(data stored in SCRATCH zone)

SWISSPROT: C3MHG1_SINFN

ID   C3MHG1_SINFN            Unreviewed;       415 AA.
AC   C3MHG1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:ACP24289.1};
GN   OrderedLocusNames=NGR_c04930 {ECO:0000313|EMBL:ACP24289.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24289.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24289.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RNA M5U methyltransferase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01024,
CC       ECO:0000256|SAAS:SAAS00828973}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001389; ACP24289.1; -; Genomic_DNA.
DR   RefSeq; WP_012707074.1; NC_012587.1.
DR   RefSeq; YP_002825042.1; NC_012587.1.
DR   ProteinModelPortal; C3MHG1; -.
DR   STRING; 394.NGR_c04930; -.
DR   EnsemblBacteria; ACP24289; ACP24289; NGR_c04930.
DR   GeneID; 7791719; -.
DR   KEGG; rhi:NGR_c04930; -.
DR   PATRIC; fig|394.7.peg.3302; -.
DR   eggNOG; ENOG4107QS4; Bacteria.
DR   eggNOG; COG2265; LUCA.
DR   HOGENOM; HOG000029866; -.
DR   KO; K03215; -.
DR   OMA; GFWQVHR; -.
DR   OrthoDB; POG091H00VG; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MHG1.
DR   SWISS-2DPAGE; C3MHG1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01024,
KW   ECO:0000256|SAAS:SAAS00828993, ECO:0000313|EMBL:ACP24289.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01024,
KW   ECO:0000256|SAAS:SAAS00829012};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01024,
KW   ECO:0000256|SAAS:SAAS00828989, ECO:0000313|EMBL:ACP24289.1}.
FT   ACT_SITE    373    373       {ECO:0000256|PROSITE-ProRule:PRU10015}.
FT   ACT_SITE    373    373       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01024}.
FT   BINDING     252    252       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   BINDING     279    279       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01024}.
FT   BINDING     299    299       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   BINDING     347    347       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
SQ   SEQUENCE   415 AA;  44507 MW;  FA18F098DB5A2D85 CRC64;
     MSTEIVTVNR LGAQGDGIAQ TEAGPVYAPF TLPGETVALA VNKAHGTLIS LKEASPDRIE
     PTCRHFGPDG VNGTCGGCTL QHASDPLYHA FKRNLVIDAL KSKGLKPEVA PLIIARPGER
     RRAVFTARRT EKELLLGFNQ AQSHHIVAVG ECPITSPGIV SRLPTIRKIA AAMASGAEPF
     RITVLETDSG LDLAFEDIKL SDRQRRSTVE AVLGERGIAR VSLNGEIIIE PVKPLIDFDG
     VSVSPPPGAF TQATRPAEEA MAKLVLGHIG KAKRVADLFA GIGTFALRIA RTARVHAVEG
     EDKALKALDF AARNTQGLKP VTVEKRDLFR RPMMAQELKV FDAVVFDPPR AGAEAQCHEL
     ARSGVKKIAA VSCNPVTLAR DLSILVAAGY RIRSVTPIDQ FLWSAHVEAV ATLEK
//

If you have problems or comments...

PBIL Back to PBIL home page