SPB1_ASHGO
ID SPB1_ASHGO Reviewed; 830 AA.
AC Q751U1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 104.
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}; OrderedLocusNames=AFR734C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO C-TERMINUS.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS54106.2; -; Genomic_DNA.
DR RefSeq; NP_986282.2; NM_212418.2.
DR AlphaFoldDB; Q751U1; -.
DR SMR; Q751U1; -.
DR STRING; 33169.AAS54106; -.
DR EnsemblFungi; AAS54106; AAS54106; AGOS_AFR734C.
DR GeneID; 4622573; -.
DR KEGG; ago:AGOS_AFR734C; -.
DR eggNOG; KOG1098; Eukaryota.
DR HOGENOM; CLU_009422_8_1_1; -.
DR InParanoid; Q751U1; -.
DR OMA; LMWVFQQ; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0000453; P:enzyme-directed rRNA 2'-O-methylation; IEA:UniProtKB-UniRule.
DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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..830
FT /note="AdoMet-dependent rRNA methyltransferase SPB1"
FT /id="PRO_0000155591"
FT REGION 485..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 345..388
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COMPBIAS 498..527
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="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 830 AA; 94998 MW; 76B16D751D2AC145 CRC64;
MGRTQKKNSK GRLDRYYYLA KEKGYRARSS FKIIQINEKF GHFLEKSKVV IDLCAAPGSW
CQVASNLCPV NSLIIGVDIV PMQPMPNVIT FQSDITTEDC RSKLRGYMKT WKADTVLHDG
APNVGLNWVQ DAFTQSHLTL QALKLAVENL VVGGTFVTKI FRSKDYNKLM WVFQQLFDKV
EATKPPASRN VSAEIFVVCK GFKAPKKLDP RLLDPKEVFE ELPDGPQNMQ AKVYNPEKKT
RKRDGYEEGD YLLYHTVPIM DFVKVEDPIQ MLGTTNKFTL DKDDHEWKIV KKLKQTTPEF
KACIEDLKVL GKKDFKMLLR WRKAARELLG LDKDEEQPEI ETVPLTEEEQ IEKELQEMQQ
KQNLKKKREK RKQNEIKQKE ITRMQMQMIT PTDLGIEAAS IGRDSLFNLK TAEKTGILDD
LARGKKRMVF TRDELAEDNE IQIDENAPLS DRDDLADADE LESQLDAMYH QFKARRIERD
AHFKAKEARG GDDDAWNGFD EVASDEEPEE SKKDYVDDDD SDVSDSDSDE AINQLIAKIK
GETGDKKLSA KARALFNDSI FDGVEADLPS EEPQAPASSE QGSKKRRLEE VSEESSSDEE
EAEEESDSDF EIVRNEKDES DDDYDSEDEA ERSQKEKHAR EVDIATVEAM TLAHQLALGQ
RSKHDIVDEG FNRYSFRDRD NLPEWFLEDE KMHSKINKPI TKEAAMAIKE KLKALNARPI
KKVAEAKARK KMRALNRLEK LKKKAGLIND DSDKSEKDKA EEIAKLMKKV TKKAKLKPKV
TLVVAKGKNR GLSGRPKGIK GKYKMVDGVM KNEQRALKRI AKKHRKKSKH
