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DOT1L_DICDI
ID   DOT1L_DICDI             Reviewed;        1845 AA.
AC   Q55AX2;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000303|PubMed:21187070};
DE            EC=2.1.1.360 {ECO:0000250|UniProtKB:Q04089};
DE   AltName: Full=Disruptor of telomeric silencing A {ECO:0000303|PubMed:21187070};
DE   AltName: Full=Histone H3-K79 methyltransferase {ECO:0000250|UniProtKB:Q04089};
DE            Short=H3-K79-HMTase {ECO:0000250|UniProtKB:Q04089};
DE   AltName: Full=SAM domain-containing protein {ECO:0000312|EMBL:EAL71677.2};
GN   Name=dotA {ECO:0000312|EMBL:EAL71677.2};
GN   Synonyms=dot1 {ECO:0000303|PubMed:21187070},
GN   KMT4 {ECO:0000303|PubMed:21187070}; ORFNames=DDB_G0271626;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1] {ECO:0000312|EMBL:EAL71677.2}
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] {ECO:0000312|EMBL:EAL71677.2}
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).
RN   [3] {ECO:0000305}
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=AX2 {ECO:0000269|PubMed:21187070};
RX   PubMed=21187070; DOI=10.1016/j.bbrc.2010.12.101;
RA   Muller-Taubenberger A., Bonisch C., Furbringer M., Wittek F., Hake S.B.;
RT   "The histone methyltransferase Dot1 is required for DNA damage repair and
RT   proper development in Dictyostelium.";
RL   Biochem. Biophys. Res. Commun. 404:1016-1022(2011).
CC   -!- FUNCTION: Histone methyltransferase that specifically methylates
CC       histone H3 to form H3K79me. This methylation is required for telomere
CC       silencing, correct growth and development, and for resistance to DNA
CC       damage induced by UV LIGHT. {ECO:0000269|PubMed:21187070}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60328, Rhea:RHEA-COMP:15549, Rhea:RHEA-
CC         COMP:15552, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.360;
CC         Evidence={ECO:0000250|UniProtKB:Q04089, ECO:0000255|PROSITE-
CC         ProRule:PRU00902};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04089}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during the whole life cycle.
CC       {ECO:0000269|PubMed:21187070}.
CC   -!- DISRUPTION PHENOTYPE: Individuals exhibit 4-5 hours delay in
CC       development. Development does progress with fewer fruiting bodies and
CC       smaller spore heads. No apparent changes in cell cycle regulation.
CC       {ECO:0000269|PubMed:21187070}.
CC   -!- MISCELLANEOUS: In contrast to other lysine histone methyltransferases,
CC       it does not contain a SET domain, suggesting the existence of another
CC       mechanism for methylation of lysine residues of histones.
CC       {ECO:0000303|PubMed:21187070}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. DOT1 family. {ECO:0000255|PROSITE-ProRule:PRU00902}.
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DR   EMBL; AAFI02000006; EAL71677.2; -; Genomic_DNA.
DR   RefSeq; XP_645574.2; XM_640482.2.
DR   AlphaFoldDB; Q55AX2; -.
DR   SMR; Q55AX2; -.
DR   STRING; 44689.DDB0233511; -.
DR   PaxDb; Q55AX2; -.
DR   PRIDE; Q55AX2; -.
DR   EnsemblProtists; EAL71677; EAL71677; DDB_G0271626.
DR   GeneID; 8618027; -.
DR   KEGG; ddi:DDB_G0271626; -.
DR   dictyBase; DDB_G0271626; dotA.
DR   eggNOG; KOG3924; Eukaryota.
DR   HOGENOM; CLU_237041_0_0_1; -.
DR   InParanoid; Q55AX2; -.
DR   Reactome; R-DDI-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q55AX2; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR   GO; GO:0031151; F:histone methyltransferase activity (H3-K79 specific); IDA:dictyBase.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:dictyBase.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0034729; P:histone H3-K79 methylation; IMP:dictyBase.
DR   GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
DR   GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR025789; DOT1_dom.
DR   InterPro; IPR030445; H3-K79_meTrfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR21451; PTHR21451; 2.
