ID   L0AZW3_THEEQ            Unreviewed;       660 AA.
AC   L0AZW3;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=BEWA_033980 {ECO:0000313|EMBL:AFZ80541.1};
OS   Theileria equi strain WA.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=1537102 {ECO:0000313|EMBL:AFZ80541.1, ECO:0000313|Proteomes:UP000031512};
RN   [1] {ECO:0000313|EMBL:AFZ80541.1, ECO:0000313|Proteomes:UP000031512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA {ECO:0000313|EMBL:AFZ80541.1,
RC   ECO:0000313|Proteomes:UP000031512};
RX   PubMed=23137308; DOI=10.1186/1471-2164-13-603;
RA   Kappmeyer L.S., Thiagarajan M., Herndon D.R., Ramsay J.D., Caler E.,
RA   Djikeng A., Gillespie J.J., Lau A.O., Roalson E.H., Silva J.C., Silva M.G.,
RA   Suarez C.E., Ueti M.W., Nene V.M., Mealey R.H., Knowles D.P., Brayton K.A.;
RT   "Comparative genomic analysis and phylogenetic position of Theileria
RT   equi.";
RL   BMC Genomics 13:603-603(2012).
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; CP001669; AFZ80541.1; -; Genomic_DNA.
DR   RefSeq; XP_004830207.1; XM_004830150.1.
DR   AlphaFoldDB; L0AZW3; -.
DR   STRING; 1537102.L0AZW3; -.
DR   EnsemblProtists; AFZ80541; AFZ80541; BEWA_033980.
DR   GeneID; 15803875; -.
DR   KEGG; beq:BEWA_033980; -.
DR   VEuPathDB; PiroplasmaDB:BEWA_033980; -.
DR   eggNOG; KOG2198; Eukaryota.
DR   OrthoDB; 197651at2759; -.
DR   Proteomes; UP000031512; Chromosome 1.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA 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; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031512};
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          86..449
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        342
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         239
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         266
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         289
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   660 AA;  75690 MW;  071CBE0ECDAE8AD6 CRC64;
     MEDLGENSSK TVQIEENNAS STKRTRLGWK SRCREMQGVR WNKKSNANQN KDNERRNYVE
     GVPSNPEFEE YYRAQKICKD EEWDTFMEYN RKMLPVSFRL NTSVPLWKQT IEKLKEMVSE
     DSELALRQCI DYSPEYLKPE DCIFYQMKTD KFSLRKNESF SRLHKFIMSE DNRGSLSRQE
     TVSMLPVLFL DPQPNENILD LCAAPGMKYL QIIDIVESKL QFLEKLDSSK NKGIIIGNDI
     CQNRVSTLSH HMKSLNSPSS AITNYDASRF PYLYNSNGEK ILFDRILADM PCSCDGTLRK
     SIEIWKTWKP TNGLHMHKIQ LSILKRAIQI LKPGGLLIYS TCSLNPLENE AIASYIASDE
     GKELGVRLEP LKQIKGMKYA TGVVDWFVPN PNGGHFEKYE QVDKSLHNRI LPSMFKSENW
     NAETASLVRR ILPHHNDTGG FFIFAIRKNT SGYSSSDQLE VPDPVKTDTT DVISVESQKD
     SKRKHANAGK LLHEFCLWKE SDEDYSNVLK FYGIDKDADI VDQMIVKLST KKSVYLFSKS
     DVVYRGYKRK NSGDSNNRYE LCKYALAGTR IFTQLKSKTI PVNCDLRITQ EGTKVLYPYS
     TRRKLFCNLV FGKLIIKGTI SKDVLLEAES NNNLANLDSC KGAGGELESG GYIYMYKAKY
//