(data stored in SCRATCH zone)

SWISSPROT: C8VVF2_DESAS

ID   C8VVF2_DESAS            Unreviewed;       159 AA.
AC   C8VVF2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase H {ECO:0000256|HAMAP-Rule:MF_00658, ECO:0000256|SAAS:SAAS01091420};
DE            EC=2.1.1.177 {ECO:0000256|HAMAP-Rule:MF_00658, ECO:0000256|SAAS:SAAS01091423};
DE   AltName: Full=23S rRNA (pseudouridine1915-N3)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00658};
DE   AltName: Full=23S rRNA m3Psi1915 methyltransferase {ECO:0000256|HAMAP-Rule:MF_00658};
DE   AltName: Full=rRNA (pseudouridine-N3-)-methyltransferase RlmH {ECO:0000256|HAMAP-Rule:MF_00658};
GN   Name=rlmH {ECO:0000256|HAMAP-Rule:MF_00658};
GN   OrderedLocusNames=Dtox_0073 {ECO:0000313|EMBL:ACV61036.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61036.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61036.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Specifically methylates the pseudouridine at position
CC       1915 (m3Psi1915) in 23S rRNA. {ECO:0000256|HAMAP-Rule:MF_00658,
CC       ECO:0000256|SAAS:SAAS01091432}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pseudouridine(1915) in 23S rRNA + S-adenosyl-L-methionine
CC         = H(+) + N(3)-methylpseudouridine(1915) in 23S rRNA + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:42752, Rhea:RHEA-
CC         COMP:10221, Rhea:RHEA-COMP:10222, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65314,
CC         ChEBI:CHEBI:74486; EC=2.1.1.177; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00658, ECO:0000256|SAAS:SAAS01125024};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00658,
CC       ECO:0000256|SAAS:SAAS01091414}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00658,
CC       ECO:0000256|SAAS:SAAS01091434}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase RlmH family.
CC       {ECO:0000256|HAMAP-Rule:MF_00658, ECO:0000256|SAAS:SAAS01091436}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00658}.
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DR   EMBL; CP001720; ACV61036.1; -; Genomic_DNA.
DR   RefSeq; WP_012813488.1; NC_013216.1.
DR   STRING; 485916.Dtox_0073; -.
DR   EnsemblBacteria; ACV61036; ACV61036; Dtox_0073.
DR   KEGG; dae:Dtox_0073; -.
DR   eggNOG; ENOG4108UXA; Bacteria.
DR   eggNOG; COG1576; LUCA.
DR   HOGENOM; HOG000218433; -.
DR   KO; K00783; -.
DR   OMA; NGEPYHK; -.
DR   OrthoDB; 1783583at2; -.
DR   BioCyc; DACE485916:G1GFV-77-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070038; F:rRNA (pseudouridine-N3-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_00658; 23SrRNA_methyltr_H; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR003742; RlmH-like.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   PANTHER; PTHR33603; PTHR33603; 1.
DR   Pfam; PF02590; SPOUT_MTase; 1.
DR   PIRSF; PIRSF004505; MT_bac; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00246; tRNA_RlmH_YbeA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VVF2.
DR   SWISS-2DPAGE; C8VVF2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00658,
KW   ECO:0000256|SAAS:SAAS01091416};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00658,
KW   ECO:0000256|SAAS:SAAS01091417};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00658,
KW   ECO:0000256|SAAS:SAAS01091427};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00658,
KW   ECO:0000256|SAAS:SAAS01091425};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00658,
KW   ECO:0000256|SAAS:SAAS01091419}.
FT   BINDING      76     76       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00658}.
FT   BINDING     108    108       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00658}.
SQ   SEQUENCE   159 AA;  18421 MW;  A7C136F7564626CA CRC64;
     MHINILAVGK LKEKYWTESQ NEYLKRLRAY AKCEVKEVVD ERFAPSVMSR EIEQVKNREG
     KRLQSLIDET SYLIALDCRG KMLESEEFAG MLKNLALTGK SNVSFIIGGS LGLSGELLSR
     ADFLLSFSRF TFPHQLMRVI LLEQIFRSFK IIKNEPYHR
//

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