ID U6M140_EIMMA Unreviewed; 449 AA.
AC U6M140;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=NOL1/NOP2/sun family domain-containing protein, putative {ECO:0000313|EMBL:CDJ56808.1};
GN ORFNames=EMWEY_00024180 {ECO:0000313|EMBL:CDJ56808.1};
OS Eimeria maxima (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5804 {ECO:0000313|EMBL:CDJ56808.1};
RN [1] {ECO:0000313|EMBL:CDJ56808.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ56808.1};
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:CDJ56808.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Weybridge {ECO:0000313|EMBL:CDJ56808.1};
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}.
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; HG719122; CDJ56808.1; -; Genomic_DNA.
DR RefSeq; XP_013333458.1; XM_013478004.1.
DR AlphaFoldDB; U6M140; -.
DR EnsemblProtists; CDJ56808; CDJ56808; EMWEY_00024180.
DR GeneID; 25336404; -.
DR VEuPathDB; ToxoDB:EMWEY_00024180; -.
DR OrthoDB; 1268at2759; -.
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 InterPro; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023273; RCMT_NOP2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF17125; Methyltr_RsmF_N; 1.
DR PRINTS; PR02012; RCMTNOP2.
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|PROSITE-ProRule:PRU01023};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU01023};
KW S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023};
KW Transferase {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT DOMAIN 355..449
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..137
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 48314 MW; BC701069673B059A CRC64;
MKGRGGVLRA GKANKNSSSS SSSGKAAAAA AAAAAAAAGK KKKDLFESKK GKKRIEEEAA
AATDDEEESG GSAGDEDLLG SAEESEEEEG GEKFKVFSGS EGEEEEGEEG EEEEEEEEED
TQIMSYSSEE DDDDDEDEHK PTPKGTIPRD DPKGTIPGET IPGETIPGET IPGDDPRGDD
PRGDDPRGDH PRGDDPKRRS QGRRSQETIP GETIPGETIP GDTFVCVYVV FVLFAADDEE
SSESEEEAEA FVSGEGVRQL PLVDLRVVKA RMEETVGLLT KQKKKGDNKK GDTAAAPDDS
SSSSSSSSSS SKKSSKSRQE LLQLLRDDIV HYYQYSPELA EYFLQLFSPS QALAFFEANE
HRRPLTIRTN TLKIRRRDLA ALLISRGCNV DPLGDWTSVG LKVYDSNVPV GATPEYLTGL
YILQAASSLI PVIALAPQPD HILGKKGIE
//
