GenomeNet

Database: UniProt
Entry: A0A2H3NNI5_9BACT
LinkDB: A0A2H3NNI5_9BACT
Original site: A0A2H3NNI5_9BACT 
ID   A0A2H3NNI5_9BACT        Unreviewed;       434 AA.
AC   A0A2H3NNI5;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=16S rRNA (cytosine(967)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00012140};
DE            EC=2.1.1.176 {ECO:0000256|ARBA:ARBA00012140};
DE   AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000256|ARBA:ARBA00030399};
DE   AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000256|ARBA:ARBA00031088};
GN   Name=rsmB {ECO:0000313|EMBL:PEN06553.1};
GN   ORFNames=CRI93_09750 {ECO:0000313|EMBL:PEN06553.1};
OS   Longimonas halophila.
OC   Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salisaetaceae;
OC   Longimonas.
OX   NCBI_TaxID=1469170 {ECO:0000313|EMBL:PEN06553.1, ECO:0000313|Proteomes:UP000221024};
RN   [1] {ECO:0000313|EMBL:PEN06553.1, ECO:0000313|Proteomes:UP000221024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42399 {ECO:0000313|EMBL:PEN06553.1,
RC   ECO:0000313|Proteomes:UP000221024};
RA   Goh K.M., Shamsir M.S., Lim S.W.;
RT   "Draft genome of Longimonas halophila.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC       of 16S rRNA. {ECO:0000256|ARBA:ARBA00002724}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC         methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42748, Rhea:RHEA-COMP:10219, Rhea:RHEA-COMP:10220,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.176;
CC         Evidence={ECO:0000256|ARBA:ARBA00000588};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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}.
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:PEN06553.1}.
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; PDEP01000008; PEN06553.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3NNI5; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000221024; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; 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; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00563; rsmB; 1.
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:UP000221024};
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          161..432
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        373
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         276
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         301
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         320
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   434 AA;  47757 MW;  E7567988DE844385 CRC64;
     MADSTVSSAR QLAYRALTRI DQTEAYVDQV DIGGTPRQRR QARDVVAGVT RQQRWLWFLI
     TQLYNGTPND LEPAVVRILK MGLYELLFQA TPARAAVHQY VELAKDVVGK RVAGLVNGIL
     RTADRQRDDL PQPDTGDPER DLAIRTSMPT WLVRRWAEAR GLAKTEALLH RLNERPTYAL
     HLFDVTPADL DDLGVAWTPS PYVDGMVRVE ALQPVVQAGW LDEGRVMVQG EGAALVVDLL
     DPQPGDTVLD LCAAPGTKTR SIAHRMNGQG RVWANDHSAH RLQALQEAPG APGIIETHTA
     DARTLTPEDA PDAPTHVLLD VPCTGTGVLG RRADLRWRRT PNDVQELVAL QDELLEAAAR
     LVPPEGILVY STCSLLPQEN EERVQAFLDR HSDFEVAPPA HLPSDVQHNG FLQTDPVAHG
     TDGAFGARLR RTAA
//
DBGET integrated database retrieval system