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Database: UniProt
Entry: A6WCA8_KINRD
LinkDB: A6WCA8_KINRD
Original site: A6WCA8_KINRD 
ID   A6WCA8_KINRD            Unreviewed;       486 AA.
AC   A6WCA8;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Fmu (Sun) domain protein {ECO:0000313|EMBL:ABS04447.1};
GN   OrderedLocusNames=Krad_2983 {ECO:0000313|EMBL:ABS04447.1};
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC   Kineococcus.
OX   NCBI_TaxID=266940 {ECO:0000313|EMBL:ABS04447.1, ECO:0000313|Proteomes:UP000001116};
RN   [1] {ECO:0000313|Proteomes:UP000001116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216
RC   {ECO:0000313|Proteomes:UP000001116};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Bagwell C.E., Shimkets L., Berry C.J.,
RA   Fliermans C., Richardson P.;
RT   "Complete sequence of chromosome of Kineococcus radiotolerans SRS30216.";
RL   Submitted (JUL-2007) 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}.
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DR   EMBL; CP000750; ABS04447.1; -; Genomic_DNA.
DR   RefSeq; WP_012087306.1; NC_009664.2.
DR   AlphaFoldDB; A6WCA8; -.
DR   STRING; 266940.Krad_2983; -.
DR   KEGG; kra:Krad_2983; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   HOGENOM; CLU_005316_0_3_11; -.
DR   Proteomes; UP000001116; 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:UP000001116};
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          188..485
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        415
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         293..299
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         318
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         344
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         362
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   486 AA;  51303 MW;  5B7FE938522BCC49 CRC64;
     MTGPKLGTGQ QRTPRSGVKQ DRFTRVDASR KVAYEVLRAV SADDAYANLV LPRMLRDRRL
     NGRDAAFATE LAYGVLRGRG TYDALLATLV DRPLAELDAG VLDVLRMGLH QLLAMRVPDH
     AAVATSVALA RNVVGGGPAG LINAVLRSAA GRDLDTWVAE VATTGNEDDD LAVRYSHPQW
     IVRSLREALR AHGHEAAELT DLLVADNTPA QVAVAALPGL SEPADLVRRA SFLEVVPGRW
     SATAVQLVHG DPGQLSLVRE GRARVQDEGS QIVAQLLAAA ALEGRDERWL DLCAGPGGKA
     ALLAATAAQR GARLTAVEVA PHRAELVRSA LAAVPGGAEV RVGDGREVGA DEPAAYDRVL
     VDAPCTGLGA LRRRPEARWR RTPADLGALG PLQRDLLASA LDAVRPGGVV AYATCSPVLS
     ETRLVVDDAV KAAAKRGVVV QRLDTPAVLE QVVPGMPSAA AGRAVQLWPH THGTDAMHVA
     LLRRES
//
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