BRE1_DICDI
ID BRE1_DICDI Reviewed; 1080 AA.
AC Q86KL1; Q555K8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Probable E3 ubiquitin-protein ligase bre1;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase bre1 {ECO:0000305};
GN Name=bre1; ORFNames=DDB_G0274241;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of histone H2B. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
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DR EMBL; AAFI02000012; EAL70013.1; -; Genomic_DNA.
DR RefSeq; XP_644058.1; XM_638966.1.
DR AlphaFoldDB; Q86KL1; -.
DR SMR; Q86KL1; -.
DR STRING; 44689.DDB0237665; -.
DR PaxDb; Q86KL1; -.
DR EnsemblProtists; EAL70013; EAL70013; DDB_G0274241.
DR GeneID; 8619487; -.
DR KEGG; ddi:DDB_G0274241; -.
DR dictyBase; DDB_G0274241; bre1.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_286274_0_0_1; -.
DR InParanoid; Q86KL1; -.
DR OMA; DENTSCT; -.
DR Reactome; R-DDI-9013422; RHOBTB1 GTPase cycle.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q86KL1; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IBA:GO_Central.
DR GO; GO:0010390; P:histone monoubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR013956; E3_ubiquit_lig_Bre1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR23163; PTHR23163; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1080
FT /note="Probable E3 ubiquitin-protein ligase bre1"
FT /id="PRO_0000327669"
FT ZN_FING 1028..1067
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 50..91
FT /evidence="ECO:0000255"
FT COILED 149..169
FT /evidence="ECO:0000255"
FT COILED 196..269
FT /evidence="ECO:0000255"
FT COILED 331..1003
FT /evidence="ECO:0000255"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1080 AA; 126556 MW; 432C39D84C26ED29 CRC64;
MSMDHQDLKR RDPPADSESQ RPSKKISLSS SEASVPIGGP PIDQNLILFQ NRAMKVRVEE
QKIEINDREQ KIKQLNTKIH QYKENISCLC RVWDQLNSGL DLLINRVDFE NAMDNLLPKD
NITESFEFLS SYITEPVTLD EKYTLDQSLQ KKVQKTQSTF SKISKALEKE HTLSKFVFRL
LKSKDGIKSN DIEKLLKEDN DKLSKQNQYI QNIYDKVQIQ FKQLTDQTTH LADQAAIYQQ
NNKELKLELE KSQDELTIER KRVIKLQDET LRTPQVKIPS PSLGSNIPGG ANNNNNNNNN
SNNNNNINNN GNNMGGSGSS SLASSTNGIN KQQSNDINGK ELTHEELIAE LQRQSDSRLL
EARKLREEKA ILLKELQQIQ IDIRVIPEER IQNSMPYQVL RQRYQLVSDE LDIHRNQCTK
LQNDLAQATI GRRLEREALE AFEAHRRQNI ERRVSQLEVE SIELKGEKEK LVCLIEQRNP
NVPSLQYIQE SRLLLDKKDD EIKQLRKEIE QLKLDIEKYK APKEEIERYK LLVQRDVESK
NIEINKLLEK INTITKQNND LKSNEQQLLQ KESELTLSLN ILKSNKNNIN INNLDKDNIE
DNSKIKQQQE QQQQQHQKID NNNKKEEEIK KEQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQQQQQE EQKKDKEMID IEKSTENIIN NNNNNNTNEQ KLNEINKNIE
NGNNENNNNN ENTINNENTI NNNNNENKDK IIFNLELNES KLKLELSTVK KQLEDITKSK
EEYDNEIKEI NEKFKAQIKE LDITISQNKI QQESQKQELE ALVMEIDSMG KAYEQMLEQN
TRLTKQLSDK EDTHAHLMAE NIKSQQTIRN SKEIQLAIEE KLNRNEEKLK SQGELMQKIE
EKSNILQKQL SKVTEDLHSC SFDLEKHKRF VRENNAHSLE LKTQLDHLSN LNAELKKKAD
DSIFALEREI DKAKRLDEEK QLLKKKLEKA TSANNNNNNN NNNNNNNNNN NSSSSEEELK
LINQRLRCTI CNDRQKNYVI AKCFHVFCKE CIYSNIDTRK RRCPSCNRAF AETDVHQIYY
