ID   SPB1_CANAL              Reviewed;         845 AA.
AC   Q59KF3; A0A1D8PQB8; Q59KF8;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-MAY-2023, entry version 85.
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=CAALFM_C604160CA; ORFNames=CaO19.76, CaO19.7727;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017628; AOW30336.1; -; Genomic_DNA.
DR   RefSeq; XP_710224.1; XM_705132.2.
DR   AlphaFoldDB; Q59KF3; -.
DR   SMR; Q59KF3; -.
DR   STRING; 237561.Q59KF3; -.
DR   EnsemblFungi; C6_04160C_A-T; C6_04160C_A-T-p1; C6_04160C_A.
DR   GeneID; 3648179; -.
DR   KEGG; cal:CAALFM_C604160CA; -.
DR   CGD; CAL0000201177; SPB1.
DR   VEuPathDB; FungiDB:C6_04160C_A; -.
DR   eggNOG; KOG1098; Eukaryota.
DR   HOGENOM; CLU_009422_8_1_1; -.
DR   InParanoid; Q59KF3; -.
DR   OrthoDB; 119516at2759; -.
DR   PRO; PR:Q59KF3; -.
DR   Proteomes; UP000000559; Chromosome 6.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; 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: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:0031167; P:rRNA methylation; IBA:GO_Central.
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   Coiled coil; Methyltransferase; Nucleus; Reference proteome;
KW   Ribosome biogenesis; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..845
FT                   /note="AdoMet-dependent rRNA methyltransferase SPB1"
FT                   /id="PRO_0000155593"
FT   REGION          223..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          366..402
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   COILED          464..502
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   COILED          739..796
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT   COMPBIAS        225..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..516
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..544
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..623
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..645
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   845 AA;  96820 MW;  0FA5DE332ECA6767 CRC64;
     MGKQQKKHSK GRLDRYYYLA KEKGYRARSS FKIIQINEKY GHFLEKSKVV IDLCAAPGSW
     CQVASQLCPI NSLIIGVDIV PIKPLPNVIT FQSDITTEDC RSRLRGHMKT WKADTVLHDG
     APNVGLGWVQ DAFTQSQLTL QALKLAVENL TAGGTFVTKI FRSRDYNNLM WVFQQLFEKV
     EATKPPASRN VSAEIFVVCK GFKAPKKLDP RLLDPKEVFE ELGGGNESKQ NNEAKIFNPE
     KFSSQRQRQG YQEGDYTLFH TMPIMDFIKQ DDPINQLGSL NKFDLPAPKD DDNDDDDHDH
     EWKILSKLKL CTPELLECIK DLKVLGRKEF KMILKFRKQA RDILGIDKDE KEEEEENPKI
     EVEPLTEEQK IDQELQDLIN KQKQKAKRLK KNANELKQKE IIRNQMNMLT DMNIGIEAAQ
     IGADSLFNLK TAEKTGQLDK LAKGKKKMIF NDEELAKDNE IHIDEEEIND NDKDSADELD
     ELENQLDDMY HQYQARKAER DANYRAKQAR GDADDEAWNG IEEDNDDVES GKDYEMESES
     DDDDDEHIRL IAEKKSNGSL SRTARNFFAS DSIFNELSDD VILEEIENKT KGSNGKMVES
     IQEQVANDNN ENDDGDNDEE ESDFEIVPNQ KSDDDDDDES MNSDDDEVST TTKSTTHQQK
     VDLATVEAMT LAHQVALGQK NKYDLIDEGI NRYSFRDKDN LPDWFIDDEK KHSKLIKPIT
     KEAAIAIKEK QKQLNARPIK KVLEAQSRKK LRALKRLEKI KKKSDLINED SGKSERDKAD
     EISKLMKKLN KKQKQKPKTT VVVARGSNRG LSGRPKGVKG KYKMVDGVMK NEQRALKRIA
     KKYKK
//