(data stored in ACNUC8465 zone)

SWISSPROT: C7N4X3_SLAHD

ID   C7N4X3_SLAHD            Unreviewed;       441 AA.
AC   C7N4X3;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:ACV21958.1};
GN   OrderedLocusNames=Shel_09160 {ECO:0000313|EMBL:ACV21958.1};
OS   Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029
OS   / RHS 1) (Peptococcus heliotrinreducens).
OC   Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales;
OC   Eggerthellaceae; Slackia.
OX   NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV21958.1, ECO:0000313|Proteomes:UP000002026};
RN   [1] {ECO:0000313|EMBL:ACV21958.1, ECO:0000313|Proteomes:UP000002026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1
RC   {ECO:0000313|Proteomes:UP000002026};
RX   PubMed=21304663; DOI=10.4056/sigs.37633;
RA   Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T.,
RA   Lucas S., Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Kuske C., Brettin T., Detter J.C., Han C., Pitluck S.,
RA   Pati A., Mavrommatis K., Ivanova N., Ovchinnikova G., Chen A.,
RA   Palaniappan K., Schneider S., Rohde M., Chain P., D'haeseleer P.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C.,
RA   Klenk H.P., Hugenholtz P.;
RT   "Complete genome sequence of Slackia heliotrinireducens type strain
RT   (RHS 1).";
RL   Stand. Genomic Sci. 1:234-241(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:SAAS00561307}.
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DR   EMBL; CP001684; ACV21958.1; -; Genomic_DNA.
DR   RefSeq; WP_012798062.1; NC_013165.1.
DR   STRING; 471855.Shel_09160; -.
DR   EnsemblBacteria; ACV21958; ACV21958; Shel_09160.
DR   KEGG; shi:Shel_09160; -.
DR   eggNOG; ENOG4105BZT; Bacteria.
DR   eggNOG; COG2265; LUCA.
DR   HOGENOM; HOG000029870; -.
DR   OMA; FYAGDMK; -.
DR   OrthoDB; 1421660at2; -.
DR   BioCyc; SHEL471855:G1GFK-911-MONOMER; -.
DR   Proteomes; UP000002026; 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; 2.
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; C7N4X3.
DR   SWISS-2DPAGE; C7N4X3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002026};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01024,
KW   ECO:0000256|SAAS:SAAS00234999, ECO:0000313|EMBL:ACV21958.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002026};
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:ACV21958.1}.
FT   DOMAIN        1     55       TRAM. {ECO:0000259|PROSITE:PS50926}.
FT   ACT_SITE    396    396       {ECO:0000256|PROSITE-ProRule:PRU10015}.
FT   ACT_SITE    396    396       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01024}.
FT   BINDING     276    276       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   BINDING     305    305       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01024}.
FT   BINDING     326    326       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   BINDING     369    369       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
SQ   SEQUENCE   441 AA;  47782 MW;  7DD91D677DD7D51B CRC64;
     MSEQITIERL LYGDAGIGHL SDGRAAFVDG ACPGDVLEVA VEKDNGNYLT CSIKEIVSLS
     EHRVTPKCPL ASVCGGCGWQ HVAYDWQLVE KRANVVSQLQ RTAHFDPDRA EAIVAECKPS
     PKQFGYRNKL EFGCQIDPKR GFLMGLHRRG SDDVLPVDSC PLAQGPLSKT PKALKGALRY
     LSGSNDLGIY RVGVRQSART RSTEIALWTT PGPFPRATVA KTLGNAMKCT SIVRVMTGEG
     KKARKLKGVE LLAGDGYWKE RVAGQPFKVS APSFFQVNTE QAETLVELAL DGLEIDEGSV
     VADLYCGVGT FTIPMAKTGA EVMAVESYGS SVRDLRRITE EEGLYIDVIG GDAARELPGL
     GHLDALLVDP PRAGLDATII PAIAAAGPRR LAYVSCDPAT WARDVKRLED QGFELVKATP
     VDMFPQTHHV EIVSIFTNRK N
//

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