ID U6LZK2_EIMMA Unreviewed; 1457 AA. AC U6LZK2; DT 22-JAN-2014, integrated into UniProtKB/TrEMBL. DT 22-JAN-2014, sequence version 1. DT 27-NOV-2024, entry version 44. DE RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1 {ECO:0000256|RuleBase:RU368012}; DE EC=2.1.1.57 {ECO:0000256|RuleBase:RU368012}; DE AltName: Full=Cap1 2'O-ribose methyltransferase 1 {ECO:0000256|RuleBase:RU368012}; GN ORFNames=EMWEY_00008200 {ECO:0000313|EMBL:CDJ57397.1}; OS Eimeria maxima (Coccidian parasite). OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia; OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria. OX NCBI_TaxID=5804 {ECO:0000313|EMBL:CDJ57397.1, ECO:0000313|Proteomes:UP000030763}; RN [1] {ECO:0000313|EMBL:CDJ57397.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ57397.1}; 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:CDJ57397.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ57397.1}; RA Aslett M.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that CC mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of CC RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG- CC capped mRNA to produce m(7)GpppNmp (cap1). CC {ECO:0000256|RuleBase:RU368012}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + S- CC adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:67020, Rhea:RHEA- CC COMP:17167, Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, CC ChEBI:CHEBI:167609; EC=2.1.1.57; CC Evidence={ECO:0000256|RuleBase:RU368012}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368012}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HG719272; CDJ57397.1; -; Genomic_DNA. DR RefSeq; XP_013334045.1; XM_013478591.1. DR EnsemblProtists; CDJ57397; CDJ57397; EMWEY_00008200. DR GeneID; 25334806; -. DR VEuPathDB; ToxoDB:EMWEY_00008200; -. DR OMA; ANTEDCA; -. DR OrthoDB; 205623at2759; -. DR Proteomes; UP000030763; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule. DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-UniRule. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0016556; P:mRNA modification; IEA:UniProtKB-UniRule. DR Gene3D; 3.40.50.12760; -; 2. DR InterPro; IPR050851; mRNA_Cap_2O-Ribose_MeTrfase. DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom. DR PANTHER; PTHR16121:SF0; CAP-SPECIFIC MRNA (NUCLEOSIDE-2'-O-)-METHYLTRANSFERASE 1; 1. DR PANTHER; PTHR16121; UNCHARACTERIZED; 1. DR Pfam; PF01728; FtsJ; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Methyltransferase {ECO:0000256|RuleBase:RU368012, KW ECO:0000313|EMBL:CDJ57397.1}; mRNA capping {ECO:0000256|RuleBase:RU368012}; KW mRNA processing {ECO:0000256|RuleBase:RU368012}; KW Nucleus {ECO:0000256|RuleBase:RU368012}; KW Reference proteome {ECO:0000313|Proteomes:UP000030763}; KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU368012}; KW Transferase {ECO:0000256|RuleBase:RU368012, ECO:0000313|EMBL:CDJ57397.1}. FT DOMAIN 895..975 FT /note="Ribosomal RNA methyltransferase FtsJ" FT /evidence="ECO:0000259|Pfam:PF01728" FT REGION 26..63 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 107..137 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 292..360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 379..423 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 666..685 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 859..900 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 982..1034 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1047..1098 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1133..1175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 772..799 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1177..1207 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 1414..1451 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 300..353 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 379..422 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 859..895 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 991..1034 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1048..1098 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1135..1170 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1457 AA; 156658 MW; 1BBD48AC41F8C16D CRC64; MPAVQGELKD AQEAVIDSLG FQQRQISLEY PQGTQQHGYE QQQQEQPQQQ QQRESGGSSF SSSYHTLLSV GKELLQQQMK QKQQQQHCVT DSSKLMELLL QLQQQQQQQQ NGQAHEADVS STGAPASEAA AMAATSSTTT DTATAAADTA ASPAAAAKEE TLQVAAQPTY LGAAELAAQL AAATAATKAV PAAAVSTTAG DAASAATAAA TTTTTDRHAF MQQQLLMAKT LCYNLSAADG EEERQTSLFY WRETRVGSQA AAAAAALGAV RMAAHAAAAA VEAAAHETVP ADTAAPAAAA SPSENATTST SSQDSEEHLA AAARLQQQQQ QQQQKKQQQQ QQQQQQQEQN MRREQIRSSA RRCYTPAARL FLDVQPLECS SSNNNSSSSN NSNSSSNNGT KHSGRRNSSN SSSNSSRRSA SHDALMVTAA KQARGSQWLP TAREGASAEQ TLAVAAAAAA AATAAAATAA TSPAAASTHL LKTATSATAE AAGETAPAPA AASSSTAAGA APAAAAGAGA AAAEPVRIVQ DVLYLYPMCP KRLTVSAVCT PHLVQSLLEH KTKLGDIFDS GQDQLYHRAR AAVFPQDSCG SVRHKNRAGD KVEELNLCAE RWCRRNCSSS NSSSSSSSSS SSNGKVCCGL VGALRKVPPS AAAPCSTTVQ GGEQQQGAAA NGARGHDAPA TTTTTAAAAA AAAGAAADAP PERKPVRVFI DLCGGPGAWS LYLLGRTATT DRAAATATAE AAAAAAAAGG PHADNKLNNG MTNDKDLFAA ITAEVLRRLA ESQSRMEQQQ QQQQQQQQAE VYGLGITLML PDTAPLDSWY AALTSNPRFT PLWGGDGTGD LCAPGNIEST AQAVFEFLRS KQQQQQQPQQ QQQQQQQQQQ QQQQLGSNTQ GRQHNLADPV PGFEEGVTLV MADGAAVTNP NDILHQDETL QELFSGRLLL AEFLAALLLL QQGGHFVIKI FDSFSVFTAS LVYAVEELQE QQRGRNRGSK HKPPQQQQRQ QQQQQQQHNY HNSNNSNSNS SYNNSSSSNI PPLSSPIHKI LEQLRLCRGP PSSNSSSSSS SRSNKRSAGS NNTPTLATKA SRHFPQRQQQ QRQPQQQQQQ QKQVQQMLQQ QLLQQQQLQQ QQQLRDLHSP LDRSKAFRTP NSNSSSSSNN SNSSSNCCLP DGLQQQWQQQ QKRDRNKELM QQQLRYLEQQ LQQQREDQKK QQELQLQLQL MQMQQLQLMQ MHRQFTPVNP AALQQQLLLQ QQLQQQQQML QLLKPQQQQM QQLQQQQQQQ QQQQQAGIYR QQLQGTSLAQ QQQLLLRQQL QQQQHRQQQQ AAKKGGDRTL AGGMLGMAAV GGAAAAAAAP TAAAAAAAAA AVTPLTQARQ RHKQQQQNPQ QQQLLLQQML LKQGGQHGAF AAAELKKTQA VSPSMMVAAG QEQQQQQQQQ LLLLQQERDR LALQQQQLEE LQQKLMKATS LGLEGQQ //