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Database: UniProt
Entry: U6LC57_9EIME
LinkDB: U6LC57_9EIME
Original site: U6LC57_9EIME 
ID   U6LC57_9EIME            Unreviewed;       615 AA.
AC   U6LC57;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03162};
DE            EC=2.1.1.205 {ECO:0000256|HAMAP-Rule:MF_03162};
DE   AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog {ECO:0000256|HAMAP-Rule:MF_03162};
GN   ORFNames=EBH_0013570 {ECO:0000313|EMBL:CDJ46813.1};
OS   Eimeria brunetti.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX   NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ46813.1};
RN   [1] {ECO:0000313|EMBL:CDJ46813.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ46813.1};
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:CDJ46813.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Houghton {ECO:0000313|EMBL:CDJ46813.1};
RA   Aslett M.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and
CC       34 of the tRNA anticodon loop of substrate tRNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_03162}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine
CC         = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 H(+) +
CC         2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42396, Rhea:RHEA-
CC         COMP:10246, Rhea:RHEA-COMP:10247, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:74445, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748;
CC         EC=2.1.1.205; Evidence={ECO:0000256|ARBA:ARBA00035600,
CC         ECO:0000256|HAMAP-Rule:MF_03162};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03162}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03162}.
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DR   EMBL; HG710493; CDJ46813.1; -; Genomic_DNA.
DR   AlphaFoldDB; U6LC57; -.
DR   EnsemblProtists; CDJ46813; CDJ46813; EBH_0013570.
DR   VEuPathDB; ToxoDB:EBH_0013570; -.
DR   OrthoDB; 119516at2759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0106339; F:tRNA (cytidine(32)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106340; F:tRNA (guanine(34)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002181; P:cytoplasmic translation; IEA:UniProtKB-UniRule.
DR   GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   HAMAP; MF_01547; RNA_methyltr_E; 1.
DR   HAMAP; MF_03162; RNA_methyltr_E_TRM7; 1.
DR   InterPro; IPR028590; RNA_methyltr_E_TRM7.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10920:SF12; TRNA (CYTIDINE(32)_GUANOSINE(34)-2'-O)-METHYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03162};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_03162};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_03162};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03162};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_03162}.
FT   DOMAIN          278..408
FT                   /note="Ribosomal RNA methyltransferase FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
FT   REGION          43..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        365
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         170
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         172
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         284
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         300
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         325
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
SQ   SEQUENCE   615 AA;  63936 MW;  4CB400E70BC95A1B CRC64;
     MGRISRDRRD IYYRRAKEEG FRARSAYKLL QLDDELHFLS PPALAAEEET SSCSSSSSCS
     SSSSSEGESD GADESSSSEV EEGVGARGNG KERKKGKREY SVSGEPVWPS CTLHPAAETA
     KKNREKSGKN QPPSDLDSNL NKKKSNKIQF SSFSIHDYPH RAVDLCAAPG SWTQVLRRRL
     WRNYELKLEE YNKYKQQQQQ QQQQQQQQQQ QDGEGIGSSD GSSSLQPEAA AATATAGPAA
     TAATAGPAAA AAAGPAAAGP AAGPAAAAAD AMQPPAPPMI VAVDLQELAP IPGVHTLQGD
     ITHASTAAAI LSFFEHKAAD LVVCDGAPDV TGMRDVDEYL QQQLLLAAAA TAARVLRPGG
     CFVCKIFRGE FTPLVYVQLM AFFADVRCCK PAASRSSSIE AFLFCRGFQP KLQRCCQPSA
     KKETERDTGA APAAAAPAAA AAAAADGDGD AAGGAAGEAA AGEGTVATAA SAAAAAAAAA
     AAAECSSSSS SSSSSSEGLA SKWAEEVIGC LVPFLNCGDI RGMDADRNYT LARVLQQQQQ
     QQEGAEGREK GRRLFVDRQE AALGLPVKSS SKQQQQQQTA TAAANNSSSS SSNRAQQQQQ
     TAAAAAAAAA ANPKP
//
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