(data stored in ACNUC8465 zone)

SWISSPROT: B5ECN6_GEOBB

ID   B5ECN6_GEOBB            Unreviewed;       444 AA.
AC   B5ECN6;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 2.
DT   08-MAY-2019, entry version 64.
DE   SubName: Full=RNA methyltransferase, TrmA family {ECO:0000313|EMBL:ACH39071.2};
GN   OrderedLocusNames=Gbem_2058 {ECO:0000313|EMBL:ACH39071.2};
OS   Geobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=404380 {ECO:0000313|EMBL:ACH39071.2, ECO:0000313|Proteomes:UP000008825};
RN   [1] {ECO:0000313|EMBL:ACH39071.2, ECO:0000313|Proteomes:UP000008825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bem / ATCC BAA-1014 / DSM 16622
RC   {ECO:0000313|Proteomes:UP000008825};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter bemidjiensis BEM.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACH39071.2, ECO:0000313|Proteomes:UP000008825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bem / ATCC BAA-1014 / DSM 16622
RC   {ECO:0000313|Proteomes:UP000008825};
RX   PubMed=20828392; DOI=10.1186/1471-2164-11-490;
RA   Aklujkar M., Young N.D., Holmes D., Chavan M., Risso C., Kiss H.E.,
RA   Han C.S., Land M.L., Lovley D.R.;
RT   "The genome of Geobacter bemidjiensis, exemplar for the subsurface
RT   clade of Geobacter species that predominate in Fe(III)-reducing
RT   subsurface environments.";
RL   BMC Genomics 11:490-490(2010).
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:SAAS00561307}.
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DR   EMBL; CP001124; ACH39071.2; -; Genomic_DNA.
DR   STRING; 404380.Gbem_2058; -.
DR   EnsemblBacteria; ACH39071; ACH39071; Gbem_2058.
DR   KEGG; gbm:Gbem_2058; -.
DR   eggNOG; ENOG4105BZT; Bacteria.
DR   eggNOG; COG2265; LUCA.
DR   HOGENOM; HOG000029870; -.
DR   KO; K03215; -.
DR   Proteomes; UP000008825; 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; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR11061; PTHR11061; 1.
DR   Pfam; PF01938; TRAM; 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; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B5ECN6.
DR   SWISS-2DPAGE; B5ECN6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008825};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01024,
KW   ECO:0000256|SAAS:SAAS00234999, ECO:0000313|EMBL:ACH39071.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008825};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01024,
KW   ECO:0000256|SAAS:SAAS00235009};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01024,
KW   ECO:0000256|SAAS:SAAS00506843, ECO:0000313|EMBL:ACH39071.2}.
FT   DOMAIN        3     61       TRAM. {ECO:0000259|PROSITE:PS50926}.
FT   ACT_SITE    401    401       {ECO:0000256|PROSITE-ProRule:PRU10015}.
FT   ACT_SITE    401    401       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01024}.
FT   BINDING     278    278       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   BINDING     307    307       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01024}.
FT   BINDING     328    328       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   BINDING     376    376       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
SQ   SEQUENCE   444 AA;  47496 MW;  7DD32526CC616FFA CRC64;
     MWSAATVAEA VVEIERLCYG GAGFGRIDGK ACFVPLTAPG DKARVRVVKE KRSFAEAEVV
     ELLEPSPLRT DPACPYFGVC GGCDWQHLPY AEQLKQKGEI FADTLARIGK VPRELVLPVS
     PSPECFGYRS RIQLKVARKG GIPTLGFFKR GSHDVVDLAA GCALAAPLLN QALAEVRGIL
     PRLPQLEGIT QVDLAMGDDG ESIAVFHYRG KDAASLLDCL LAARPELPSV TGAYVKTGEK
     GEMSAVFGVD SLSYGVPAGL FPGSREVRLR FSRGGFSQVN YRQNLELIKT VGEWGALREG
     ARVLDLYCGN GNISVPIAPL VGEVVGVEGY APSIVDAAAN AEANGALNAR YLVGDAALSV
     RRLAKRKEKF DLVVLDPPRA GAEAAGELAI LAPERILYVS CDPATLARDL GQLCGAGYRV
     ARSKPVDMFP QTYHLESVTE LIRD
//

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