GenomeNet

Database: UniProt
Entry: U6KX56_EIMTE
LinkDB: U6KX56_EIMTE
Original site: U6KX56_EIMTE 
ID   U6KX56_EIMTE            Unreviewed;       905 AA.
AC   U6KX56;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=NOL1/NOP2/sun family domain-containing protein, putative {ECO:0000313|EMBL:CDJ42546.1};
GN   ORFNames=ETH_00033305 {ECO:0000313|EMBL:CDJ42546.1};
OS   Eimeria tenella (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ42546.1};
RN   [1] {ECO:0000313|EMBL:CDJ42546.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ42546.1};
RA   Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA   Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA   Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA   Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA   Tomley F., Pain A.;
RT   "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDJ42546.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ42546.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) 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}.
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DR   EMBL; HG675723; CDJ42546.1; -; Genomic_DNA.
DR   RefSeq; XP_013233296.1; XM_013377842.1.
DR   AlphaFoldDB; U6KX56; -.
DR   EnsemblProtists; CDJ42546; CDJ42546; ETH_00033305.
DR   GeneID; 25255727; -.
DR   VEuPathDB; ToxoDB:ETH2_1417500; -.
DR   VEuPathDB; ToxoDB:ETH_00033305; -.
DR   OMA; LHRCMRF; -.
DR   OrthoDB; 197651at2759; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
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; IPR023270; RCMT_NCL1.
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   PRINTS; PR02011; RCMTNCL1.
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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          52..476
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          481..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          767..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        366
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         177..183
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         221
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         313
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   905 AA;  98421 MW;  7B970E37BC9C0E32 CRC64;
     MGRRNPSKKA SQETAGADGD GIWQNGVVRH SAAFESFYKE QKIVPEEEWT AFLECLQSDL
     PTAFRVVSIT PFRHYVHKFL QKTLESLQED AAAAASCAAD MRGALKPLEW YKSGYEAFQL
     DVSRHVLRTC KPLLSLHKFL VEQSEAATIY RQEAVSMIPA LFLEKEMRGD SLILDMCAAP
     GSKTSQLLEA LHQACERERR KNGEEVDGWP PLPTGAIVAN DADVTRSHML VHHLRHLHSP
     CLLVTSHAAQ FFPTVFHPLR SEDAATGPAA AATAAPEGAD VLLGSNSNGS SSSSSKEETA
     RLVPIQFDGV LCDVPCSGDG TLRKSRALWA SWSPHQGLGC HRLQLQILLR GIKLCKVGGR
     IVYSTCAFNP IENEAVVCAA ITKSRGAVEL EDCSGDLPSL RRSPGKSSWR VEWEGRWYDF
     FDEVPKTAKA TKKLRQSMFP PVGEPGEPAV PLHRCMRFLP HINNTGGFFV AVLRKVREVP
     LAPGSASGDG SRSESNPCGP LDHLEDPEKV QKDIENKREA DGIPEDEDPA AAAAGAPAAR
     RFEQIQLDMV GLDWQPELLQ QQQQQLLAQE KRLELDGEAE KDLKPVASEA TAAAAAALQA
     SAAAAASSPR CAPPLQPGTS PLALSRAILE QILQLAFETL EIRGEISARK STSPELRAAA
     QRLSSHLYFR LKTAESADSG DLESLEGNLG NEDNSERYPR RLFFVSQGVK SLVRAVGASR
     YKIINGGCLA FQARARGVYR IAYGAAQWLA PFCELLSGCA ADSPLQQQQQ QQQQQQQLAA
     HAGGPADCGL PAESSEAERR RVLHIPCQLL YGLVATKQED RRVPFKKIQE LPCGQALVNS
     SCDGSLLFLA KIPQAAGCSS SFTNVAVPAW RGRTNVELML DSNSRLALRS LMEESGVPAT
     EGESL
//
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