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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / IFO 6347 / NRRL 1970;
Birren B.W.,
Lander E.S.,
Galagan J.E.,
Devon K.,
Nusbaum C.,
Ma L.-J.,
Jaffe D.B.,
Butler J.,
Alvarez P.,
Gnerre S.,
Grabherr M.,
Kleber M.,
Mauceli E.W.,
Brockman W.,
Rounsley S.,
Young S.K.,
LaButti K.,
Pushparaj V.,
DeCaprio D., ![]()
Crawford M.,
Koehrsen M.,
Engels R.,
Montgomery P.,
Pearson M.,
Howarth C.,
Kodira C.D.,
Yandava C.,
Zeng Q.,
Alvarado L.,
Oleary S.,
Untereiner W.;
"Annotation of the Chaetomium globosum CBS 148.51 genome.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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- FUNCTION: Histone methyltransferase that specifically methylates histone H3 to form H3K79me. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histones (By similarity).
- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N6-methyl-L-lysine.
- ENZYME REGULATION: Ubiquitination of histone H2B to form H2BK123ub1 is required for efficient DOT1 methyltransferase activity on histone H3 (By similarity).
- SUBCELLULAR LOCATION: Nucleus (By similarity).
- MISCELLANEOUS: In contrast to other lysine histone methyltransferase, it does not contain a SET domain, suggesting the existence of another mechanism for methylation of lysine residues of histones.
- SIMILARITY: Belongs to the DOT1 family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 510 AA [This is the length of the unprocessed precursor] |
Molecular weight: 56217 Da [This is the MW of the unprocessed precursor] |
CRC64: 1D678E4D39D6A9D4 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MSIFNQKSKF KVKTEVRKVK QAVEPTPESK KRYVGNGSAS ASTNGTPRAS PTPSSLQVKR
70 80 90 100 110 120
PRPRPGAGAA SPATGPSLSS STSASPLDLT RKRRAPAGSS SSRSPATASP APRALSDSEP
130 140 150 160 170 180
GSDDDDDDDW RDRLDPSKRR KRAHTEDPDR RLRHPRLWAG QGDEDKPGIV HAVQVASLAD
190 200 210 220 230 240
KCQPVMKLAR DEVGVRLRYP GAKYTERYEL VWGKDKIDGA LDIMKVVKFV ASTYLTDAEA
250 260 270 280 290 300
KPFLDHNLGI NRRLEKSKNT NDGEGFKAAL AEYNNQLLAL QTEGAIARNI DAMRGVPREL
310 320 330 340 350 360
VEFILDQVYD RTVAPKVDLL AKYENGTDNV YGELLHPFIS DIFDRTKLSS DMVFVDLGSG
370 380 390 400 410 420
VGNVTLQAAL ERGCESWGCE MMENACNLAE AQKKEFTARC RMWGIAPGKV HLERGDFRKS
430 440 450 460 470 480
ERTLAALKRA DVVLVNNQAF TSELNDHLVN IFLDLKIGCK IVSLKTFVHD NKIAENDVAS
490 500 510
SILEVEDLRY HEGYVSWTGA AGSFCISTRK
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Q2H9L1 in FASTA format |
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