LEO1_DICDI
ID LEO1_DICDI Reviewed; 487 AA.
AC Q54MB8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=RNA polymerase-associated protein LEO1;
GN Name=leo1; ORFNames=DDB_G0286051;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: The PAF1 complex is a multifunctional complex. May be
CC involved in both initiation and elongation, histone methylation and RNA
CC processing.
CC -!- SUBUNIT: Component of the PAF1 complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LEO1 family. {ECO:0000305}.
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DR EMBL; AAFI02000085; EAL64404.1; -; Genomic_DNA.
DR RefSeq; XP_637916.1; XM_632824.1.
DR AlphaFoldDB; Q54MB8; -.
DR SMR; Q54MB8; -.
DR STRING; 44689.DDB0267056; -.
DR PaxDb; Q54MB8; -.
DR PRIDE; Q54MB8; -.
DR EnsemblProtists; EAL64404; EAL64404; DDB_G0286051.
DR GeneID; 8625427; -.
DR KEGG; ddi:DDB_G0286051; -.
DR dictyBase; DDB_G0286051; leo1.
DR eggNOG; KOG2428; Eukaryota.
DR HOGENOM; CLU_560727_0_0_1; -.
DR InParanoid; Q54MB8; -.
DR OMA; DNDQRES; -.
DR Reactome; R-DDI-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DDI-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q54MB8; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990269; F:RNA polymerase II C-terminal domain phosphoserine binding; IBA:GO_Central.
DR GO; GO:0016570; P:histone modification; IEA:InterPro.
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; IEA:InterPro.
DR InterPro; IPR007149; Leo1.
DR PANTHER; PTHR23146; PTHR23146; 1.
DR Pfam; PF04004; Leo1; 1.
PE 3: Inferred from homology;
KW Activator; Coiled coil; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..487
FT /note="RNA polymerase-associated protein LEO1"
FT /id="PRO_0000328894"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 331..357
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..76
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..427
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 56191 MW; FD2549E734F30850 CRC64;
MNDFGEEDER QILEGTFVDK SSKQTTNDNE NNNNNNNREE ENENQDKNVT TKNDEDNNND
ANDGDDDDDD LFGDKDLEEN DNVNSDNEKN KSKKDKEDQD QEEQQEDQED EEYSNKKKKK
KSKKNKNRHS TEEDETMEDA NENLDFATGA GEEEEEEEPE LIRDPITLTH IETSNVLPAQ
KIMKLKLLNI LGIQPKPFDP ITFEDEEAMN GDEKSKFNVE SVIRWRWGLD LNGRPAKESN
TRLVTWSDGS SHLYIGNEVL EIKEQPLQNE QFYVYSSQDG FIECEGKIDS RLSIRPTNIK
SKVHQRLSEN VAKRTVKVSK IKSIHTTLDP EKEKEKREKE LLDALREKKK QKDDSYRPNR
GRGGKSGSLT ASYLENDDDD YDSYRNEKGD DFVVDDDEDE EDDDYKESDD DGSDSSDDDG
SESGESESDS DGDNKSKKKE NKNSNDNKNN KSRKQDFDDD EDEDEDLIVS TKKVKRRVID
DDDDDED
