ID I1IQZ1_BRADI Unreviewed; 880 AA.
AC I1IQZ1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN Name=100833836 {ECO:0000313|EnsemblPlants:KQJ90616};
GN ORFNames=BRADI_4g32840v3 {ECO:0000313|EMBL:KQJ90616.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EMBL:KQJ90616.1};
RN [1] {ECO:0000313|EMBL:KQJ90616.1, ECO:0000313|EnsemblPlants:KQJ90616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ90616.1,
RC ECO:0000313|EnsemblPlants:KQJ90616};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQJ90616.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQJ90616.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQJ90616}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ90616};
RG EnsemblPlants;
RL Submitted (AUG-2018) to UniProtKB.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR EMBL; CM000883; KQJ90616.1; -; Genomic_DNA.
DR RefSeq; XP_003578274.1; XM_003578226.3.
DR AlphaFoldDB; I1IQZ1; -.
DR STRING; 15368.I1IQZ1; -.
DR EnsemblPlants; KQJ90616; KQJ90616; BRADI_4g32840v3.
DR GeneID; 100833836; -.
DR Gramene; KQJ90616; KQJ90616; BRADI_4g32840v3.
DR KEGG; bdi:100833836; -.
DR eggNOG; KOG2198; Eukaryota.
DR HOGENOM; CLU_005316_4_4_1; -.
DR InParanoid; I1IQZ1; -.
DR OMA; QLFTEYV; -.
DR OrthoDB; 197651at2759; -.
DR Proteomes; UP000008810; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
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; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008810};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 82..529
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 346
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 200..206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 880 AA; 98272 MW; DE595408B6622620 CRC64;
MGGGRKRGRS QRRHFKQGRE NVWKDNPQRP PAGGGGGDQG AAGSGEGREG NDSWQPFSTE
NPAFEAYYKE QQIVPEEEWN DFMSMLRKPL PAAFRINASC QFYQDICSQL ENDFRKSLET
EVSDEHEKDA IRPLPWYPGN LAWHLNFSRM QLRRNQALES FHEFLKQENE VGNITRQEAV
SMVPPLFLNV QPDHHILDMC AAPGSKTFQL LEMIHQSTKP GVLPNAMVVA NDVDVQRCNL
LIHQTKRMCT ANLIVTNHEA QNFPGCSLTK FCPETYLDES KPQRLEFDRV LCDVPCSGDG
TVRKAPDMWR KWNAGMGNGL HRLQVEIAMR GIALLKVGGR MVYSTCSMNP VENEAVVAEI
LRRCGDSVEL LDVSNELPEL VRRPGLSTWK VRDRGSWLGT HEDVLHYRKN AISPSMFPSG
KGSTDNRKVG GSGELNMDVA DADMDSGDMV ERKEESRIAI NGSNNGETNI EEINQVESES
GEVPRDSEKK SDSTSICTEH SNLPLHRCMR IVPHDQNSGA FFIAVLQKLS VLNENQVVEV
MKGEHSILKD RAVKPVDSPG SDKVPSEEIP VHQQGVEGSH VSGKQQNGDM DAISKDKASE
EGSVIVNETQ NDEAATRDKR KTQNQGRWRG VDPVIFFRDE ATITSIVSFY GIKDSFTLEG
HLVTRNPDTN HVKRIYYVSK SVQDVLELNV KVGERLKITS LGLKIFERQS SKDGSPCTFR
LSSEGLPLLL PYITKQILYA SALDFQHLLQ YRIIKFPDFV DAKFGEEASA LLPGCCVVVL
REGHQHIDSI ATDPSAIAIV CWKGKTNLCV MVSPLDGKEL LERVSLRFGL KVPKADDRKT
KLKVDGSDEQ LDCGAETVDP ECKPESKASD MDISDVKEVE
//
