ID B8HE98_PSECP Unreviewed; 375 AA.
AC B8HE98;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumB {ECO:0000313|EMBL:ACL39133.1};
GN OrderedLocusNames=Achl_1142 {ECO:0000313|EMBL:ACL39133.1};
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Pseudarthrobacter.
OX NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL39133.1, ECO:0000313|Proteomes:UP000002505};
RN [1] {ECO:0000313|EMBL:ACL39133.1, ECO:0000313|Proteomes:UP000002505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 /
RC NCIMB 13794 / A6 {ECO:0000313|Proteomes:UP000002505};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
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DR EMBL; CP001341; ACL39133.1; -; Genomic_DNA.
DR RefSeq; WP_015936356.1; NC_011886.1.
DR AlphaFoldDB; B8HE98; -.
DR STRING; 452863.Achl_1142; -.
DR KEGG; ach:Achl_1142; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_0_0_11; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000002505; Chromosome.
DR GO; GO:0016436; F:rRNA (uridine) methyltransferase activity; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR011825; 23SrRNA_MeTrfase_RlmC.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR030391; MeTrfase_TrmA_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010280; U5_MeTrfase_fam.
DR NCBIfam; TIGR02085; meth_trns_rumB; 1.
DR PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
DR PROSITE; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01024}.
FT ACT_SITE 333
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 211
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 306
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 375 AA; 41260 MW; 54DEFD2448FD7244 CRC64;
MHCSYFDAAR CRSCTLMGTP YGEQLAGKQA HCQTLLADHT ALEWLEPVAS QESAFRNKAK
MVISGTARNP TIGILDAEAH GIDLRKCGVC SPGLRAVFPV VAAFIRTHRL TPYDVPNRSG
ELKHLIVTES PDGEIMLRLV LRSEQLVPRI RKHLPDLLEA LPQVKVVSIN LHPEHKAVLE
GDREILLTEQ STLNMRVNDI NLHLRPQSFF QTNSHMAAAL YRQGREWVNE LAPASVWDLY
CGVGGFALHV ANPSRTVTGI ETSSEAIVSA RLSSDEAGLQ GMEFEAGDAT AFALAARQAP
DLVIVNPPRR GIGKELCGWL ESSDVQHVVY SSCNAQSLAR DLAALPSFTA RRVRVLDMFP
QTTHYEVMVL LERAG
//