ID EAF_DROWI Reviewed; 539 AA.
AC B4MR74;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Ell-associated factor Eaf {ECO:0000250|UniProtKB:Q7JRJ1};
GN Name=Eaf {ECO:0000250|UniProtKB:Q7JRJ1}; ORFNames=GK22015;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1] {ECO:0000312|EMBL:EDW74613.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW74613.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Promotes transcriptional elongation by Su(Tpl)/ELL. Essential
CC for development (By similarity). {ECO:0000250|UniProtKB:Q7JRJ1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96JC9}.
CC -!- SIMILARITY: Belongs to the EAF family. {ECO:0000255}.
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DR EMBL; CH963849; EDW74613.1; -; Genomic_DNA.
DR RefSeq; XP_002063627.2; XM_002063591.2.
DR AlphaFoldDB; B4MR74; -.
DR SMR; B4MR74; -.
DR STRING; 7260.B4MR74; -.
DR eggNOG; KOG4795; Eukaryota.
DR HOGENOM; CLU_025755_2_1_1; -.
DR OMA; SSHMGKQ; -.
DR OrthoDB; 318263at2759; -.
DR PhylomeDB; B4MR74; -.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0032783; C:super elongation complex; IEA:EnsemblMetazoa.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR InterPro; IPR027093; EAF_fam.
DR InterPro; IPR019194; Tscrpt_elong_fac_Eaf_N.
DR PANTHER; PTHR15970; ELL-ASSOCIATED FACTOR EAF; 1.
DR PANTHER; PTHR15970:SF2; ELL-ASSOCIATED FACTOR EAF; 1.
DR Pfam; PF09816; EAF; 1.
PE 3: Inferred from homology;
KW Activator; Developmental protein; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..539
FT /note="Ell-associated factor Eaf"
FT /id="PRO_0000386606"
FT REGION 119..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7JRJ1"
SQ SEQUENCE 539 AA; 59127 MW; 23B6622A63C4FC1D CRC64;
MMMTKQKNTL ADRLNIGGEV RELRLGATFN PKNSSTAFHT IKYDFKPASV DPNRMAAVDV
GSNNQVTVTV PNLENSGVPH TVYKGNQRKY AKECLMIYDK ETGAITLEKL NHNIQVKKTR
SEMTHHKPSF LPATNINHNN IPMSTNGSGP GPGPGPGSGP SPPLSGSASG SGQKLENSTM
RISSKTKVST GSRRNNIIDF KPRNSPMQQS SPSRPVASHR SPQSAPAWNA NNAQQTLPSI
PMIMDDDDFG LGAALHNGTG GGQANISGSS TGSSTGQPDY GGGGSSSSST MHRQRQVPQH
GQHGKRQQMH QNHQQHPSPP MHQQQQQQQQ QQHYGRGINN GGGSNNYAQQ QQPQQHHQQQ
EQQRPSSSST YSHHSNNMPM DLDFPRENDL TSQTMAQAGA AIEEQIGGVL SASSSSSESD
SSDSDSGSES DDSTDDESRP MQQQQLPNLG LGSISPSYNN HQQLQQQPPQ QQQQQQQQQQ
YNHHMQQQHQ PQQQHHHHHQ QQQQQQQQSD MYTSNRGFPN DLLQNDLQLS SNSSDDDDD
//
