GenomeNet

Database: UniProt
Entry: Q8X225
LinkDB: Q8X225
Original site: Q8X225 
ID   DIM5_NEUCR              Reviewed;         331 AA.
AC   Q8X225; Q1K5Y7;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   16-JAN-2019, entry version 111.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K9 methyltransferase dim-5;
DE            Short=H3-K9-HMTase dim-5;
DE            Short=HKMT;
GN   Name=dim-5; ORFNames=29E8.110, NCU04402;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
OS   1257 / FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 18889 / 74-OR8-1a / 40-21 / DSM 1258 / FGSC 988;
RX   PubMed=11713521; DOI=10.1038/35104508;
RA   Tamaru H., Selker E.U.;
RT   "A histone H3 methyltransferase controls DNA methylation in Neurospora
RT   crassa.";
RL   Nature 414:277-283(2001).
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=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
RA   Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
RA   Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the
RT   Neurospora genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
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.,
RA   Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA   Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA   Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA   Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA   Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA   Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA   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.,
RA   Paulsen I., 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).
RN   [4]
RP   FUNCTION, AND METHYLATION OF HISTONE H3.
RX   PubMed=12679815; DOI=10.1038/ng1143;
RA   Tamaru H., Zhang X., McMillen D., Singh P.B., Nakayama J.,
RA   Grewal S.I., Allis C.D., Cheng X., Selker E.U.;
RT   "Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in
RT   Neurospora crassa.";
RL   Nat. Genet. 34:75-79(2003).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 30-331 IN COMPLEX WITH ZINC
RP   IONS, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-251;
RP   ASN-254; HIS-255 AND TYR-296.
RX   PubMed=12372305; DOI=10.1016/S0092-8674(02)00999-6;
RA   Zhang X., Tamaru H., Khan S.I., Horton J.R., Keefe L.J., Selker E.U.,
RA   Cheng X.;
RT   "Structure of the Neurospora SET domain protein DIM-5, a histone H3
RT   lysine methyltransferase.";
RL   Cell 111:117-127(2002).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 30-331 IN COMPLEX WITH
RP   HISTONE H3; S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS, FUNCTION,
RP   CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-191; ASP-222; PHE-294;
RP   LEU-330 AND TRP-331.
RX   PubMed=12887903; DOI=10.1016/S1097-2765(03)00224-7;
RA   Zhang X., Yang Z., Khan S.I., Horton J.R., Tamaru H., Selker E.U.,
RA   Cheng X.;
RT   "Structural basis for the product specificity of histone lysine
RT   methyltransferases.";
RL   Mol. Cell 12:177-185(2003).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates histone H3 to form H3K9me3. H3K9me3 marks chromatin
CC       regions for DNA methylation. {ECO:0000269|PubMed:11713521,
CC       ECO:0000269|PubMed:12372305, ECO:0000269|PubMed:12679815,
CC       ECO:0000269|PubMed:12887903}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:12372305,
CC         ECO:0000269|PubMed:12887903};
CC   -!- INTERACTION:
CC       Q96UA9:9G6.050 (xeno); NbExp=2; IntAct=EBI-1268994, EBI-15849296;
CC       P07041:hh3; NbExp=2; IntAct=EBI-1268994, EBI-1270655;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO:0000269|PubMed:12372305}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL35215.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAF06044.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF419248; AAL35215.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BX908809; CAF06044.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002239; EAA28243.2; -; Genomic_DNA.
DR   RefSeq; XP_957479.2; XM_952386.3.
DR   PDB; 1ML9; X-ray; 1.98 A; A=30-331.
DR   PDB; 1PEG; X-ray; 2.59 A; A/B=30-331.
DR   PDBsum; 1ML9; -.
DR   PDBsum; 1PEG; -.
DR   ProteinModelPortal; Q8X225; -.
DR   SMR; Q8X225; -.
DR   DIP; DIP-39600N; -.
DR   IntAct; Q8X225; 2.
DR   ChEMBL; CHEMBL3309062; -.
DR   PRIDE; Q8X225; -.
DR   EnsemblFungi; EAA28243; EAA28243; NCU04402.
DR   GeneID; 3873656; -.
DR   KEGG; ncr:NCU04402; -.
DR   EuPathDB; FungiDB:NCU04402; -.
DR   InParanoid; Q8X225; -.
DR   KO; K11419; -.
DR   OMA; DKFTDPD; -.
DR   EvolutionaryTrace; Q8X225; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromosome; Complete proteome; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; Zinc.
FT   CHAIN         1    331       Histone-lysine N-methyltransferase, H3
FT                                lysine-9 specific dim-5.
FT                                /FTId=PRO_0000186062.
FT   DOMAIN       77    159       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      162    297       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      315    331       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      172    174       S-adenosyl-L-methionine binding.
FT   REGION      254    255       S-adenosyl-L-methionine binding.
FT   METAL        79     79       Zinc 1.
FT   METAL        79     79       Zinc 2.
FT   METAL        81     81       Zinc 1.
FT   METAL        87     87       Zinc 1.
FT   METAL        87     87       Zinc 3.
FT   METAL        92     92       Zinc 1.
FT   METAL        94     94       Zinc 2.
FT   METAL       141    141       Zinc 2.
FT   METAL       141    141       Zinc 3.
FT   METAL       145    145       Zinc 2.
FT   METAL       147    147       Zinc 3.
FT   METAL       151    151       Zinc 3.
FT   METAL       257    257       Zinc 4.
FT   METAL       319    319       Zinc 4.
