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Database: UniProt
Entry: Q4UBT4_THEAN
LinkDB: Q4UBT4_THEAN
Original site: Q4UBT4_THEAN 
ID   Q4UBT4_THEAN            Unreviewed;       366 AA.
AC   Q4UBT4;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Nucleolar protein, putative {ECO:0000313|EMBL:CAI75717.1};
GN   ORFNames=TA04885 {ECO:0000313|EMBL:CAI75717.1};
OS   Theileria annulata.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC   Theileriidae; Theileria.
OX   NCBI_TaxID=5874 {ECO:0000313|EMBL:CAI75717.1, ECO:0000313|Proteomes:UP000001950};
RN   [1] {ECO:0000313|EMBL:CAI75717.1, ECO:0000313|Proteomes:UP000001950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ankara {ECO:0000313|Proteomes:UP000001950};
RX   PubMed=15994557; DOI=10.1126/science.1110418;
RA   Pain A., Renauld H., Berriman M., Murphy L., Yeats C.A., Weir W.,
RA   Kerhornou A., Aslett M., Bishop R., Bouchier C., Cochet M., Coulson R.M.R.,
RA   Cronin A., de Villiers E.P., Fraser A., Fosker N., Gardner M., Goble A.,
RA   Griffiths-Jones S., Harris D.E., Katzer F., Larke N., Lord A., Maser P.,
RA   McKellar S., Mooney P., Morton F., Nene V., O'Neil S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rawlings N.D., Rutter S., Saunders D.,
RA   Seeger K., Shah T., Squares R., Squares S., Tivey A., Walker A.R.,
RA   Woodward J., Dobbelaere D.A.E., Langsley G., Rajandream M.A., McKeever D.,
RA   Shiels B., Tait A., Barrell B.G., Hall N.;
RT   "Genome of the host-cell transforming parasite Theileria annulata compared
RT   with T. parva.";
RL   Science 309:131-133(2005).
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; CR940352; CAI75717.1; -; Genomic_DNA.
DR   RefSeq; XP_955193.1; XM_950100.1.
DR   AlphaFoldDB; Q4UBT4; -.
DR   STRING; 5874.Q4UBT4; -.
DR   GeneID; 3864935; -.
DR   KEGG; tan:TA04885; -.
DR   VEuPathDB; PiroplasmaDB:TA04885; -.
DR   eggNOG; KOG2198; Eukaryota.
DR   InParanoid; Q4UBT4; -.
DR   OMA; WNREYAS; -.
DR   OrthoDB; 8499at2759; -.
DR   Proteomes; UP000001950; Chromosome 3.
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; IPR023269; RCMT_subfamily_9.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF16; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02010; RCMT9.
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:UP000001950};
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          24..365
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        265
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         121..127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         150
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         203
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   366 AA;  42370 MW;  979A622489C77562 CRC64;
     MDSLIDIQNH YENKVLPYNP DLLSHKLDSW LEDLGVDVEK YKNEITDILS SRKYRYYRKV
     GDCNFPDDRV VLWLRDVEVY NTTGNIPPSC YGLDASSAAV VDSLRLKRLS SAKEAWVLDM
     CCAPGGKLFA TIDAADKIRS DTKWNIIGLD SSIRRIELCK SMLKKELFDR DRIDVNFKFI
     NSQEFSEFNG ESMFEKFDRI ILDVECTLEG SLRSVIRTLR FWGIKWLENN WNREYASKII
     ANQRELLTQA IKLVKPGGFI VYSTCSLDKE QNEHLLCDVI KQFQNIKFHP LPIHSCSCCS
     YNSEERQETW PAESCEHILK LKCSDEYFYS VNMNHCNNKN SPSAVRFVPL NGKTDGLFIA
     LLFKTI
//
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