SPB1_DEBHA
ID SPB1_DEBHA Reviewed; 831 AA.
AC Q6BNQ8;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=AdoMet-dependent rRNA methyltransferase SPB1 {ECO:0000255|HAMAP-Rule:MF_03163};
DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_03163};
DE AltName: Full=2'-O-ribose RNA methyltransferase {ECO:0000255|HAMAP-Rule:MF_03163};
DE AltName: Full=S-adenosyl-L-methionine-dependent methyltransferase {ECO:0000255|HAMAP-Rule:MF_03163};
GN Name=SPB1 {ECO:0000255|HAMAP-Rule:MF_03163};
GN OrderedLocusNames=DEHA2E19690g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Required for proper assembly of pre-ribosomal particles
CC during the biogenesis of the 60S ribosomal subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03163}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90675, ChEBI:CHEBI:90676; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03163};
CC -!- SUBUNIT: Component of the nucleolar and nucleoplasmic pre-60S ribosomal
CC particle. {ECO:0000255|HAMAP-Rule:MF_03163}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|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:0000255|HAMAP-Rule:MF_03163}.
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DR EMBL; CR382137; CAG88435.2; -; Genomic_DNA.
DR RefSeq; XP_460162.2; XM_460162.1.
DR AlphaFoldDB; Q6BNQ8; -.
DR SMR; Q6BNQ8; -.
DR STRING; 4959.XP_460162.2; -.
DR PRIDE; Q6BNQ8; -.
DR EnsemblFungi; CAG88435; CAG88435; DEHA2E19690g.
DR GeneID; 2902988; -.
DR KEGG; dha:DEHA2E19690g; -.
DR VEuPathDB; FungiDB:DEHA2E19690g; -.
DR eggNOG; KOG1098; Eukaryota.
DR HOGENOM; CLU_009422_8_1_1; -.
DR InParanoid; Q6BNQ8; -.
DR OMA; LMWVFQQ; -.
DR OrthoDB; 1362679at2759; -.
DR Proteomes; UP000000599; Chromosome E.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:UniProtKB-UniRule.
DR GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 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 Pfam; PF11861; DUF3381; 1.
DR Pfam; PF01728; FtsJ; 1.
DR Pfam; PF07780; Spb1_C; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Coiled coil; Methyltransferase; Nucleus; Reference proteome;
KW Ribosome biogenesis; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..831
FT /note="AdoMet-dependent rRNA methyltransferase SPB1"
FT /id="PRO_0000155596"
FT REGION 492..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 346..389
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COILED 440..479
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COILED 729..782
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COMPBIAS 572..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..627
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
SQ SEQUENCE 831 AA; 95072 MW; EFFFD6B0740C16A9 CRC64;
MGKTQKKNSK GRLDRYYYLA KEKGYRARSS FKIIQINEKY GHFLEKSKVV IDLCAAPGSW
CQVASQLCPI NSLIIGVDIV PIKALPNCIT FQSDITTEDC RSQLRGHMKT WKADTVLHDG
APNVGLGWVQ DAFTQSHLTL QALKLAVENL NTGGTFVTKI FRSRDYNNLM WVFQQLFEKV
EATKPPASRN VSAEIFVVCK GYKSPKKMDP RLLDPREVFE ELPTGPDNNE AKIFNPEKKV
RRRQGYEEGD YTLFHEMPLL EFIKNEDPIN TLGTLNKLSE PPQDDHEWKI LKKSKLCTPE
LLECIKDLKV LGRKDFKHLL KFRKQARDLL GLDAKEETQE IEVEPLTEDQ QIEKELQELT
EKQKQKARKA KKQSNEIKQK EIQRSQMNML TDMNIGIEAA QIGAESLFNL KTAIKTGQLE
KLSKGKKKMI FNDEEIMKDN DINFDEEADA NSEDEIDELE AQLDDMYNSY QNRRAERDAN
YRAKKLRGDV DDEGWEGIES DKEGSDKETE ANDYEMESES DSDDDEHIQR IADQRKKELS
KNAKVFFASN SIFGELGDEA LLEEMNKKEA KTNQVTNENA VGHANDISNK PEQMEVDSSD
SENDVSDDSD FEIVPNAPDE ELSDSDSDNE NDVSRKYSKA KDQQSKVDIA TVEAMTLAHQ
VALGHKNKHD LVNEGIHKYS FRDHDDLPEW FVDDEKRNSK IVKPITKEAA LAIKEKQKQL
NARPIKKVLE AQGRKKLRAL KRLEKLKKKS DMINEDSAKS ERDKADEIQK LMKKLTKKQK
TKPKATLVVA RGSNRGLSGR PKGVKGKYKM VDGVMKNEQR ALKRIAKKHK K