FT   METAL       321    321       Zinc 4.
FT   METAL       326    326       Zinc 4.
FT   BINDING     215    215       S-adenosyl-L-methionine.
FT   BINDING     217    217       S-adenosyl-L-methionine.
FT   BINDING     251    251       S-adenosyl-L-methionine.
FT   MUTAGEN     191    191       Y->F: Reduces enzyme activity by 97%.
FT                                {ECO:0000269|PubMed:12887903}.
FT   MUTAGEN     191    191       Y->V: Reduces enzyme activity by over
FT                                99%. {ECO:0000269|PubMed:12887903}.
FT   MUTAGEN     222    222       D->E: Reduces enzyme activity by over
FT                                99%. {ECO:0000269|PubMed:12887903}.
FT   MUTAGEN     222    222       D->K: Reduces enzyme activity by 97%.
FT                                {ECO:0000269|PubMed:12887903}.
FT   MUTAGEN     222    222       D->Q: Reduces enzyme activity by 97%.
FT                                {ECO:0000269|PubMed:12887903}.
FT   MUTAGEN     251    251       R->H: Reduces enzyme activity by over
FT                                99%. {ECO:0000269|PubMed:12372305}.
FT   MUTAGEN     254    254       N->Q: Reduces enzyme activity by over
FT                                99%. {ECO:0000269|PubMed:12372305}.
FT   MUTAGEN     255    255       H->K: Reduces enzyme activity by over
FT                                99%. {ECO:0000269|PubMed:12372305}.
FT   MUTAGEN     294    294       F->W: Reduces enzyme activity by over
FT                                99%. {ECO:0000269|PubMed:12887903}.
FT   MUTAGEN     294    294       F->Y: Reduces enzyme activity by 20%.
FT                                {ECO:0000269|PubMed:12887903}.
FT   MUTAGEN     296    296       Y->F: Reduces enzyme activity by over
FT                                99%. {ECO:0000269|PubMed:12372305}.
FT   MUTAGEN     330    330       L->A: Reduces enzyme activity by over
FT                                99%. {ECO:0000269|PubMed:12887903}.
FT   MUTAGEN     331    331       W->A: Reduces enzyme activity by 97%.
FT                                {ECO:0000269|PubMed:12887903}.
FT   STRAND       41     44       {ECO:0000244|PDB:1ML9}.
FT   STRAND       46     49       {ECO:0000244|PDB:1ML9}.
FT   HELIX        73     75       {ECO:0000244|PDB:1ML9}.
FT   HELIX        86     88       {ECO:0000244|PDB:1ML9}.
FT   HELIX        93     95       {ECO:0000244|PDB:1ML9}.
FT   STRAND       96     98       {ECO:0000244|PDB:1PEG}.
FT   STRAND      115    118       {ECO:0000244|PDB:1ML9}.
FT   STRAND      119    121       {ECO:0000244|PDB:1PEG}.
FT   TURN        122    125       {ECO:0000244|PDB:1PEG}.
FT   HELIX       129    134       {ECO:0000244|PDB:1ML9}.
FT   HELIX       155    158       {ECO:0000244|PDB:1ML9}.
FT   STRAND      164    168       {ECO:0000244|PDB:1ML9}.
FT   STRAND      170    172       {ECO:0000244|PDB:1ML9}.
FT   STRAND      174    177       {ECO:0000244|PDB:1ML9}.
FT   STRAND      187    190       {ECO:0000244|PDB:1ML9}.
FT   STRAND      194    196       {ECO:0000244|PDB:1ML9}.
FT   HELIX       198    207       {ECO:0000244|PDB:1ML9}.
FT   HELIX       210    212       {ECO:0000244|PDB:1ML9}.
FT   HELIX       214    217       {ECO:0000244|PDB:1ML9}.
FT   STRAND      218    220       {ECO:0000244|PDB:1ML9}.
FT   STRAND      227    230       {ECO:0000244|PDB:1ML9}.
FT   HELIX       232    235       {ECO:0000244|PDB:1ML9}.
FT   STRAND      240    242       {ECO:0000244|PDB:1ML9}.
FT   STRAND      244    247       {ECO:0000244|PDB:1ML9}.
FT   HELIX       249    252       {ECO:0000244|PDB:1ML9}.
FT   STRAND      260    269       {ECO:0000244|PDB:1ML9}.
FT   HELIX       270    275       {ECO:0000244|PDB:1ML9}.
FT   STRAND      277    284       {ECO:0000244|PDB:1ML9}.
FT   STRAND      291    294       {ECO:0000244|PDB:1ML9}.
SQ   SEQUENCE   331 AA;  37572 MW;  2C97AB4B5E582D88 CRC64;
     MEKAFRPHFF NHGKPDANPK EKKNCHWCQI RSFATHAQLP ISIVNREDDA FLNPNFRFID
     HSIIGKNVPV ADQSFRVGCS CASDEECMYS TCQCLDEMAP DSDEEADPYT RKKRFAYYSQ
     GAKKGLLRDR VLQSQEPIYE CHQGCACSKD CPNRVVERGR TVPLQIFRTK DRGWGVKCPV
     NIKRGQFVDR YLGEIITSEE ADRRRAESTI ARRKDVYLFA LDKFSDPDSL DPLLAGQPLE
     VDGEYMSGPT RFINHSCDPN MAIFARVGDH ADKHIHDLAL FAIKDIPKGT ELTFDYVNGL
     TGLESDAHDP SKISEMTKCL CGTAKCRGYL W
//
DBGET integrated database retrieval system