ID A0A0G2I7K7_9EURO Unreviewed; 643 AA.
AC A0A0G2I7K7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 28.
DE RecName: Full=rRNA methyltransferase 1, mitochondrial {ECO:0000256|ARBA:ARBA00034881};
GN ORFNames=EMCG_08011 {ECO:0000313|EMBL:KKZ66240.1};
OS Emmonsia crescens UAMH 3008.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=1247875 {ECO:0000313|EMBL:KKZ66240.1, ECO:0000313|Proteomes:UP000034164};
RN [1] {ECO:0000313|Proteomes:UP000034164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 3008 {ECO:0000313|Proteomes:UP000034164};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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:KKZ66240.1}.
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DR EMBL; LCZI01000501; KKZ66240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2I7K7; -.
DR VEuPathDB; FungiDB:EMCG_08011; -.
DR Proteomes; UP000034164; 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; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR013123; SpoU_subst-bd.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 285..376
FT /note="RNA 2-O ribose methyltransferase substrate binding"
FT /evidence="ECO:0000259|SMART:SM00967"
FT REGION 44..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 71116 MW; 0B90DAA97FE6A747 CRC64;
MLNRHCSSLL KSHRLCFAGF SEHSFAKGIR HASIGSAIQK GIYTSRNSYP GRENRENRES
GERRGGRGSS ENWGNRWNGE DRGNRGNRED RGDRENRKNR ENRDNRDNRD SRGNWENRDG
RDGREGREGR ESRGGRANPS WTPRGSQGNF RNGNDRQRPS DESNFSGSDS RVRFLRAPDE
SRSDWRSSEM ETGGYSAPTF RPANTRPTWN QHDAQRNNEN RSDNRMFGSE SNFSRPKNRR
ERYAEKRSDR SEQTEFELER PPHTQPHVSI TAPHAVPYTT AASEFIYGTS AVLAALRCGR
RKLYKLYIHE TPDKVSLRLG RKQSREPMLD TIIKFGLAAG VQVKQVAGNW PKLLDKMSGG
RPHNGCILEA SQLPKLPVDS LLPVTSPSET HFNATVCQQS AEEAEVNGTS GRIPRSAYKD
EDSSSTENEV KPTRYPFALL LDGIRDEGNV GAIIRSAYYF GVDAVIVSTR SSAPISAVAI
KASAGAAENI PILTTTNPTL FVKNTHMNGW KFYAAEAPAA ANASQQTLGT STEQILSRRD
VSTKLNEAPC VLMLGSEDQG LQRSVRQQAD GAVVIPGALT SNSEKDRAGV DSLNVSVASA
LLCEAFLGDP SSTGLGSSPA DEGMMSTVDM IREEAKEDPN KMF
//
