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Database: UniProt
Entry: Q17ME6_AEDAE
LinkDB: Q17ME6_AEDAE
Original site: Q17ME6_AEDAE 
ID   Q17ME6_AEDAE            Unreviewed;       852 AA.
AC   Q17ME6;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   RecName: Full=Putative rRNA methyltransferase {ECO:0000256|HAMAP-Rule:MF_03163};
DE            EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_03163};
DE   AltName: Full=2'-O-ribose RNA methyltransferase SPB1 homolog {ECO:0000256|HAMAP-Rule:MF_03163};
GN   Name=5579906 {ECO:0000313|EnsemblMetazoa:AAEL001037-PA};
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159 {ECO:0000313|EnsemblMetazoa:AAEL001037-PA, ECO:0000313|Proteomes:UP000008820};
RN   [1] {ECO:0000313|EnsemblMetazoa:AAEL001037-PA, ECO:0000313|Proteomes:UP000008820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL001037-PA,
RC   ECO:0000313|Proteomes:UP000008820};
RG   Aedes aegypti Genome Working Group (AGWG);
RA   Matthews B.J.;
RT   "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AAEL001037-PA}
RP   IDENTIFICATION.
RC   STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL001037-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) to UniProtKB.
CC   -!- FUNCTION: Probable methyltransferase involved in the maturation of rRNA
CC       and in the biogenesis of ribosomal subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_03163}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleotide in rRNA + S-adenosyl-L-methionine = a 2'-O-
CC         methylribonucleotide in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:48628, Rhea:RHEA-COMP:12164, Rhea:RHEA-COMP:12165,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90675, ChEBI:CHEBI:90676; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03163};
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000256|HAMAP-
CC       Rule:MF_03163}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03163}.
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DR   RefSeq; XP_001657887.1; XM_001657837.1.
DR   AlphaFoldDB; Q17ME6; -.
DR   STRING; 7159.Q17ME6; -.
DR   PaxDb; 7159-AAEL001037-PA; -.
DR   EnsemblMetazoa; AAEL001037-RA; AAEL001037-PA; AAEL001037.
DR   GeneID; 5579906; -.
DR   KEGG; aag:5579906; -.
DR   VEuPathDB; VectorBase:AAEL001037; -.
DR   eggNOG; KOG1098; Eukaryota.
DR   HOGENOM; CLU_009422_8_1_1; -.
DR   InParanoid; Q17ME6; -.
DR   OMA; DITTEDC; -.
DR   OrthoDB; 119516at2759; -.
DR   Proteomes; UP000008820; Chromosome 3.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; 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_03163; RNA_methyltr_E_SPB1; 1.
DR   InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR   InterPro; IPR015507; rRNA-MeTfrase_E.
DR   InterPro; IPR012920; rRNA_MeTfrase_SPB1-like_C.
DR   InterPro; IPR024576; rRNA_MeTfrase_Spb1_DUF3381.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR028589; SPB1-like.
DR   PANTHER; PTHR10920:SF13; PRE-RRNA 2'-O-RIBOSE RNA METHYLTRANSFERASE FTSJ3; 1.
DR   PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR   Pfam; PF11861; DUF3381; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF07780; Spb1_C; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_03163};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_03163};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03163};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008820};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_03163};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_03163};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_03163};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03163}.
FT   DOMAIN          24..199
FT                   /note="Ribosomal RNA methyltransferase FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
FT   DOMAIN          236..396
FT                   /note="DUF3381"
FT                   /evidence="ECO:0000259|Pfam:PF11861"
FT   DOMAIN          612..827
FT                   /note="Ribosomal RNA methyltransferase SPB1-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF07780"
FT   COILED          716..765
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         56
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         58
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         92
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
FT   BINDING         117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03163"
SQ   SEQUENCE   852 AA;  97582 MW;  27EA94D25377D069 CRC64;
     MGKKGKVGKD RKDKFYKLAK ETGYRSRAAF KLIQLNRRFG FLQQSQVCID LCAAPGGWMQ
     VAKQNMPVSS VVIGIDLFPI KNVPGCISLV GDITSDKTKS DLAKELKTWK ADVVLNDGAP
     NVGRNWLFDA YQQVCLTLSA VKLATQFLRP GGWFVTKVFR SKDYNALIWV LKQLFKKVHA
     TKPSASRNES AEIFVVCQHY RAPDKIDPRF LDAKYVFEEL DVEPQVKVNL LKEVEKAKKP
     KVEGYDGTDV RKIITVTEFL KEEKPLGLLG RVTEIRFDDK AISNHPRTTS EIKECCKDIK
     VLGRKDLRDL LKWHKMMSSE LFPQEEKAEE ETKGKGKRVT KLNEQIEQEE AEGDDEETVE
     LKSMEKEIAE LRKEEEQDAK RKRKKANKER AKLNEKLSLK MVIKGDEGPT EQADAMMFSL
     NAVRSKKQMD DLLDADPDVL MEQDFHDDDD DGLPKKKQKF VKYDKETKGD LYEDEKVLAQ
     KSDDEDSDAD LDREGLGLDD TEELQFENDD EAEEDVDSDN PDAQNPLITD LDYRDKEEKR
     RQKAQLWFEK DTFKNVLAGE DQAVDYDLDR LTEMYRKSGA KIVGDDDKDR PLGKKARQRA
     KHDVAKEDSS SDDSDSEAEV EDQSYEHKTV EKIGGKDGFE VVSTEKREKK VKLNEQELAL
     GQLLVSGKKT KRDLIDAAWN RYMFNDSNLP EWFVKDEEKT MKKQAPVPHE VAETYKKNLE
     EMNVRSIKKV MEAKARKKKH ATKRLEKIKK KAETIMENVD NTNQEKIRLL KKLYKKTDAK
     KKDITYVVAK KSGTSGKKVR RPKGVEGRFK VVDPRMKKDR RAMDAKERRS AKKGGKKGGK
     AKPGKGGKGK KK
//
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