ID V4NI93_9CAUL Unreviewed; 457 AA.
AC V4NI93;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=rRNA methyltransferase {ECO:0000313|EMBL:ESQ75781.1};
GN ORFNames=ABAC402_07385 {ECO:0000313|EMBL:ESQ75781.1};
OS Asticcacaulis sp. AC402.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282361 {ECO:0000313|EMBL:ESQ75781.1, ECO:0000313|Proteomes:UP000017812};
RN [1] {ECO:0000313|EMBL:ESQ75781.1, ECO:0000313|Proteomes:UP000017812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC402 {ECO:0000313|EMBL:ESQ75781.1,
RC ECO:0000313|Proteomes:UP000017812};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ESQ75781.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWGC01000013; ESQ75781.1; -; Genomic_DNA.
DR AlphaFoldDB; V4NI93; -.
DR STRING; 1282361.ABAC402_07385; -.
DR PATRIC; fig|1282361.3.peg.1433; -.
DR eggNOG; COG0144; Bacteria.
DR eggNOG; COG0781; Bacteria.
DR OrthoDB; 9810297at2; -.
DR Proteomes; UP000017812; Unassembled WGS sequence.
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; IPR018314; Fmu/NOL1/Nop2p_CS.
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; PS01153; NOL1_NOP2_SUN; 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:UP000017812};
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}.
FT DOMAIN 164..455
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 270..276
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 291
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 317
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 333
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 457 AA; 49743 MW; 4FD46B5D0F98A789 CRC64;
MNKPRPAKKP LQKSRPRPPR PEPERIDDGG DIGMNARLAA LTLIDAALAK RTGFDEAVTR
SDFLDLSDSE RGFARALAML VLRRLGQLDY IIEKKTQKAP NDGVWALLRI GLAQIGFMQV
PDFAAVSTTV KLAEREAHTR PFKGLINAIL RSVIREGGLN KPLPSRLAPD WLFQRWKAAY
GEANAEGIAL MLTEEPATDL TFKTAADLDR LKDDLQGEPL GGLALRSSLR GNIAEWAGYG
EGVWWVQDAA ASVGAGLLGD LTGKTAIDLC AAPGGKALQM IAAGAEVIAL DRSKNRLKRV
EENLIRTGMT ADVVMGDAET WEDRRQFDAV LLDAPCSATG TLRRQPDVLW ATRPTDIAKL
ADVQHRLLDS AGGRVKPGGS LVYCTCSLER EEGETQVLAF LRRHPDFAIQ KPEDATVAAL
GIPVESVAQQ GWLRLLPHHR PGGQDGFFIA HLVRQNG
//