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G7KMG0 (G7KMG0_MEDTR) Unreviewed, UniProtKB/TrEMBL

Last modified October 31, 2012. Version 8. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesSubmitted name:
Histone-lysine N-methyltransferase ASHH3 EMBL AES75763.1
Gene names
ORF Names:MTR_6g059310 EMBL AES75763.1
OrganismMedicago truncatula (Barrel medic) (Medicago tribuloides) EMBL AES75763.1
Taxonomic identifier3880 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existencePredicted

General annotation (Comments)

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. SAAS SAAS001214

Sequence similarities

Contains 1 SET domain. RuleBase RU004538

Contains 1 post-SET domain. RuleBase RU004541 SAAS SAAS001214

Ontologies

Keywords
   Cellular componentNucleus SAAS SAAS003616
   Molecular functionMethyltransferase SAAS SAAS001214 RuleBase RU004541 EMBL AES75763.1
Transferase
Gene Ontology (GO)
   Biological_processhistone lysine methylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionhistone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
G7KMG0 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: 03E41D1C5AD8E335

FASTA34839,707
        10         20         30         40         50         60 
MPIMKKNSEQ NRFEAVFTKL MNNLGETVDF ELPDSIKNRT TQYTHIKHVY VTKNRKRKSD 

        70         80         90        100        110        120 
DGIFCSCESS SDSTAVCGRD CHCGMLLSSC SSGCKCGISC LNKAFQHRPV KKMKLVKTEK 

       130        140        150        160        170        180 
CGSGIVADED IKLGEFVIEY VGEVIDDKTC EQRLWNMKDR GETNFYLCEI NRDMVIDATN 

       190        200        210        220        230        240 
KGNKSRYINH SCCPNTEMQK WIIDGETRIG IFASRDIKKG EHLTYDYQFV QFGADQDCHC 

       250        260        270        280        290        300 
GAVQCRRKLG ARPTKPKLVA YQTNCGLLSS GQVYQNGGLQ TGSSRVVDHS KCLLNCIDEV 

       310        320        330        340 
IMIKQLGNLR FGIIKWFDEY SRKHKIMFED GCVEIYDMSK EDWELVRL

« Hide

References

[1]"The Medicago genome provides insight into the evolution of rhizobial symbioses."
Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K., Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S., Krishnakumar V. expand/collapse author list , Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y., Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L., Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.
Nature 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: A17 EMBL AES75763.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CM001222 Genomic DNA. Translation: AES75763.1.
RefSeqXP_003619545.1. XM_003619497.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID11443283.
KEGGmtr:MTR_6g059310.

Phylogenomic databases

KOK11423.

Family and domain databases

InterProIPR006560. AWS.
IPR025787. Hist-Lys_N-MeTrfase_SET2_plant.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamPF00856. SET. 1 hit.
[Graphical view]
SMARTSM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEPS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS51578. SAM_MT43_SET2_2. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG7KMG0_MEDTR
AccessionPrimary (citable) accession number: G7KMG0
Entry history
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: October 31, 2012
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry info