP DFDNNDDDDD GMDQHGARRI MAVCYPTERD EASFGVMVDE NGAIVDYLRM
     VHFTKRTFGG GNNGLRKAES MDLFKKFVQR RKPHAIGLNI EDMECTRLKR DLEEAVADLF
     SQNLIYKPIP VFLMDNEAAK VYMRSNVSLA ENPDHPPTLR QALSLARLLL DPIPEYAHLW
     NIDEDIFCLS LHPLQRDIDQ EQLALVLSHE LVNKVNEEGV DINKCAEFPH YTNMLQFTCG
     LGPRKATDLL KSIKANDNLI ESRSKLVVGC KLGPKVFMNC AGFIKIDTIK VSEKTDAYVE
     VLDGSRVHPE TYEWARKMAV DALEVDDSAD PTAALQEIME SPDRLRDLDL DAFADELSRQ
     GFGEKKSTLY DISSELSARY KDLRQPFQEP TGELLYDLLA RSGKEIREGA KVLGTVQSVQ
     YRKVDKDAAD SMLPDVGEDG LFTCPCCKSF TSSAPGGIQE HMLGDSRQGG CPGTPVGIRV
     RFDNGMTGFC PNKNISSSHV DNPLTRVKIN QPYYFKVLKL DKERFSLFLS CKSSDLKEDD
     LSQRDQYWDE HQYQADLELM KSESKKKTEA NTRVKRVIAH PNFHNVSYEA ATKMLDEMDW
     SECIIRPSAN KDSGLSVTWK ICDRVYHNFF VKESAKDQVF SIGRQLSVGG EDFEDLDELI
     ARFVQPMIQI SHEITTHKYF FPNGTCEETE AVEQFVREKK RELGRSPYVF SASYRQPCQF
     CISYMFDNTE RIRHEYFKIV PHGVRFRHQN FDTLDRMMAW FKRHFHEPPI ELRRSAIPAP
     QYRVGAPPAA PYYPPQFVGY H