ID A0A0K0IZ34_BRUMA Unreviewed; 786 AA.
AC A0A0K0IZ34;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=Bm13809 {ECO:0000313|EMBL:CRZ25681.1,
GN ECO:0000313|WBParaSite:Bm13809.1, ECO:0000313|WormBase:Bm13809},
GN BM_Bm13809 {ECO:0000313|EMBL:CRZ25681.1};
OS Brugia malayi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=6279 {ECO:0000313|Proteomes:UP000006672, ECO:0000313|WBParaSite:Bm13809.1};
RN [1] {ECO:0000313|EMBL:CRZ25681.1, ECO:0000313|Proteomes:UP000006672}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ25681.1,
RC ECO:0000313|Proteomes:UP000006672};
RX PubMed=17885136; DOI=10.1126/science.1145406;
RA Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA Blaxter M.L., Scott A.L.;
RT "Draft genome of the filarial nematode parasite Brugia malayi.";
RL Science 317:1756-1760(2007).
RN [2] {ECO:0000313|EMBL:CRZ25681.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR3 {ECO:0000313|EMBL:CRZ25681.1};
RA Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:Bm13809.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (DEC-2019) to UniProtKB.
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}.
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DR EMBL; LN857010; CRZ25681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K0IZ34; -.
DR STRING; 6279.A0A0K0IZ34; -.
DR EnsemblMetazoa; Bm13809.1; Bm13809.1; WBGene00234070.
DR WBParaSite; Bm13809.1; Bm13809.1; WBGene00234070.
DR WormBase; Bm13809; BM09920; WBGene00234070; -.
DR InParanoid; A0A0K0IZ34; -.
DR OrthoDB; 119516at2759; -.
DR Proteomes; UP000006672; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0008649; F:rRNA methyltransferase activity; IEA:UniProtKB-UniRule.
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 {ECO:0000256|HAMAP-Rule:MF_03163};
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:UP000006672};
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..200
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT DOMAIN 240..385
FT /note="DUF3381"
FT /evidence="ECO:0000259|Pfam:PF11861"
FT DOMAIN 566..766
FT /note="Ribosomal RNA methyltransferase SPB1-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF07780"
FT REGION 419..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 350..385
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT COMPBIAS 419..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..451
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..786
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 786 AA; 90228 MW; A0BAB57862CB91F7 CRC64;
MGKKTKIGKQ RRDKYYHLAK EAGYRSRAAF KLLQLNKRFE FLQKSRAVVD LCAAPGGWLQ
VAIQNMPVSS ICIGVDLVPI KPINKCVTLQ GDITTEKTRQ MVRKELHGWE ADCVLHDGAP
NVGRNWVQDA FQQNCLTLSA LRLATQILTK NGIFVTKIFR SSDYCHLISV FEKLFKQVHV
WKPAASRLES AEIFVVCEKY LKPEKLDPDL LDPKKVFAES TQQSVISNPQ LMLQPRAKLK
KVPATGYENE SVSLHKTINA TDFIHSNNYL ELLASAYKIA LDDERWLNNE STTDEVKCCL
EDIKVCGPRE LRLILKWRRN IITKINEEGN ETENPTKDDV MAVNPEDERM AEIEQQLSMA
KAEEKAALKK KKRKLLKDKA NLEKRKKLKM LVEGDTYEIP DEQELFSLKK LAIAKNKRCA
DSELSNSKNE NESDNDEGCS SDDDNDDYGI DDDAEEFHHE QDPSMSKAEK TEAQKAEWFG
RHQVAELVDD EEGALKAIEN FMKKFNNTSQ SSFNKKKKDE RDGQKSIADA WSDRGNNADS
QKLSNGAGID AGTTSVFMDD DESDEEYHDI DKIDTKTSSS DIPQKEKPGK AKKLSPELLA
LGEQLIYSSK TRRDLEDWGW NRYTNNDEGL PDWFVEDEKK HFKKELPVSK DRVDFYKNRM
RDINTRTIKK VAEAKARKKK RRDRKLQLAK KRAEGIIESE NMEQAEKIRE IRKLYRKTAS
SIKEKKKITY AVMTKGKRGS LSRPKGPYKV VDARLKKDNR RQKQMNQKKG YKAGGRGGRR
RNRRSD
//