DR   Pfam; PF08123; DOT1; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51569; DOT1; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; DNA damage; DNA repair; Methyltransferase; Nucleus;
KW   Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..1845
FT                   /note="Histone-lysine N-methyltransferase, H3 lysine-79
FT                   specific"
FT                   /id="PRO_0000413849"
FT   DOMAIN          1125..1446
FT                   /note="DOT1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          83..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          585..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          625..639
FT                   /note="Required for interaction with nucleosomes and DNA"
FT                   /evidence="ECO:0000250|UniProtKB:Q04089"
FT   REGION          741..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          862..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          963..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1463..1559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1610..1661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1735..1762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1772..1791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1799..1845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..762
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..1069
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1083..1102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1463..1519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1520..1534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1537..1559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1610..1643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1741..1758
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1799..1818
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1251..1254
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT   BINDING         1274..1283
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00902"
FT   BINDING         1300
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q04089,
FT                   ECO:0000255|PROSITE-ProRule:PRU00902"
SQ   SEQUENCE   1845 AA;  212281 MW;  6CDF92C0D67AAD87 CRC64;
     MSTNSTPRKQ KLSNSKSLQN SPISPTVKKT NSFPLGNNIP TNINRSKKDK NNNSNNNINN
     NNSNGIGSNT IINSTPIATT PVPPLPFIHS SSSSSSSPSP SSSSSSPFPK AKKSPSLSIN
     QQQQQQPQQP QQSPQSQQSP QSQQSQQSQQ QQPQQPQEQQ EPLPNLSFLR NQEPDKNVLP
     TSRKRPPSVM PSTPNQSSNS SSLNSSLNFS SSNSSPSPTS TQSNNSRFET RSQNDQYENN
     NNNNNNNNNN NNNNNNNNNN NNNIECIVID DDDDDDDDEG NSIKSTHTST QSTPIRDRRQ
     RDNKWTINPL PQFQREIIDV DTPSPPNESL SIVSQTTTNT ITDTTSIQTP TLIRQSSSLL
     SSSSSLSPST TSTPLTQNNI NLQNAQVIAT MTAPMEIELP TIVQLEPLFS SEFTTSTQNL
     FIQTPPFTST LTLPTTTAQT SQTLFTIQTS HDINNNNNNN NNNKNKNKNK KEIEKEKEKL
     REALKQKLKE YENENEKERE KERKREREIE IERERKERER KEREKERKKE KEREREREER
     ERKEIERKER EREEREERER KEIERKETER KEIERKEIER KEIERKERER KERKEREERE
     EREREERERK EREEREKEIE MEREKKKEKE KEKEKEKEKE KEKEKEKEKE KEKEKEKEKK
     RKENEVENEI EKERREKNDS YMVLNYHHSI DDHHSESESE SDSDQDSIYS ISTQELSSVI
     SDNDFCDSDN EKVANNNRTV GETFLNDSRN NNNNNNNNKN NNNKKIENDK NQLIERERLI
     SAFNDKAFLY ALDTIREVLG GIDFKLKVSK EQIIEISTNA KKPLNILSEP EQQQQQQQQQ
     QQQQHQQQQQ QQQQQQQQQQ QQTTKTTTTT NNTTTTTAET EKPKEVFLLK KPIKIPYGRD
     CKKRLIRRFH GTSRNPLFHK NLESTLKLLK RAKFDWASIE FDTKSYLMNC NCKTVCHKSE
     RMKDNPTNKL QNNNRNNNNN NNNIINNNNN NNNKNNNNKN NNNKNNNRNN NSIAKKIGTN
     NNNNNTTIIK NNNNNNNNNN NNNNNNNNII KNNNNNNKNN NNNNNTIVKK IETIKKDINK
     KPTKTTTTTS SSSSSTSSSN SLTVIKKPVK KINGSQRICL FEDDFDVGIG VPVTTGTSET
     TTTRASSIRR KMNISNIFDD FTKKPRQNKY NEIEMPDLFA SKECNYTLEQ QAPFIRAQKL
     LLTQQHENNL YNGKRFMKYD EWLDLYHGEM RSSIQNPKVL KHYISFSQEV YGEAEPTLLR
     HWIHLGLIKP TDVFCDIGCG IGNVLFQLAA QVGCRVIGVE IRKDLYDISQ SMLEIYKKRS
     LELGLHPSTQ QIKIYNCDVK GSLEFDFSEP NVFFMHNTCF GPELEISIME LFKKYSKPGT
     KVITMKTLCP RFKPSDKKTK PWGIFKYPYE SYEMEEGSLS WRSATNCSFY SFTIDDKDSD
     IVTDQTHLNR VILSTPKKKH SKLQLFSSSS LPSSPPSSSS SSSPPNIATN TTTTTTTTTT
     TSPSSISLPS PYLSPSKKTP NSNKRDRSDI DNSNSDDGDE NNNNININNN NNNSNNKPIK
     LKLSMDHSID NQSNSESSDT DVEYMPWSKR NNRKKRKSLS YSLDSYLSSR ISPSLSLSTS
     SSSSSSLDSS PYSSPPSSSS SDNENDDDNG DDEDDSSSSN DTKLKEKLLL MKNNEKIGGA
     PPLTRRNANS DTNKLVQGCY QSLSSYALPK EESQIHKLQL QAKLLEHKNS LVLKHQKSIH
     DQQKRLSRKQ KKLAKKNKKK EQQLQAQAKT INYNNNNNNN NQNDNQVNHN NLNENEINTD
     LINGYNNNNN NNIINNDNDN DNDNDKDDDK DSNNKDYNNI NDNNK
 
 
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