ID E8U963_DEIML Unreviewed; 420 AA.
AC E8U963;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=NusB/RsmB/TIM44 {ECO:0000313|EMBL:ADV67602.1};
DE Flags: Precursor;
GN OrderedLocusNames=Deima_1957 {ECO:0000313|EMBL:ADV67602.1};
OS Deinococcus maricopensis (strain DSM 21211 / LMG 22137 / NRRL B-23946 /
OS LB-34).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=709986 {ECO:0000313|EMBL:ADV67602.1, ECO:0000313|Proteomes:UP000008635};
RN [1] {ECO:0000313|EMBL:ADV67602.1, ECO:0000313|Proteomes:UP000008635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC {ECO:0000313|Proteomes:UP000008635};
RX PubMed=21677853; DOI=10.4056/sigs.1633949;
RA Pukall R., Zeytun A., Lucas S., Lapidus A., Hammon N., Deshpande S.,
RA Nolan M., Cheng J.F., Pitluck S., Liolios K., Pagani I., Mikhailova N.,
RA Ivanova N., Mavromatis K., Pati A., Tapia R., Han C., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brambilla E.M., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Deinococcus maricopensis type strain (LB-
RT 34).";
RL Stand. Genomic Sci. 4:163-172(2011).
RN [2] {ECO:0000313|Proteomes:UP000008635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21211 / LMG 22137 / NRRL B-23946 / LB-34
RC {ECO:0000313|Proteomes:UP000008635};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Kyrpides N.,
RA Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Zeytun A.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Pukall R., Gehrich-Schroeter G.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Deinococcus maricopensis DSM 21211.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR EMBL; CP002454; ADV67602.1; -; Genomic_DNA.
DR RefSeq; WP_013557107.1; NC_014958.1.
DR AlphaFoldDB; E8U963; -.
DR STRING; 709986.Deima_1957; -.
DR KEGG; dmr:Deima_1957; -.
DR eggNOG; COG0144; Bacteria.
DR eggNOG; COG0781; Bacteria.
DR HOGENOM; CLU_005316_0_4_0; -.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000008635; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 1.10.940.10; NusB-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR035926; NusB-like_sf.
DR InterPro; IPR006027; NusB_RsmB_TIM44.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF01029; NusB; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF48013; NusB-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000008635};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..420
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003228485"
FT DOMAIN 136..416
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 357
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 288
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 304
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 420 AA; 43999 MW; C0EACBA15D214798 CRC64;
MTDAPTRAPR RANPARAVAV RVLARVLGGA FAAPTLDEAL AHARLPARDA GLATHIVYGA
LRHAPTLLPA LDALLKGSTP IKARALLLAG AFEKLVLGTA PHAAVSEYVT LARDGFASPG
LVNAVLRRVD VAPDASPYAL PSWLEQEFRT AFGEVAPDAM LDQLQPSPLW LYLDDAGVRA
LDEEGSAVEG GRGDVYRVAL DRPLRETRAY RTGHAQPINP ASHACVLALG DVDGLPVLDL
AGGAGVKAAM LARRGARVTS VDKIAGKHRA ARENLARLGV QAQFVTADLT RPLNAPPAPL
VLLDAPCTGS GTLRAHPEIK LRLTEPAVGE MAALQRTLLT RAADLVQPGG TLVYSVCSLA
DAEGPQVAAA FLAEHPDFQA EALPDLHVPV VQAGPGVRTV PVEGVDGFFI VRLHRRAQGA
//
