ID   A0A0F4ZD53_9PEZI        Unreviewed;       534 AA.
AC   A0A0F4ZD53;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-NOV-2023, entry version 30.
DE   RecName: Full=rRNA methyltransferase 1, mitochondrial {ECO:0000256|ARBA:ARBA00034881};
GN   ORFNames=TD95_002249 {ECO:0000313|EMBL:KKA28534.1};
OS   Thielaviopsis punctulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX   NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA28534.1, ECO:0000313|Proteomes:UP000033483};
RN   [1] {ECO:0000313|EMBL:KKA28534.1, ECO:0000313|Proteomes:UP000033483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA28534.1};
RA   Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase TrmH family.
CC       {ECO:0000256|ARBA:ARBA00007228}.
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:KKA28534.1}.
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DR   EMBL; LAEV01001276; KKA28534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4ZD53; -.
DR   OrthoDB; 5404245at2759; -.
DR   Proteomes; UP000033483; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0031167; P:rRNA methylation; IEA:InterPro.
DR   CDD; cd18105; SpoU-like_MRM1; 1.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR047182; MRM1.
DR   InterPro; IPR047261; MRM1_MeTrfase_dom.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR004441; rRNA_MeTrfase_TrmH.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR013123; SpoU_subst-bd.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   NCBIfam; TIGR00186; rRNA_methyl_3; 1.
DR   PANTHER; PTHR46103; RRNA METHYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR46103:SF1; RRNA METHYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   Pfam; PF08032; SpoU_sub_bind; 1.
DR   SMART; SM00967; SpoU_sub_bind; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
DR   SUPFAM; SSF55315; L30e-like; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033483};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          201..283
FT                   /note="RNA 2-O ribose methyltransferase substrate binding"
FT                   /evidence="ECO:0000259|SMART:SM00967"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          52..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   534 AA;  59386 MW;  434DD671B6809196 CRC64;
     MSEDANEEES SGRMSRRKRF HESDSEFGKK SLVYAINYGN LKETAEKIMR EKMAEREAAR
     RRAHGLPEKE EELVDKNSPV FARPAKPFGD RGSNGELDSG NRSFKQRQSR DRQSGDRESQ
     DKQFSSKAFG DKEPRDRPFG ERHFGGGRER RTPQDRFSSE RRPPREDRPF GNSKNFELRT
     ERKKTLIGTP IVPYTTAASQ FLYGKSVVKS ALRAGRRKMY TLYIYNGDNR KDSPDDAMFI
     SLAKQRGIAW KLVPTDGQPM MDRMSQGRPH NGYVLEASPL PQPPVLSLGP CSENPWKKSF
     EIKIGFQTRE EELINGTNTT IPFETKINQK PLVLLLHEVV DPGNLGGIIR TALFMGVSAV
     AVTKNNSATL TPVVMKSAAG AVEEIPIFTV EDSTVFIEES RKTGWRTIAA VAPDPRRPDR
     SIGLDALAAE NPLAKDPCIL VLGSEGQGIP RHLRQKIDLD VSIPRMAKTS VVDSLNVSVA
     AGLLCHAFLQ DRSSRSPIGE AKAPSVVPEE TAEGATSTLA SNNLEKEEDS EQLF
//