MRM1_DICDI
ID MRM1_DICDI Reviewed; 531 AA.
AC Q76NT0; Q54ZH2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=rRNA methyltransferase 1, mitochondrial {ECO:0000250|UniProtKB:P25270};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:P25270};
DE AltName: Full=rRNA (guanosine-2'-O)-methyltransferase {ECO:0000250|UniProtKB:P25270};
DE Flags: Precursor;
GN Name=mrm1; ORFNames=DDB_G0277479;
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-
CC methylguanosine in the mitochondrial large subunit ribosomal RNA (mtLSU
CC rRNA), a universally conserved modification in the peptidyl transferase
CC domain of the mtLSU rRNA. {ECO:0000250|UniProtKB:P25270}.
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:P25270};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P25270}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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; AAFI02000020; EAL68702.1; -; Genomic_DNA.
DR RefSeq; XP_642670.1; XM_637578.1.
DR AlphaFoldDB; Q76NT0; -.
DR SMR; Q76NT0; -.
DR STRING; 44689.DDB0169271; -.
DR PaxDb; Q76NT0; -.
DR EnsemblProtists; EAL68702; EAL68702; DDB_G0277479.
DR GeneID; 8621087; -.
DR KEGG; ddi:DDB_G0277479; -.
DR dictyBase; DDB_G0277479; -.
DR eggNOG; KOG0838; Eukaryota.
DR HOGENOM; CLU_513327_0_0_1; -.
DR InParanoid; Q76NT0; -.
DR OMA; LACARNC; -.
DR PRO; PR:Q76NT0; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0016435; F:rRNA (guanine) methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000154; P:rRNA modification; IBA:GO_Central.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR013123; SpoU_subst-bd.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR Pfam; PF00588; SpoU_methylase; 1.
DR Pfam; PF08032; SpoU_sub_bind; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Mitochondrion; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..531
FT /note="rRNA methyltransferase 1, mitochondrial"
FT /id="PRO_0000337262"
FT REGION 70..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 60066 MW; BF9F2B6D4F074243 CRC64;
MISIFKILSS PKPATTTTNI INPINIINGI RYFSSNQEDY PLFKKPVFNG KVLRGGRKVF
KNDLIYSKKE SHYNNNNNSN NNSNNNNNNN NSNNRNNNNF SNNRNNNNNR NNNNNNSNRN
NNNSNDNNFR NNNNNNRRTE YYKNDFDSSK YISNKPEIRI FDLHEQAVYG INPVWVALSS
GNRTFNALYV CGTLLPKLKE LGIDIKNIEN SKREYISDFD HNYGRETNQI EDENQDEQYS
NQHDEQEQNE YEEEQEEEKV QEEEEDNNNN NNIKKTTFNR YNDRKNLVAL KEIVKNSFKL
KIPVRSVNKG TLDSFSKGRP HQGIILDASP LTLLNIDFLE KFDINERVNK RMNGGGGGGG
GGGGNKINND KYPLWLVLDE LWDPQNVGAI IRNCSFFNID GVVISNKNSS PITPAASKSS
SGACESFVIN RTESIEGFLK SSQRNGWNVV GTSLDDLNEN QPCLDINQIK LDQPTILILG
NEGFGLKPSV LEICNKTIKI VGGNYKIDSL NVSVTSGILI HTLLSSGTLP K
