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Database: UniProt
Entry: A0A0D2VE67_GOSRA
LinkDB: A0A0D2VE67_GOSRA
Original site: A0A0D2VE67_GOSRA 
ID   A0A0D2VE67_GOSRA        Unreviewed;       570 AA.
AC   A0A0D2VE67;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=B456_013G151300 {ECO:0000313|EMBL:KJB81596.1};
OS   Gossypium raimondii (New World cotton).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB81596.1, ECO:0000313|Proteomes:UP000032304};
RN   [1] {ECO:0000313|EMBL:KJB81596.1, ECO:0000313|Proteomes:UP000032304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23257886; DOI=10.1038/nature11798;
RA   Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA   Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA   Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA   Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA   Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA   Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA   Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA   Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA   ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA   Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA   Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA   Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA   Wang X., Schmutz J.;
RT   "Repeated polyploidization of Gossypium genomes and the evolution of
RT   spinnable cotton fibres.";
RL   Nature 492:423-427(2012).
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}.
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DR   EMBL; CM001752; KJB81596.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2VE67; -.
DR   SMR; A0A0D2VE67; -.
DR   STRING; 29730.A0A0D2VE67; -.
DR   EnsemblPlants; KJB81596; KJB81596; B456_013G151300.
DR   Gramene; KJB81596; KJB81596; B456_013G151300.
DR   eggNOG; KOG1122; Eukaryota.
DR   OMA; ITACEKP; -.
DR   Proteomes; UP000032304; Chromosome 13.
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; 1.
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:UP000032304};
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          233..522
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..88
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..547
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..563
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        452
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         325..331
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         349
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         376
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         395
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   570 AA;  64170 MW;  C8E8512D610B5AFD CRC64;
     MASNKSKGAK SKNQPPKKKQ RNDLFIDKKR PAKKDEVLDD VSDGHSEEEE EAGDLLDGDE
     QMSDFDDDDV SEISDEDDAP WADDFLQGSD DNEDTHFDSG SSSTSGSGSD SHSDETDIEE
     KSRAIDEQRA REEEDAQAEM ELNIKEESDE FRLPTKEELE AEQQRPPDLA NLQMRMKEIV
     RVLSNFKHMR QEGTTRKDYI DQLKIDLGSY YGYNEFLIRV LVDMFPVVEL MELIEAFEKP
     RPTCIRTNTL RTRRRDLADV LSKRGVELDQ LSKWSKVGLV VYNSHVPIGA TPEYLAGFYY
     IQGASSFLPV MALAPQEKER VVDMAAAPGG KTTYVAALMK NSGIIYANEI REARLKSLTA
     NLHRMGVTNT IVCNYDGREL PKVLGQNSVD RVLLDAPCSG TGVITKDPSV KTSKSLDDIQ
     KCAHLQKQLI LAAIDMVDAN SKSGGYIVYS TCSIMVPENE AVSDYALKKR DVKVVPCGLD
     FGSPGYIRFR EHRFHTSLEN TRRFYPHVHN MDGFFVAKLK KMSNAKKNPV NSEDLETVVQ
     TQRPENTPID KDNTEELKQN LKKQGNKGKM
//
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