ID A0A0H1BKL6_9EURO Unreviewed; 836 AA.
AC A0A0H1BKL6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=AdoMet-dependent rRNA methyltransferase spb1 {ECO:0000313|EMBL:KLJ09721.1};
GN ORFNames=EMPG_14844 {ECO:0000313|EMBL:KLJ09721.1};
OS Blastomyces silverae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ09721.1, ECO:0000313|Proteomes:UP000053573};
RN [1] {ECO:0000313|Proteomes:UP000053573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KLJ09721.1}.
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DR EMBL; LDEV01002281; KLJ09721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H1BKL6; -.
DR STRING; 2060906.A0A0H1BKL6; -.
DR OrthoDB; 119516at2759; -.
DR Proteomes; UP000053573; 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:UP000053573};
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..391
FT /note="DUF3381"
FT /evidence="ECO:0000259|Pfam:PF11861"
FT DOMAIN 623..831
FT /note="Ribosomal RNA methyltransferase SPB1-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07780"
FT REGION 335..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..463
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..574
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..650
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 836 AA; 94598 MW; 33A45339EAA07F16 CRC64;
MAIQKKHGKG RLDKWYKLAK EKGYRARAAF KLIQLNKKYG FLEKSKVVID LCAAPGSWCQ
VAAECMPSQS LIIGVDLAPI KPIPKVITFQ SDITTDKCRA TIRQHLKTWK ADTVLHDGAP
NVGVAWVQDA FSQAELVLQS LKLATEFLVP GGTFVTKVFR SKDYNPLLWV FKQLFNTVDA
TKPPSSRNVS AEIFVVCQGF KAPKHIDPKF LDARHVFAEL QDPTPNHEAK VFNPEKKKRK
RDGYEEGNYT QFKEIPVSEF INTTDPISIL GEYNKLSFDQ STGGDLALAT LARLPETTKE
IQLCCEDLKV LGKKEFRNLL RWRIKVREKF GLAVKKGASK PAESEEVAEV EPMDEELAIQ
EDLQRIRDKE TSRKKKERRR ENERKQKEIV RMQMHMTTPM EIGIEQSGPL GEGAMFALKP
VNRAGDVSQI TSGKMVPIES DDEEDDSSTI DDDSDDEEDR LERELDSLYE RYRTDQEDRD
AKLRAKKARK EFETEEWEGI SDSDKEGGED TDSGDTRLQD AIPRPAIDSK GLSNKAAMFF
DQDIFQGLGD LGDEDEEDDE DDEDDEDEED EGGSEGENAA RQQEDGAEHD EYSDVSESDD
PGTQQPSKLD RKQTSEKRQS KSKMNSKGND ISPDFEEEEK KDPRKKNGQL DIDIITAEAM
ALAQQIVTGE KTTQDVVDDG FNKYTFRDND GLPEWFMDDE GKHSKPLRPI TAAASAAIRE
KLRAINARPI KKVLEARGRK KFKAAQRLEK LRKKSALLAE DEAMSEKDKA QTIARMMSRA
MKKKPKQHVK LVVAKGANKG ISGRPKGVKG KYKIVDSRMK KDIRAEKRLA KKRKKN
//
