ID W7AN61_PLAVN Unreviewed; 498 AA.
AC W7AN61;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=5-methylcytosine rRNA methyltransferase NSUN4 {ECO:0000256|ARBA:ARBA00040337};
DE AltName: Full=5-methylcytosine tRNA methyltransferase NSUN4 {ECO:0000256|ARBA:ARBA00041914};
DE AltName: Full=NOL1/NOP2/Sun domain family member 4 {ECO:0000256|ARBA:ARBA00042050};
GN ORFNames=PVPCR_0900920 {ECO:0000313|EMBL:CAD2103711.1}, YYG_01728
GN {ECO:0000313|EMBL:EUD72728.1};
OS Plasmodium vinckei petteri.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX NCBI_TaxID=138298 {ECO:0000313|EMBL:EUD72728.1, ECO:0000313|Proteomes:UP000030659};
RN [1] {ECO:0000313|EMBL:EUD72728.1, ECO:0000313|Proteomes:UP000030659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:EUD72728.1,
RC ECO:0000313|Proteomes:UP000030659};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium vinckei petteri CR.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CAD2103711.1, ECO:0000313|Proteomes:UP000515268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ramaprasad A.;
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in rRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61484, Rhea:RHEA-COMP:15836, Rhea:RHEA-COMP:15837,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00036484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cytidine in tRNA + S-adenosyl-L-methionine = a 5-
CC methylcytidine in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:61468, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:15827,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000256|ARBA:ARBA00036266};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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}.
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DR EMBL; LR865414; CAD2103711.1; -; Genomic_DNA.
DR EMBL; KI965397; EUD72728.1; -; Genomic_DNA.
DR AlphaFoldDB; W7AN61; -.
DR EnsemblProtists; EUD72728; EUD72728; YYG_01728.
DR VEuPathDB; PlasmoDB:PVPCR_0900920; -.
DR eggNOG; KOG2198; Eukaryota.
DR OrthoDB; 317522at2759; -.
DR Proteomes; UP000030659; Unassembled WGS sequence.
DR Proteomes; UP000515268; Chromosome PVPCR_09.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808:SF3; 5-METHYLCYTOSINE RRNA METHYLTRANSFERASE NSUN4; 1.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 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}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
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 111..421
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 202..208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 314
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 498 AA; 57483 MW; A916D4C79E4BB13E CRC64;
MKCSGKVGYF LNLKKEYGDR AEVLMKKLEE GKTVQAAFIN DFIKIDYINI FKVLLYMIKD
KKVKTSFGGL FVDEKYANLL TYFATSENNN NLSYEIITQN SCKHNENCDS VNVASQLDGG
TIVQYNTSDE NAKSGLYEKT ESNGDYRKIT ISKSELLNID GVIKYDGMIE NVEKLAYYLN
PCSFLSAYFL DVKKNEHVLD MCAAPGGKSL IIANKLFGFD ISPLDRINNI NILDDKNIEI
NCCLNVLNYY KVNREGCLVV NEFNKARYDR LKQVLHKHLP SDLIKSGNLH ITNYNGLQLN
SFIRFQKFHK ILLDVPCSTD EHLIKKGTND INKWTFNSIK NNSNIQYDLL VNSFHLLHKN
GVIIYSTCAL SHYENDYNIE RFIKKFKKEV KILDFLEEEY ERVYKEKIMN NHTIENDSHM
PCHCKMETPD NSTNHANHNV SCTSHTNNDA SCTNTKNFSE FKKNTNFLKF FEKTKYGYIS
LPDKSPFGIL YICKIKKI
//