ID A0A1A0HID0_9ASCO Unreviewed; 455 AA.
AC A0A1A0HID0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=S-adenosyl-L-methionine-dependent methyltransferase {ECO:0000313|EMBL:OBA23756.1};
GN ORFNames=METBIDRAFT_35104 {ECO:0000313|EMBL:OBA23756.1};
OS Metschnikowia bicuspidata var. bicuspidata NRRL YB-4993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowia.
OX NCBI_TaxID=869754 {ECO:0000313|EMBL:OBA23756.1, ECO:0000313|Proteomes:UP000092555};
RN [1] {ECO:0000313|EMBL:OBA23756.1, ECO:0000313|Proteomes:UP000092555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL YB-4993 {ECO:0000313|EMBL:OBA23756.1,
RC ECO:0000313|Proteomes:UP000092555};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., LaButti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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:OBA23756.1}.
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DR EMBL; LXTC01000001; OBA23756.1; -; Genomic_DNA.
DR RefSeq; XP_018714237.1; XM_018856573.1.
DR AlphaFoldDB; A0A1A0HID0; -.
DR STRING; 869754.A0A1A0HID0; -.
DR GeneID; 30029549; -.
DR OrthoDB; 102852at2759; -.
DR Proteomes; UP000092555; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR048889; NSUN5_RCM1_N.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807:SF4; 28S RRNA (CYTOSINE-C(5))-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF21153; NSUN5_N; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000092555};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01023}.
FT DOMAIN 129..453
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 368
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 262
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 311
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 455 AA; 50935 MW; 95F991C88F8A72E0 CRC64;
MKLYFEAEKF LKGGERGLKT RIFNAKLSNS PKHIYALVIS ALKYKEYIQH IVRKARLKDA
PELKKLKVSE ALLALLVYDF LFSAKGRIQL GKHPVKDAFL ANKTRMQAEL TKLKLKHGVK
SVAELPMKSG LDDDETPVRW IRINTIKLNA AAFFKKHPFF AELTAVDDLA QITGPGVIFK
DPYIQNLYGI HPREKLTNTS AYLHGEVIIQ DRASCFPGEI LFNDPSDVHT QIIDATAAPG
NKTTHAASFV AHSENSVVFA FERDDKRVKV LKMMCEKATG KLKKGLIHPT HADFTTVLPQ
DFPQVSGLIV DPSCSGSGIF GRAIEDALEQ AKEDIDTERL QKLAAFQFTI MKHALSFPKA
RKVVYSTCSI HPHENERVVV DLLRDVAVQA QGWHLAPRDH VIALWPRRGW KEEFTSLCEG
DDDRCSELAG GCVRSVPKED GGIGFFAACF VRDEQ
//
