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Database: UniProt
Entry: A0A1B6PJA7_SORBI
LinkDB: A0A1B6PJA7_SORBI
Original site: A0A1B6PJA7_SORBI 
ID   A0A1B6PJA7_SORBI        Unreviewed;       845 AA.
AC   A0A1B6PJA7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=SORBI_3007G225800 {ECO:0000313|EMBL:KXG25732.1};
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG25732.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:KXG25732.1, ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=19189423; DOI=10.1038/nature07723;
RA   Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA   Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA   Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA   Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA   Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA   Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA   Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA   Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT   "The Sorghum bicolor genome and the diversification of grasses.";
RL   Nature 457:551-556(2009).
RN   [2] {ECO:0000313|Proteomes:UP000000768}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX   PubMed=29161754; DOI=10.1111/tpj.13781;
RA   McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA   Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA   Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT   "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT   a transcriptome atlas, and signatures of genome organization.";
RL   Plant J. 93:338-354(2018).
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; CM000766; KXG25732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6PJA7; -.
DR   STRING; 4558.A0A1B6PJA7; -.
DR   EnsemblPlants; KXG25732; KXG25732; SORBI_3007G225800.
DR   Gramene; KXG25732; KXG25732; SORBI_3007G225800.
DR   eggNOG; KOG2198; Eukaryota.
DR   InParanoid; A0A1B6PJA7; -.
DR   OMA; YRTVNFA; -.
DR   OrthoDB; 197651at2759; -.
DR   Proteomes; UP000000768; Chromosome 7.
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:SF14; OS08G0484400 PROTEIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000000768};
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          103..529
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          50..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        367
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         221..227
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         253
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         314
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   845 AA;  95572 MW;  024EE8CFE8849310 CRC64;
     MLAARTPVSL HHRIVAGGQR GRCVGGSERR RGRAPCGQFA QALESLWRHS PWTHPPDPPA
     AAAGTATSGE AKPSRQPPVL ENAAFEEYYK VQQIVRKEEW DAFMNVLRKP LPVAFRINAC
     CQFYKDICSK LENEFRRSLE SEVSNEHGED AIAPLPWYPC NLAWHLNFSR KELRKNQALE
     SFHEFLKHES EVGNITRQEA VSMVPPLFLN VQPDHHILDM CAAPGSKTFQ LLEIIHLSKE
     PGLLPGALVI ANDLNVRRCD LLIHNTKRMC TASLIVTNHE AENFPYCSLA KDYLESYKDP
     CKLQRLEFDR ILCDVPCSGD GTIRKGHDMW RKWNSGMGNQ LHLLQVNIAM RGIALLKVGG
     RMVYSTCSMN PVENEAVIAE LLRRSGNSVE LLDVSSELPE LVRRPGLTTW KVQDRESWFQ
     SHNEVPHNRK NVVLPSMFPA SNCTTEESHT VCGDVEVNMD NMSSFSRNIN IEETKKVNHH
     MDGVSISPNK ILDCTSNIVS SKFPLHRCMR IVPHDQNSGA FFIAVLHKLS PLNGSQIKGT
     KIQHTLGTDR IMQFQKEPEP ETRTYETILT LQQHNVSEVD TEMLGRRQNL STDSQPSKDK
     NSTEVEMVFS DIESTQVESG DIMKLQKQSR WKGVDPVLFL NDEAMIKNVI SFFGIKESFP
     LEGHLVTRST DNARRIYYVS KSVKEILELN AEVGGQLKIA SLGVKMFERH RSKVACPCAY
     RLSYEGLSLL LPYIRKRILY ASPIDFHRLL QYRSINFAHF LDTRFGEQAA SLMLGCCVVV
     LLEGHKHVDS ISKDPSTIAI VCWRGKGTMN VMVSPSDRKD LLERMVYGFG LKDCVEEDEK
     ILSQG
//
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