ID A0A9W5T935_BABOV Unreviewed; 876 AA. AC A0A9W5T935; DT 08-NOV-2023, integrated into UniProtKB/TrEMBL. DT 08-NOV-2023, sequence version 1. DT 29-MAY-2024, entry version 4. DE RecName: Full=Putative rRNA methyltransferase {ECO:0000256|HAMAP-Rule:MF_03163}; DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03163}; DE AltName: Full=2'-O-ribose RNA methyltransferase SPB1 homolog {ECO:0000256|HAMAP-Rule:MF_03163}; GN ORFNames=BaOVIS_009160 {ECO:0000313|EMBL:GFE53512.1}; OS Babesia ovis. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida; OC Babesiidae; Babesia. OX NCBI_TaxID=5869 {ECO:0000313|EMBL:GFE53512.1, ECO:0000313|Proteomes:UP001057455}; RN [1] {ECO:0000313|EMBL:GFE53512.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Selcuk {ECO:0000313|EMBL:GFE53512.1}; RA Yamagishi J., Sevinc F., Xuan X.; RT "Genome sequence of Babesia ovis."; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Probable methyltransferase involved in the maturation of rRNA CC and in the biogenesis of ribosomal subunits. {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_03163}; 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:GFE53512.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BLIY01000006; GFE53512.1; -; Genomic_DNA. DR Proteomes; UP001057455; Unassembled WGS sequence. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0030687; C:preribosome, large subunit precursor; IEA:TreeGrafter. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IEA:TreeGrafter. DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:TreeGrafter. DR GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:TreeGrafter. DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:TreeGrafter. DR CDD; cd02440; AdoMet_MTases; 1. 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:UP001057455}; KW Ribonucleoprotein {ECO:0000313|EMBL:GFE53512.1}; KW Ribosomal protein {ECO:0000313|EMBL:GFE53512.1}; 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..213 FT /note="Ribosomal RNA methyltransferase FtsJ" FT /evidence="ECO:0000259|Pfam:PF01728" FT DOMAIN 256..415 FT /note="DUF3381" FT /evidence="ECO:0000259|Pfam:PF11861" FT DOMAIN 662..866 FT /note="Ribosomal RNA methyltransferase SPB1-like C- FT terminal" FT /evidence="ECO:0000259|Pfam:PF07780" FT REGION 396..415 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 466..661 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 830..876 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 490..535 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 558..575 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 587..608 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 609..659 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 858..876 FT /note="Basic 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 876 AA; 99817 MW; F4DF4670341615E3 CRC64; MKTRVKQGKE RQDKYYYLAK EQGYRARSAF KIIQLAKKFN IFENCNVLVD LCAAPGGWLQ VAAKHLPISS IIVGVDLVPI RPIKGVVTIQ ADIRTQRCRN LISQQLRGAE VDVVLHDGAP NVGANWNLDA FNQNVLVLEA AKLASQVLRK GGIFVTKIFR YLSLCINHIM LYRSADYNSL IWTLGKCFER VKVTKPSSSR NVSAEIFAVC IGFRTLKSLD PKLFNCEHVF ISQATPTEEE TNESAKITSL NQLLRQRKKV NKEGYEEGDD FREYNILDFV TTDNPPQMLV SSNRFVFRPR DKPETLEKDN ELLKQILSHP LTTEEVRLLC SDLKVAGRSD LHHLLKWRHK ICKDLFPVDK KPKVENEVAA YPEQVEEPEE DTLKRQELEV ADRVRKELRR TERKQRRAMM KHKKAMAGNS VILDSDPSLF RLSTLKGRDI DDLMNDSPDS GDDSHSETLG QGGDDILYAG SDDNTSEADS MDLQFETDSE DDDKIAKMEV DLEVQHEMSK LTEETRPKST KKLTRRQRVN EERGAELSSL LENMQYEARL KAQQEMQDSD DELDDSEDDD TGASGDVTDV EVIDDSQGGD DTNQIISEES PGETKATKTS GPTKDDRDTK RALEDAMIDR WFDQDVFHDQ PRETARKQKT RENKNAKAKN KEPTFTVVPA ISDADAVERA RDAIELELSR NKETIAEVQA MGSLLVNKDT RMALIDGAYN KRTFDDGELP SWFEEDEKKH SNYELPVTKE LMKRYKAKLH ELKNRPIRKV LEARGRRKLR VERKLKSVLP RVEALQNSDT GGARTAKKLL RKVQNTASNK REKVYVVSRR GGTTTTAPTG GKGSRKVTKA VDKRMKKDNV RQKRKPKSRS RKARIH //