ID U6GLH6_EIMAC Unreviewed; 2049 AA.
AC U6GLH6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 22-FEB-2023, entry version 39.
DE RecName: Full=rRNA adenine N(6)-methyltransferase {ECO:0000256|RuleBase:RU362106};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU362106};
GN ORFNames=EAH_00043370 {ECO:0000313|EMBL:CDI79464.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI79464.1};
RN [1] {ECO:0000313|EMBL:CDI79464.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI79464.1};
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:CDI79464.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI79464.1};
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. rRNA adenine N(6)-methyltransferase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01026, ECO:0000256|RuleBase:RU362106}.
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; HG671030; CDI79464.1; -; Genomic_DNA.
DR RefSeq; XP_013250434.1; XM_013394980.1.
DR EnsemblProtists; CDI79464; CDI79464; EAH_00043370.
DR GeneID; 25272407; -.
DR VEuPathDB; ToxoDB:EAH_00043370; -.
DR OMA; DICNIAW; -.
DR OrthoDB; 1337at2759; -.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001737; KsgA/Erm.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11727; DIMETHYLADENOSINE TRANSFERASE; 1.
DR PANTHER; PTHR11727:SF18; RRNA ADENINE N(6)-METHYLTRANSFERASE; 1.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR Pfam; PF00398; RrnaAD; 1.
DR SMART; SM00650; rADc; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01026}; RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01026};
KW rRNA processing {ECO:0000256|RuleBase:RU362106};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PROSITE-ProRule:PRU01026}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU01026}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2049
FT /note="rRNA adenine N(6)-methyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004671343"
FT DOMAIN 234..382
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT REGION 58..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1226..1245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1608..1640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1674..1719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1788..1840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 851..886
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1301..1390
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 452..477
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 222
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 294
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 316
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 337
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 2049 AA; 221389 MW; F7AB1BDD57C9117A CRC64;
MIVLGEASVF VWLLAAAAAA HTAAVYTPQL SAAAPLSNQQ QQQQQQQQQQ LFPLFLSVPD
LSPRPTAATG GPPLLLKRRG GPSSSHRGAP LSLLRGAPSG APFEGRPYRG CPKRREGGPP
EAKEGGPPGG PPGGPPGASR SAFRPLENLQ IYPLKQNPQQ QTGGPPELPV ERGGPLEGPL
EGPREGPRDG APLVLDASAE EGTARLPRGE FRPKQSLGQN FLADANICRR IVKAFKGAVA
AAAQREAQQQ QQQQQQQQGG AGAAPLSRVV EVGPGTGALT RLLYPLYPDM LAVEIDPRAI
ALLSQRLPGL QLLHEDVLQV NWPYLGHHMQ RLRIVGNLPF YLTSQLLFCL LDCRHYIDLA
VVTLQKEVAE VESAVVRVDF RHESDEELLN GVLFAAFGQR RKMLRHSLKV GLGAPGAPMY
PPPGAPSNGA RGPGGPHCLL RRWGPLRPTT ALPLPLKGPP SVGPPGVGPP GVGPPGVGPQ
GVGPLRGPRL VVTGPLGAPQ GAPVPYAAAW SSLRSGGPRT QQHLLLLLLL QVHRATYTTR
RLSSSSSSYS SSSNTSSKGS SSSVKQQEAA SSAPNLHQRG PPSKTFWGPP NARQLMSGLL
ARGGSPLAAT AAAAAAAPSS SSSSRSSSSS RQGVAAVLQY SQQHLEAFDA VHCATALLLL
GRIYRQQGHA AAAAAAAASA AAAFQKSPQQ HYQKQQQQQQ QQQQQQQLLL PQSLPPFLRL
LYTNPTFSAL RSKLLRHLEA LTVGSSSNSS RSNSSSSSSS SSSSTRQLVS NTLWALGALG
ACDVPLALAA VAVLQPLLQP LLQQLQQQQQ QQQQQQQQLL LLLPVDICNI AWGLATMLDR
SGAALIASLP SQQQQQQHKQ QQQQQQQQEQ QEAAEARLQL QAAVKETFAG LAVSFLQQVE
AFEARGYSTV IWAAAKAAVY RHPEDAAAKQ QTLSALLQVQ NNNLRALQQL LQQQQQQQQH
QQPQPKQQEQ QQQHPQQQQQ QQQQQQTKLI RGQEVTVAAH SSATQSGGGP PVGAPRMSSP
EKETEGLIEV QQGAAAACKA TFMRIYSSSN SAAVSLGGPL RGPPWGPLGA SSSCAQSAVF
KCLFKASLNC LLRPQGLQQL SPQQIANVLW AFAAVGEVSP SLCAAAAAEL LRRAQASFCL
GGAPKGGLPA AAKPSKCLLP ERDSSGLEVS LHASQKETMQ KQGGPQQGGP PLSCRDVAAA
LLASSQQQQF PEALFVSLPK LLISNSNSSN SSSSSNSNSS SSSSSRFLGE ASLRDLAGLC
IGLQRAAESK AGGPLLQLQL KRHGAPPERR LLRQLVRRHL KETAALLGAD AEKRIQELQQ
QKQQQQQQKL QQQKQQLLQQ QLLLLLQQQE QQQEQHQEQL LQDKKLHSGK RDSNEDLEQQ
QEQQQQQQQE RYMAAAILVW RSVCREIMQR LKLGGPRGLA FGGPRITSKG DSKLLLQGPP
EGIGCLRDLW ALTCCLSTVS FLSPSLLRGL TSAALLVAET RSSKCIREQT IQQQQQQQQQ
HQQQQQSQQQ QQQQPDQQQH QHQPKQQQQQ QQQQQQQQQK QQQQQQQQQQ QQQQQANGSR
PPLSPRWALR GGLQKEMPRA LLSTDDFLVV YKPPYWLANA QQTAAGAPGG PFGFDTPPWA
SWGAPGGPLS SNLSPPTTKG DNRLLFSEAL LNSGRPEPLH LFLRARVQEG ALPLLPGAPA
DTTQGGPHGS PHEGPHGGPH GGPHLSSSRY KGAPTKEVSP NAEFVSVLSD SSVSSGCTHR
LDCETSGPLL FAKTSRGFHF ARMQFEAHTL NKFYLALVHG RVQQQQQQEE QQQKEQQQQS
ELQQQNKRMG EQQKEQQQKL QEQQHQQNEQ QQQQQQQQME QQQQMSWGGL KLLQGSEGFW
GVSGPIETLK GPPPHNHIFS ICSRVYSLLL VKLLTGRTHQ IRIHLSTMGH PIAADYKYHK
GQKQQLLQHL LLDSAAHPCC WFLSLMVAVS AVAAAASAVA AAAAAAVAVA ADPSSYLFDL
SWCPRLFLHC CYLGVVQQQF KGGPPGGPSV GRQGAPGAPL QMRDLEVYSE LPSDLAEALR
CLEVVSVCV
//