GenomeNet

Database: UniProt
Entry: B9RU15
LinkDB: B9RU15
Original site: B9RU15 
ID   ATXR5_RICCO             Reviewed;         374 AA.
AC   B9RU15;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   10-APR-2019, entry version 47.
DE   RecName: Full=Probable Histone-lysine N-methyltransferase ATXR5;
DE            EC=2.1.1.43;
DE   Flags: Precursor;
GN   Name=ATXR5; ORFNames=RCOM_1460410;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae;
OC   Acalyphoideae; Acalypheae; Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale;
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B.,
RA   Gedil M., Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M.,
RA   Ravel J., Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 146-374 IN COMPLEX WITH HTR1
RP   PEPTIDE AND S-ADENOSYL-L-METHIONINE, AND SUBUNIT.
RX   PubMed=24626927; DOI=10.1126/science.1248357;
RA   Jacob Y., Bergamin E., Donoghue M.T., Mongeon V., LeBlanc C.,
RA   Voigt P., Underwood C.J., Brunzelle J.S., Michaels S.D., Reinberg D.,
RA   Couture J.F., Martienssen R.A.;
RT   "Selective methylation of histone H3 variant H3.1 regulates
RT   heterochromatin replication.";
RL   Science 343:1249-1253(2014).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       monomethylates 'Lys-37' of histone H3 (H3K27me1). Has much higher
CC       activity on nucleosomes containing H3.1 than H3.3. Involved in the
CC       formation of constitutive heterochromatin and the silencing of
CC       heterochromatic elements (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24626927}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; EQ973815; EEF45134.1; -; Genomic_DNA.
DR   RefSeq; XP_002517234.1; XM_002517188.2.
DR   PDB; 4O30; X-ray; 2.10 A; A/B=146-374.
DR   PDB; 5VA6; X-ray; 2.40 A; A/B=146-374.
DR   PDB; 5VAC; X-ray; 1.95 A; A=146-374.
DR   PDB; 5VAH; X-ray; 2.40 A; A/B=146-374.
DR   PDB; 5VBC; X-ray; 2.10 A; A/B=146-374.
DR   PDBsum; 4O30; -.
DR   PDBsum; 5VA6; -.
DR   PDBsum; 5VAC; -.
DR   PDBsum; 5VAH; -.
DR   PDBsum; 5VBC; -.
DR   ProteinModelPortal; B9RU15; -.
DR   SMR; B9RU15; -.
DR   DIP; DIP-61672N; -.
DR   STRING; 3988.XP_002517234.1; -.
DR   GeneID; 8259125; -.
DR   KEGG; rcu:8259125; -.
DR   InParanoid; B9RU15; -.
DR   OrthoDB; 1014608at2759; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloroplast; Chromatin regulator; Complete proteome;
KW   Metal-binding; Methyltransferase; Nucleus; Plastid;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase;
KW   Transit peptide; Zinc; Zinc-finger.
FT   TRANSIT       1     46       Chloroplast. {ECO:0000255}.
FT   CHAIN        47    374       Probable Histone-lysine N-
FT                                methyltransferase ATXR5.
FT                                /FTId=PRO_0000429174.
FT   DOMAIN      240    362       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING      59    109       PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   REGION      250    252       S-adenosyl-L-methionine binding.
FT   REGION      312    316       S-adenosyl-L-methionine binding.
FT   REGION      364    365       substrate binding.
FT   BINDING     216    216       Substrate.
FT   BINDING     334    334       Substrate.
FT   BINDING     368    368       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|PubMed:24626927}.
FT   BINDING     374    374       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190,
FT                                ECO:0000269|PubMed:24626927}.
FT   HELIX       170    186       {ECO:0000244|PDB:5VAC}.
FT   STRAND      193    196       {ECO:0000244|PDB:4O30}.
FT   TURN        199    201       {ECO:0000244|PDB:5VAC}.
FT   HELIX       204    206       {ECO:0000244|PDB:5VAC}.
FT   HELIX       209    211       {ECO:0000244|PDB:5VAC}.
FT   HELIX       221    236       {ECO:0000244|PDB:5VAC}.
FT   STRAND      241    247       {ECO:0000244|PDB:5VAC}.
FT   TURN        248    250       {ECO:0000244|PDB:5VAC}.
FT   STRAND      251    258       {ECO:0000244|PDB:5VAC}.
FT   STRAND      264    268       {ECO:0000244|PDB:5VAC}.
FT   STRAND      271    275       {ECO:0000244|PDB:5VAC}.
FT   HELIX       276    278       {ECO:0000244|PDB:5VAC}.
FT   STRAND      287    291       {ECO:0000244|PDB:5VAC}.
FT   STRAND      293    295       {ECO:0000244|PDB:5VAC}.
FT   HELIX       296    298       {ECO:0000244|PDB:5VAC}.
FT   STRAND      300    303       {ECO:0000244|PDB:5VAC}.
FT   STRAND      305    308       {ECO:0000244|PDB:5VAC}.
FT   HELIX       310    313       {ECO:0000244|PDB:5VAC}.
FT   STRAND      319    323       {ECO:0000244|PDB:4O30}.
FT   HELIX       324    327       {ECO:0000244|PDB:5VAC}.
FT   STRAND      330    337       {ECO:0000244|PDB:5VAC}.
FT   STRAND      340    349       {ECO:0000244|PDB:5VAC}.
FT   STRAND      362    364       {ECO:0000244|PDB:5VAC}.
SQ   SEQUENCE   374 AA;  42515 MW;  4506A8C135E308A1 CRC64;
     MAPASITTTT TVARRIVGSR RRTKATSPPD SPPPKKLKPI SEILAKAQYA VVERADYGDV
     SCMQCGSGER AEELLLCDKC DKGFHMKCVR PIVVRVPIGS WLCPKCSGQR RVRRLSQRKI
     IDFFRIQKCN HKTDKCSSPQ DIRKHRRRSG SLVYQKRRRR LLPFVSSEDP AQRLKQMGTL
     ASALTELQME FSDDLTYSSG MAPRSANQAR FEEGGMQVLT KEDIETLEQC RAMCKRGDCP
     PLLVVFDSRE GFTVEADGQI KDMTFIAEYT GDVDYIRNRE HDDCDSMMTL LLAKDPSKSL
     VICPDKRGNI ARFISGINNH TLDGKKKQNC KCVRYSVNGE CRVFLVATRD IAKGERLYYD
     YNGYEHEYPT QHFV
//
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