BRE1_ASPFU
ID BRE1_ASPFU Reviewed; 725 AA.
AC Q4WDD7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=E3 ubiquitin-protein ligase bre1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q07457};
DE AltName: Full=RING-type E3 ubiquitin transferase bre1 {ECO:0000305};
GN Name=bre1; ORFNames=AFUA_6G04390;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates monoubiquitination
CC of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for
CC epigenetic transcriptional activation and is also a prerequisite for
CC H3K4me and H3K79me formation. {ECO:0000250|UniProtKB:Q07457}.
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:0000250|UniProtKB:Q07457};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q07457}.
CC -!- SIMILARITY: Belongs to the BRE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL85601.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AAHF01000012; EAL85601.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_747639.1; XM_742546.1.
DR AlphaFoldDB; Q4WDD7; -.
DR SMR; Q4WDD7; -.
DR STRING; 746128.CADAFUBP00009127; -.
DR PRIDE; Q4WDD7; -.
DR GeneID; 3505313; -.
DR KEGG; afm:AFUA_6G04390; -.
DR eggNOG; KOG0978; Eukaryota.
DR HOGENOM; CLU_019713_2_0_1; -.
DR InParanoid; Q4WDD7; -.
DR OrthoDB; 782448at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002530; Chromosome 6.
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; 2.
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..725
FT /note="E3 ubiquitin-protein ligase bre1"
FT /id="PRO_0000245301"
FT ZN_FING 673..712
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 175..228
FT /evidence="ECO:0000255"
FT COILED 269..526
FT /evidence="ECO:0000255"
FT COILED 559..656
FT /evidence="ECO:0000255"
FT COMPBIAS 16..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 82107 MW; F16D57124C18550A CRC64;
MPATEASPVV CSESAIVKME DRKRPATHDH NDSAPPLKKQ ATSVNGGSKP HPDADMPWKD
DLERFQKDAI WRQMQEYKRE KMSLETKLKE MSKATAYHND HLRVIDAWFN QLIDEVKTLM
GALDEDKDRP SFRSSLLFEN MEDFEKHLKA RSDDIRAIIT RLQSFSINAP PEVTDLQSQL
AKKLAEEKGT IAELEKALAE KQQLEESLEA ASLRYMVAEK KLDRARSLTV AKLEKQYLLG
AQRPGGDSAS GNREEQSPVN GLPSSAERNT ELEEAHKQLV AVSEKQKEQL QKLESENANL
LSQITELNIK RTKPTDDDYA HTDLFKQLRS QYDDVVKRIN HLEATNIQLR EEAAKLRSER
TAYRNQVDEE TQNVIAEKEA QLMRAETDLA RIRNARDELL ADQQMRKAAQ EQEKIATTKV
QELADAAQAR INALESEVDR LRLQLDNTKA AHTEIDDVPL EELRAKYQNL ERQYSMLNTE
LTSMQTACKK YSLLASQKVA DFSALEEKVA RLTAEKSKAD QKYFAAMKSK EARELEVRTL
RIQNSKSSDI VSQLKESEAT TRSLLANMEK QASETKEALN SIISKHHAAQ QQIAENNIVI
DGLKAQVNEL KALSVSKDSS LASASSACRK AETEIESLKV TLADTKKSLE NWKNKSLGNS
SSEYEMLRSL ALCTVCRRNF KNTAIKTCGH VFCKECVEER LTSRSRKCPN CNRSFGNNDH
MHITL
