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Database: UniProt
Entry: F0X979_GROCL
LinkDB: F0X979_GROCL
Original site: F0X979_GROCL 
ID   F0X979_GROCL            Unreviewed;       858 AA.
AC   F0X979;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=rRNA methyltransferase {ECO:0000313|EMBL:EFX06045.1};
GN   ORFNames=CMQ_4114 {ECO:0000313|EMBL:EFX06045.1};
OS   Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS   (Graphiocladiella clavigera).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX   NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN   [1] {ECO:0000313|EMBL:EFX06045.1, ECO:0000313|Proteomes:UP000007796}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX   PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA   DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA   Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA   Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA   Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT   "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT   symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP-
CC       Rule:MF_03163}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03163}.
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DR   EMBL; GL629735; EFX06045.1; -; Genomic_DNA.
DR   RefSeq; XP_014175527.1; XM_014320052.1.
DR   AlphaFoldDB; F0X979; -.
DR   STRING; 655863.F0X979; -.
DR   GeneID; 25977290; -.
DR   eggNOG; KOG1098; Eukaryota.
DR   HOGENOM; CLU_009422_8_1_1; -.
DR   InParanoid; F0X979; -.
DR   OrthoDB; 119516at2759; -.
DR   Proteomes; UP000007796; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   HAMAP; MF_03163; RNA_methyltr_E_SPB1; 1.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR012920; rRNA_MeTfrase_SPB1-like_C.
DR   InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR028589; SPB1-like.
DR   PANTHER; PTHR10920:SF13; PRE-RRNA 2'-O-RIBOSE RNA METHYLTRANSFERASE FTSJ3; 1.
DR   PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR   Pfam; PF11861; DUF3381; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF07780; Spb1_C; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_03163};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03163};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW   Rule:MF_03163}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_03163};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_03163};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03163}.
FT   DOMAIN          24..200
FT                   /note="Ribosomal RNA methyltransferase FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
FT   DOMAIN          234..390
FT                   /note="DUF3381"
FT                   /evidence="ECO:0000259|Pfam:PF11861"
FT   DOMAIN          640..854
FT                   /note="Ribosomal RNA methyltransferase SPB1-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07780"
FT   REGION          362..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          443..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..832
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..469
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..528
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..612
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        613..631
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..671
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         56
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         58
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
SQ   SEQUENCE   858 AA;  97155 MW;  A6CF04BF092DA62C CRC64;
     MAVQKKHGKG RLDKWYKLAK EKGYRARAAF KLIQLNKKYG FLEKSKVLLD LCAAPGSWCQ
     VAAETMPANS IIVGVDLSPI KSIPKVITFQ SDITTEKCRA TIRQHLKTWK ADTVLHDGAP
     NVGTAWVQDS FNQAELALQA MKLATDFLIE GGTFVTKVFR SKDYNSLLWV FNQLFTKVEA
     TKPPSSRNVS AEIFVVCRGF KAPKRIDPRF LDPKAVFAEL ADPTPNNEAK VYNPEVKKRK
     RDGYEEGDYT QFKEMPASEF IQTTDPIAIL GQYNRLSFEQ PKNGDVALAA LDKLPETTEE
     IRLSCADLKV LSRKEFKVLL RWRLRVRELF GFPSKKTAAK PLSEEVTQVD TMDEEMKIQQ
     ELQAMKDRTD SKKKREKRKE NEKKQKDIVR MQMNMTAPMD IGMEQADAMG DGSMFALKKL
     QEPDALRRIA KGKMAFLNTD KKVDRDSGIG SSGETDNESD EEEDRLEREL DGLYDEYQDR
     KSSADAKYRA KKARERKGDD DWEGFSGEDK DIEDSDGDLE EDSSDDDDDT AGGKPTKSLL
     TDLDNGPDEE GGLSKRARSF FNQDIFKDIP GVLDDLVEEE EGEDEDEDEE EEEEGEIEDE
     EMPDVDENDA EEDDIPSKGK SGKKGAKEEV TFDESESEDG GGGGFEVVKR SKQDTDENDW
     EEEDKRLRSD GRLDIDIITA EAMTLAQSLA SGQRLKHDVI DDGFNKHAFR DKDGLPEWFL
     DDESRHDKLH RPITKAGADA IKEKMRAFNA RPIKKVREAQ ARKKFKAVQK LEKLKKKSEL
     LIADEGMTEK EKGDTISKML SKAAKKKPHT PMKVVVARGS NRGIKGRPKG VKGRYKLVDA
     RMKKETRALK RVAKKYKK
//
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