ID   U6LZK2_EIMMA            Unreviewed;      1457 AA.
AC   U6LZK2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   02-OCT-2024, entry version 43.
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 + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167,
CC         Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609;
CC         EC=2.1.1.57; Evidence={ECO:0000256|RuleBase:RU368012};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU368012}.
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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   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
//