ID   BUR1_ASPFU              Reviewed;         580 AA.
AC   Q4WTN5;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Serine/threonine-protein kinase bur1;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
GN   Name=bur1; ORFNames=AFUA_5G05510;
OS   Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS   Af293) (Neosartorya fumigata).
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 / CBS 101355 / FGSC A1100 / Af293;
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: Serine/threonine-protein kinase involved in transcription
CC       regulation. Phosphorylates the UBC2/RAD6 ubiquitin-conjugating enzyme
CC       (E2), leading to monoubiquitination of histone H2B and the silencing of
CC       telomeric-associated genes. Also required for histone H3 methylation.
CC       Necessary for the recovery from pheromone-induced growth arrest in the
CC       cell cycle G1 phase (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.22;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC         [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC         COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC         ChEBI:CHEBI:456216; EC=2.7.11.23;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR   EMBL; AAHF01000003; EAL92041.1; -; Genomic_DNA.
DR   RefSeq; XP_754079.1; XM_748986.1.
DR   AlphaFoldDB; Q4WTN5; -.
DR   SMR; Q4WTN5; -.
DR   STRING; 330879.Q4WTN5; -.
DR   EnsemblFungi; EAL92041; EAL92041; AFUA_5G05510.
DR   GeneID; 3511249; -.
DR   KEGG; afm:AFUA_5G05510; -.
DR   VEuPathDB; FungiDB:Afu5g05510; -.
DR   eggNOG; KOG0600; Eukaryota.
DR   HOGENOM; CLU_470065_0_0_1; -.
DR   InParanoid; Q4WTN5; -.
DR   OMA; PWHGHAS; -.
DR   OrthoDB; 10753at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
DR   GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0070691; C:P-TEFb complex; IEA:EnsemblFungi.
DR   GO; GO:0070693; C:P-TEFb-cap methyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0140836; F:RNA polymerase II CTD heptapeptide repeat S5 kinase activity; IEA:EnsemblFungi.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:EnsemblFungi.
DR   CDD; cd07866; STKc_BUR1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF584; SERINE_THREONINE-PROTEIN KINASE BUR1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..580
FT                   /note="Serine/threonine-protein kinase bur1"
FT                   /id="PRO_0000085678"
FT   DOMAIN          25..326
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        155
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         31..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   580 AA;  65107 MW;  F2BBE96748382704 CRC64;
     MAIASLERDD HGNPRFRGCT SIRDFEFLGK LGEGTFGEVY KARSKKDGSI VALKKILMHN
     EKDGFPITAL REIKLLKMLS HRNILQLKEM AVERSKGDGR KKPSMYMVTP YMEHDLSGLL
     ENPAVNFTEP QIKCYMLQLL EGLKYLHGNR ILHRDMKAAN LLISNNGVLQ IADFGLARPY
     DEPPPEPGKG GGEAKRDYTT LVVTRWYRPP ELLLQLRRYT TAIDMWGVGC VFGEMFKGKP
     ILAGSSDLNQ TQLIFNLVGT PTEENMPGWS SLPGCEGVKS FGYKPGSLRE VFKDQNPMAI
     SLLEELLKLD WRKRINAIDA INHPYFSSPP FPARPGELPS FEDSHEFDRR RFRGQRGAIP
     PAPAGGSVDQ QQTTEIAVFP VLHALAGSLH TGFKTILQSA LLKTGMLYHM DLQTRGSRFQ
     ASLVQKIAAC LLNLLCLLIH HGAWVIQIGR HVREVNAIIS EDGPMGNWIH TSRLTVTLVD
     ILEKGKAIVR VPLLIGVIWN SNTLMKGINR VILGTDVLQE REAGVLTFER LEQRIEHCTD
     DDKLVLVSTD AERLRQMNPV TLLVLNDSKF ITHLLLSMTY
//