BUR1_NEUCR
ID BUR1_NEUCR Reviewed; 559 AA.
AC Q871M9; Q7RWH6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Serine/threonine-protein kinase bur1;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=Serine-threonine kinase 1;
GN Name=stk-1; Synonyms=bur1; ORFNames=B20D17.070, NCU01435;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in transcription
CC regulation. Phosphorylates the mus-8/ubc2 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD70970.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX294023; CAD70970.1; ALT_INIT; Genomic_DNA.
DR EMBL; CM002240; EAA26759.3; -; Genomic_DNA.
DR RefSeq; XP_955995.3; XM_950902.3.
DR AlphaFoldDB; Q871M9; -.
DR SMR; Q871M9; -.
DR STRING; 5141.EFNCRP00000007589; -.
DR PRIDE; Q871M9; -.
DR EnsemblFungi; EAA26759; EAA26759; NCU01435.
DR GeneID; 3872142; -.
DR KEGG; ncr:NCU01435; -.
DR VEuPathDB; FungiDB:NCU01435; -.
DR HOGENOM; CLU_000288_181_21_1; -.
DR InParanoid; Q871M9; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
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:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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..559
FT /note="Serine/threonine-protein kinase bur1"
FT /id="PRO_0000085685"
FT DOMAIN 40..341
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 359..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 46..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 559 AA; 62666 MW; 43F1136CB67D8CA2 CRC64;
MSIDEAKEGG GGPAMSPRAF ALAHQRDRGS FVGCSRIADY EVLGKLGEGT FGEVHRARSR
KTGALVALKK IIMHNERDGF PITALREIKL LKLLSHKNVL RLEEMAIEHP PRTDKRTRPI
VYMVTPYMDH DLSGLLDNPS VRFTEPQVKC YLLQLLEGLK YLHANHILHR DMKAANLLIN
NKGVLQIADF GLARHYEGDI PQPGKGSGEG KRDYTSLVVT RWYRPPELLM HLKRYTTAID
MWGVGCVFAE MLEGKPVLQG ESDLHQLELV WDLCGTPSEE TMPGWRTLPG GQAFSSKPRP
GNLARRFEKH GPVVISLLKE LFKLDWRSRI NAIDALNHPY FRTAPLPALP GDLPTFEESH
EFDRRKFQDR KAALPPAPKG GTVGRGAVVN SQGPDTGFSG RDGYGGGGRN GANGGRYPPY
HRGPPPGDER VPSWHSARGL PPRPPMPADY HGSGPMDHTD GYRDRPPRRG PGGPPGGGGG
PSNVDTYIPS YDRDGPAPRR EDWRRRDDWD DRRGGVDRDR RRPEYDVRSR DSRTRSRTRS
RSPVRDRDRG RDRDAYARR
