SPT6H_CAEBR
ID SPT6H_CAEBR Reviewed; 1521 AA.
AC Q93148; A8XSS8; Q60Z16;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Suppressor of Ty 6 homolog;
DE AltName: Full=Abnormal embryogenesis protein 5;
GN Name=emb-5; ORFNames=CBG18001;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Higashi K., Sano T., Miwa J.;
RT "An EMB-5 homolog of Caenorhabditis briggsae is essentially identical to
RT EMB-5 of Caenorhabditis elegans.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: May regulate transcriptional elongation by RNA polymerase II.
CC May be required for several aspects of morphogenesis of C.briggsae,
CC including regulation of division in the germline and gut and
CC specification of ventral-uterine precursor cell fate (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with glp-1 and lin-12. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SPT6 family. {ECO:0000305}.
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DR EMBL; D88767; BAA13699.1; -; mRNA.
DR EMBL; HE600963; CAP35530.1; -; Genomic_DNA.
DR RefSeq; XP_002642063.1; XM_002642017.1.
DR AlphaFoldDB; Q93148; -.
DR SMR; Q93148; -.
DR STRING; 6238.CBG18001; -.
DR GeneID; 8584057; -.
DR KEGG; cbr:CBG_18001; -.
DR CTD; 8584057; -.
DR WormBase; CBG18001; CBP10840; WBGene00037500; Cbr-emb-5.
DR eggNOG; KOG1856; Eukaryota.
DR HOGENOM; CLU_001680_4_0_1; -.
DR InParanoid; Q93148; -.
DR OrthoDB; 56990at2759; -.
DR Proteomes; UP000008549; Chromosome III.
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; 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; 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 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1521
FT /note="Suppressor of Ty 6 homolog"
FT /id="PRO_0000072168"
FT DOMAIN 1182..1251
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 1299..1388
FT /note="SH2"
FT REGION 1..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1521
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 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 16
FT /note="G -> D (in Ref. 2; CAP35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="R -> P (in Ref. 1; BAA13699)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="A -> G (in Ref. 1; BAA13699)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="R -> G (in Ref. 1; BAA13699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1521 AA; 176036 MW; AF16D6EB689EDD2B CRC64;
MDFIDNQAEE SDASTGRSDD DEPQSKKMKM AKDKLKKKKK VVASSDEDED DEDDEEEGRK
EMQGFIADED DEEEDARSEK SDRSRRSEIN DELDDEDLDL IDENLDRQGE RKKNRVRLGD
SSDEDEPIRR SNQDDDDLQS ERGSDDGDKR RGHGGRGGGG YDSDSDRSED DFIEDDGDAP
RRHRKRHRGD EHIPEGAEDD ARDVFGVEDF NFDEFYDDDD GEEGLEDEEE EIIEDDGEGG
EIKIRRKRDT TKKTTLLESI EPSELERGFL SAADKKIMIE DAPERFQLRR TPVTEADDDE
LEREAQWIMK FAFEETTVTN QAAVDADGKL ECLMNIDSSE IEDKRRAVVN AIKAVLHFIR
VRSNSFEVPF IGFYRKESID NLLTMNNLWI VYDYDEKYCH LSEKKRRLYD LMRRMREYQE
LSDDITAKRR PINEMDLIDI NFAETLEQLT DIHANFQLLY GSLLEDMTKW EKERRAADGE
ETEYRAKFKS SIRNDKYQMC VENGIGELAG RFGLTAKQFA ENLDWRKHDI DQDSAFPLEA
AEEYICPAFI DRETVLNGAK FMLAKEISRQ PLVRSRVRQE FRDNAHFWVK PTKKGRDTID
ETHPLFNKRY IKNKPIRNLT DEEFLYYHKA KQDGLIDMVL MYESDEDQAA NQFLVKKFLS
DSIFRKDEYT DNVEQWNAVR DQCVNMAITE MLVPYMKEEV YNTILEEAKM AVAKKCKKEF
ASRIARSGYV PEKEKLDEED EEHSARRRMM AICYSPVRDE ASFGVMVDEN GAIVDYLRMV
HFTKRGHGGG NTGALKEESM ELFKKFVQRR RPHAIALNIE DMECTRLKRD LEEAVAELYS
QSKIFSQINV YLMDNELAKV YMRSNISIAE NPDHPPTLRQ AVSLARQLLD PIPEYAHLWN
SDEDIFCLSL HPLQRDIDQE ILAQLLNHEL VNRVNEEGVD INKCAEFPHY TNMLQFTCGL
GPRKATSLLK SIKANDNLIE SRSKLVVGCK LGPKVFMNCA GFIRIDTRRV SDKTDAYVEV
LDGSRVHPET YEWARKMAVD ALEVDDSADP TAALQEIMET PERLRDLDLD AFADELNRQG
FGEKKATLYD ISSELSERYK DLRAPFVEPS GEALYDLLTR SGKEVKVGCK MLGTVQSVQY
RKVERDTIDS MIPEHTEEDQ YICPSCKIFT AADPQSVREH LLNAGRPGGC VGSACGIRVR
LDNGMTAFCP NKFISSSHVD NPLTRVKLNQ PYWFKVMAIN KEKFSILLSC KSSDLKEDAP
AERDDFWDQQ QYDDDVAAMK KETTKKKDAD TRVKRVIAHP NFHNVSYEAA TKMLDEMDWS
DCIIRPSANK ESGLSVTWKI CDRIYHNFFV KESAKDQVFS IGRTLSVGGE DFEDLDELIA
RFVLPMIQIS HEITTHKYFF TQGTSEDTDQ VETFVHEKRR ELGRSPYVFS ASYRQPCQFC
ISYMFDNSNR IRHEHFKISP RGIRFRQQNF DSLDRMMAWF KRHFNEPPPG IRSSLSYRPT
GRTGPPPSAP YQQPPQQQYY R
