MRM2_DICDI
ID MRM2_DICDI Reviewed; 640 AA.
AC Q86AH1; Q55A99;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=rRNA methyltransferase 2, mitochondrial {ECO:0000250|UniProtKB:P53123};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P53123};
DE AltName: Full=rRNA (uridine-2'-O)-methyltransferase {ECO:0000250|UniProtKB:P53123};
DE Flags: Precursor;
GN Name=fsjB; ORFNames=DDB_G0271998;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose
CC methyltransferase that catalyzes the formation of a 2'-O-methyluridine
CC in the mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a
CC universally conserved modification in the peptidyl transferase domain
CC of the mtLSU rRNA. {ECO:0000250|UniProtKB:P53123}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC methyluridine in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:54152, Rhea:RHEA-COMP:13812, Rhea:RHEA-COMP:13814,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478;
CC Evidence={ECO:0000250|UniProtKB:P53123};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P53123}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. {ECO:0000305}.
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DR EMBL; AAFI02000007; EAL71433.1; -; Genomic_DNA.
DR RefSeq; XP_645367.1; XM_640275.1.
DR AlphaFoldDB; Q86AH1; -.
DR STRING; 44689.DDB0238606; -.
DR PaxDb; Q86AH1; -.
DR EnsemblProtists; EAL71433; EAL71433; DDB_G0271998.
DR GeneID; 8618256; -.
DR KEGG; ddi:DDB_G0271998; -.
DR dictyBase; DDB_G0271998; fsjB.
DR eggNOG; KOG4589; Eukaryota.
DR HOGENOM; CLU_427914_0_0_1; -.
DR PRO; PR:Q86AH1; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008649; F:rRNA methyltransferase activity; ISS:dictyBase.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; ISS:dictyBase.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..640
FT /note="rRNA methyltransferase 2, mitochondrial"
FT /id="PRO_0000330907"
FT REGION 175..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 594
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0C0R7"
FT BINDING 439..442
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 460
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 476..477
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
FT BINDING 554
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9UI43"
SQ SEQUENCE 640 AA; 73168 MW; E0D3B2E5D2F584EA CRC64;
MLANRANRLV LKRLVHLNTS NIIKPICSYR SLASSSKSKT QFTKKPPISE FSIDEILEHF
ILKKKTIEGK ENKDKNTIKV EKVNTKIDRF SSEVIIKEKN KKNNNIEDED EFGIEEMIAK
NNNNNNNPNN NNNNNNTKKV PTFNRFSTEV IVKSNNNNIN EFENEEITKN NLNKKAPKFN
RSSSGVVINT TSNDNNNDKN NNEFENEEIM LNSGKTNKKA SKMDRYSSEV IIKEKNNEEI
LVNNNNNNNN NTTTTTNNNN NNKASKMERY SSEVIIKEKK DNNNDIEKDD IEKDEIIVNI
MNGFEDKDES AVEFLKRHRI EHQVPKSTIY LKEKTMEEDE MVRKRLSVNR DNINFSNNKN
RKQIFTKKNH QNGAGILPKG LANNIVKNDW MKRQMTDPYV AMAQKNDLIS RAAYKIINID
EQIQLFKPGQ IVVDLGAAPG GWSKYIQERV TNRGLVISVD TSSNFQLDKD CFIHGDFTLT
ETQNKIFELT KFKSLNDLKL YKHSLIHSDS KIQNLIENGG ANGNGSGNGD LQKQPIDNMF
KQKSACYVDV VVSDMAPSYS GLQQVDHSRL IDLQRLALFF AFKTLKKGGT FVCKVSRGGE
EKKFFKLLES NFISVKSMKP GASRSESTEI YYIGKNYIGK
