ID A0A2P4TBU0_BAMTH Unreviewed; 680 AA.
AC A0A2P4TBU0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN ORFNames=CIB84_002409 {ECO:0000313|EMBL:POI33839.1};
OS Bambusicola thoracicus (Chinese bamboo-partridge) (Perdix thoracica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Bambusicola.
OX NCBI_TaxID=9083 {ECO:0000313|EMBL:POI33839.1, ECO:0000313|Proteomes:UP000237246};
RN [1] {ECO:0000313|EMBL:POI33839.1, ECO:0000313|Proteomes:UP000237246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RTK389 {ECO:0000313|EMBL:POI33839.1};
RC TISSUE=Blood {ECO:0000313|EMBL:POI33839.1};
RA Tiley G.P., Kimball R.T., Braun E.L., Burleigh J.G.;
RT "Comparison of the Chinese Bamboo Partridge and Red Junglefowl genome
RT sequences highlights the importance of demography in genome evolution.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
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:POI33839.1}.
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DR EMBL; PPHD01002811; POI33839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P4TBU0; -.
DR Proteomes; UP000237246; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023273; RCMT_NOP2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00446; nop2p; 1.
DR PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 2.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02012; RCMTNOP2.
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:UP000237246};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
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 267..587
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..121
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..671
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 517
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 359..365
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 416
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 443
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 460
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 680 AA; 75979 MW; BE1617E59E2B6A34 CRC64;
MGRKLDPTRK EKRGPGRKAR KQRGAEVELA RFLPPVKEQG DPQEEGSPVK TAGQAPQHRP
GFKDDNAKWL TPAKGKKSLS KKTSVELSSS GEVEEDSWEM EEEEEDGSSE ELMDDYGASS
SEEEELLPIE KAALKQKADN GDLSEDDSEE DEVAEETSRQ KTEQKEKEDT DLQLNLEIDE
EFKLPTDEQI EKENILSICS IYLHVIHQRI KSNMEVLQNF GVKREEGRTR QEYLALLRRD
MAAYYSYSDF LLKMLMDIFP LPELINFLEA NEVPRPVTIR TNTLKTRRRD LAQALINRGV
NLDPLGKWSK TGLVIYDSSV PIGATPEYLA GHYMLQGASS LLPVMALAPQ ENERILDMCC
APGGKTSYIG GENGMGLNSG KGVYLGTSIE GFQSLADVFP LAAQLMKNTG MILANDNNAE
RLRSVVGNLH RLGVTNAVVS NCDGRQFPKV LGGFDRVLLD APCSGTGVIS KDPAIKTNKD
EKDIMRCAHL QKELLLSAID SVNATSETGG YIVYCTCSIT VEENEWVVDY ALKKRNVRLV
ATGLDFGKEG FTRFKDRRFH PSLKSTRRFY PHTHNMDGFF IAKLKKFSNA IPKTQKDEEP
AADATNPSTG PETVTEPQAK KKKLEESKIA EEQKKPQPAL KNRHSLQGQR RPLKAVRPSP
HKSHAPVPNR KKQRVKQNGQ
//
