SPB1_NEUCR
ID SPB1_NEUCR Reviewed; 831 AA.
AC Q9P6V8; Q1K813;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 111.
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; ORFNames=68B2.180, NCU03669;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; AL353821; CAB88626.2; -; Genomic_DNA.
DR EMBL; CM002240; EAA32209.1; -; Genomic_DNA.
DR PIR; T48834; T48834.
DR RefSeq; XP_961445.1; XM_956352.2.
DR AlphaFoldDB; Q9P6V8; -.
DR SMR; Q9P6V8; -.
DR STRING; 5141.EFNCRP00000003395; -.
DR EnsemblFungi; EAA32209; EAA32209; NCU03669.
DR GeneID; 3877666; -.
DR KEGG; ncr:NCU03669; -.
DR VEuPathDB; FungiDB:NCU03669; -.
DR HOGENOM; CLU_009422_8_1_1; -.
DR InParanoid; Q9P6V8; -.
DR OMA; LMWVFQQ; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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..831
FT /note="AdoMet-dependent rRNA methyltransferase spb1"
FT /id="PRO_0000155600"
FT REGION 442..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 349..396
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT COMPBIAS 451..467
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..530
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..588
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..618
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 56
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 92
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03163"
SQ SEQUENCE 831 AA; 93958 MW; D8B91C1D37BDD986 CRC64;
MAIQKKHGKG RLDKWYKLAK EKGYRARAAF KLIQLNKKYG FLEKSKVALD LCAAPGSWCQ
VCAETMPTNS IIIGVDLAPI KPIPKVITFQ SDITTEKCRA TIRSHLKTWK ADVVLHDGAP
NVGTAWVQDS YNQAELALHS LKLATEFLIE GGTFVTKVFR SKDYNSLLWV CNQLFAKVEA
TKPPSSRNVS AEIFVVCRGF KAPKRIDPKL LDPRSVFEDV AGPAPNNEAK VYNPEVKKRK
REGYEEGDYT QFKEISASEF INTVDPIAIL GQYNKLSFEQ PKNGDVALAA LDKLPETTEE
IRLCCADLKV LGRKEFKLLL KWRLKVREIF GFPSKKTQKA AVDEEVAVVE NMDEELRIQE
ELQRIKEKET SKKKRERRRE NEKKQKEIVR MQMNMTAPMD IGVEQEGPRG EGAMFRLKTI
DQNAALNKIA KGKMAVIKET EKPKDYDFGS DGETDESDEE ADRLEEELDN LYDQYRERKA
AADAKYRAKK ARKENGDDEW EGVSGDEEKG SDDDDDEELE VDSSDDDSDS EDGESGKKLI
TDLDGQPEEK DGLSKRAKNF FSQGIFAEIP GLLEEPESEE EEAQEAELVE AVEDLKVTKK
EKKEAKETKA KSKKAAEESD DDDDFEVVKN NEDDDWENVE KKKKNGRPDI DIITAEAMTL
AHQLATGEKT SYDVIDDGYT KHAFKDRDGL PDWFLDDESK HDKPHKPITK AAAQAIKEKL
RAYNARPIKK VAEAKARKKF KQAQRLEKLK KKADMLAGDD GMSEKEKAAS ISKLMASVAK
KTRRAPIKVV KAAGSNKGLQ GRPKGVKGRY KMVDPRMKKE LRAMKRISKK K
