(data stored in ACNUC7421 zone)

SWISSPROT: Q5LWH2_RUEPO

ID   Q5LWH2_RUEPO            Unreviewed;       417 AA.
AC   Q5LWH2;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 78.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase rumA {ECO:0000313|EMBL:AAV93360.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:AAV93360.1};
GN   Name=rumA {ECO:0000313|EMBL:AAV93360.1};
GN   OrderedLocusNames=SPO0029 {ECO:0000313|EMBL:AAV93360.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93360.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93360.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93360.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93360.1; -; Genomic_DNA.
DR   STRING; 246200.SPO0029; -.
DR   EnsemblBacteria; AAV93360; AAV93360; SPO0029.
DR   KEGG; sil:SPO0029; -.
DR   eggNOG; ENOG4107QS4; Bacteria.
DR   eggNOG; COG2265; LUCA.
DR   HOGENOM; HOG000029866; -.
DR   KO; K03215; -.
DR   OMA; FYAGDMK; -.
DR   Proteomes; UP000001023; 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; 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; SSF53335; SSF53335; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWH2.
DR   SWISS-2DPAGE; Q5LWH2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01024,
KW   ECO:0000256|SAAS:SAAS00234999, ECO:0000313|EMBL:AAV93360.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
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:AAV93360.1}.
FT   ACT_SITE    370    370       {ECO:0000256|PROSITE-ProRule:PRU10015}.
FT   ACT_SITE    370    370       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01024}.
FT   BINDING     249    249       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   BINDING     276    276       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01024}.
FT   BINDING     296    296       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
FT   BINDING     344    344       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01024}.
SQ   SEQUENCE   417 AA;  44163 MW;  BC849270B6DD43C2 CRC64;
     MPLYQAAMTQ EITITRLGHQ GDGIAPGPVY VPRSLPGEVV SGTPEGDRLA DMRVVTPSPH
     RVAPPCRHYR ACGGCQLQHA SDGFVAEWKQ EVVRAALAAQ GIEAVMRPVH TSPPQSRRRA
     TIAVRRTKKG ALAGFHGRAS DVITEIPDCH LLDPALLAAI PMAEALAMLG GSRKGVMAVT
     LTLSVAGLDV AVRGGKPLDG PLEVALGQLA EVQGLARLAW EDEVIAMRHP PAQNFGKAAV
     VPPPGAFLQA TRDGEQALLA AVRETIAGAR RVADLFAGCG TFALPLAETA EVHAVEGESA
     MTAALDRGWR RAQGLKRVTT EARDLFRRPL LPDELAAFDA VVLDPPRAGA EAQVAELARA
     KPPVIAYVSC NPVTFARDAK TLVQAGYSLN WVQVVDQFRW SAHVELAAAF SLAHIGG
//

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