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Database: UniProt
Entry: A0A2D3VBI1_9PEZI
LinkDB: A0A2D3VBI1_9PEZI
Original site: A0A2D3VBI1_9PEZI 
ID   A0A2D3VBI1_9PEZI        Unreviewed;       870 AA.
AC   A0A2D3VBI1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   08-NOV-2023, entry version 22.
DE   SubName: Full=Related to AdoMet-dependent rRNA methyltransferase spb1 {ECO:0000313|EMBL:CZT18949.1};
GN   ORFNames=RCC_04794 {ECO:0000313|EMBL:CZT18949.1};
OS   Ramularia collo-cygni.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX   NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT18949.1, ECO:0000313|Proteomes:UP000225277};
RN   [1] {ECO:0000313|EMBL:CZT18949.1, ECO:0000313|Proteomes:UP000225277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URUG2 {ECO:0000313|EMBL:CZT18949.1,
RC   ECO:0000313|Proteomes:UP000225277};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; FJUY01000006; CZT18949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D3VBI1; -.
DR   STRING; 112498.A0A2D3VBI1; -.
DR   OrthoDB; 119516at2759; -.
DR   Proteomes; UP000225277; 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:UP000225277};
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..407
FT                   /note="DUF3381"
FT                   /evidence="ECO:0000259|Pfam:PF11861"
FT   DOMAIN          644..864
FT                   /note="Ribosomal RNA methyltransferase SPB1-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07780"
FT   REGION          383..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..681
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          776..870
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..462
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        463..477
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..551
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        585..602
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..637
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..811
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..862
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   870 AA;  97436 MW;  642751A07A71CD86 CRC64;
     MGQDKKSAKG RLDKYYYLAK EKGYRARAAF KLIQLNKKFN FLQNARCLID LCAAPGSWLQ
     VAAEIMPPKS LIVGVDLTPI KPIPKAISFQ GDITTDKCRA TIRGHLKTWK ADCVIHDGAP
     NVGTAWVQDA FSQNELVLSS LKLATEFLIP NGTFVTKVFR SKDSAKLEWI FKQLFTKVEQ
     TKPPSSRNVS AETFYVCRGF KAPKHLDPRF LDPTHAFSEI EESAPNNEAK VFNPEIKKRK
     RDGYEEGDWT QFKECSASDF IQTNDPIAVL GSMNKLHFRQ EANGDIAQAA LDKLPETTEE
     VRLCCQDLKV LGRKEFKVLL RWRLKARDRF GFRVKKTAKE EAEAAKPAVD APQVKEGVEG
     EEVAVVESMD GEMRLQEEIQ AMKDAQSKVK RKERRKDNER KQKETVRMQM GMTTPSEIGI
     EAGDQGSSEA VFRLKDADKR TDIRQAIMRG RMHTAVEPEK PKEESEEESE DEYGDALEAQ
     LDGMYEQYQE RVEDRDTKAR AKRARKLARG NDVEEEFEGF GAEDKDPNDS DASSDDGLLE
     DDDDSLDSDD GEGALTTDLQ PKDPMGGGLT RRAASFFEQD IFKGIDGLDE EDEEDEEDEP
     ELDKARDSGV DVESPNLKPA TEEEEDDDSE DAMSFASDDD AASETSSIEA VPSNIQPEEE
     DWEEGTTRPS APGENPAQPS ISIITAEAMT LAHQLATGKV TKQQLLDDNF NKYTLRDVDG
     LPEWFLDDEN KHSRLARPVS GEAAAAIKEK LRALNARPIK KVREAKARKT LRTARRLEKL
     KKKSEGLAEQ DGEGGGEAGR DAMERMSKMM AKAKKGTKKR NPVKVVFAGG HNKGAGRPRG
     VKGKYKMVDS RLKKDVRGLK RAEKKGRVRR
//
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