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Database: UniProt
Entry: C6Y303_PEDHD
LinkDB: C6Y303_PEDHD
Original site: C6Y303_PEDHD 
ID   C6Y303_PEDHD            Unreviewed;       387 AA.
AC   C6Y303;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Fmu (Sun) domain protein {ECO:0000313|EMBL:ACU03216.1};
GN   OrderedLocusNames=Phep_0995 {ECO:0000313|EMBL:ACU03216.1};
OS   Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457
OS   / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU03216.1, ECO:0000313|Proteomes:UP000000852};
RN   [1] {ECO:0000313|EMBL:ACU03216.1, ECO:0000313|Proteomes:UP000000852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
RC   NCIMB 9290 / NRRL B-14731 / HIM 762-3
RC   {ECO:0000313|Proteomes:UP000000852};
RX   PubMed=21304637; DOI=10.4056/sigs.22138;
RA   Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA   Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O.,
RA   Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Pedobacter heparinus type strain (HIM 762-
RT   3).";
RL   Stand. Genomic Sci. 1:54-62(2009).
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; CP001681; ACU03216.1; -; Genomic_DNA.
DR   RefSeq; WP_012781160.1; NZ_AQGK01000003.1.
DR   AlphaFoldDB; C6Y303; -.
DR   STRING; 485917.Phep_0995; -.
DR   KEGG; phe:Phep_0995; -.
DR   eggNOG; COG0144; Bacteria.
DR   HOGENOM; CLU_713402_0_0_10; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000000852; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
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; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF77; SUN PROTEIN; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
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:UP000000852};
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          120..387
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        341
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         241
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         268
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"
SQ   SEQUENCE   387 AA;  44695 MW;  873CB664337002E6 CRC64;
     MRVEHQLRAF EQIFKSYDGV LPLHRFLFAY FKRNKQMGSS DRRWASRYLY NFFRLGKALI
     KEEYTLRLAV ADFLCSHTSS LVIDTYLPGL KDQVVLSLPE KLALIKQQYP SFELDDVFSF
     HHKLSAGIDQ QDFVPSFFIQ PDLFIRVDTG YIEKVAATLR LEEIDFEKIS ETTLALPNGT
     KLDSVLAAHK QYQVQDLSSQ QTGSFFKPQA WDKWWDCCAA SGGKSLLLYD LEPKVELLVS
     DVRESSLHNL DERFQQAGLK KYQKKVLDLL QNNEQDLHHY EFDGILLDAP CSGSGTWGRT
     PEMLYYFEDH KISYFSGLQK KIAANVVKYL KEGKPLIYIT CSVFKEENED VVAFLLENLP
     LKLEKMQVIK GYAAKADTMF VARLIKQ
//
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