GenomeNet

Database: UniProt
Entry: A0A182UV50_ANOME
LinkDB: A0A182UV50_ANOME
Original site: A0A182UV50_ANOME 
ID   A0A182UV50_ANOME        Unreviewed;      1154 AA.
AC   A0A182UV50;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Ribosomal RNA adenine methylase transferase N-terminal domain-containing protein {ECO:0000259|SMART:SM00650};
OS   Anopheles merus (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM004186-PA, ECO:0000313|Proteomes:UP000075903};
RN   [1] {ECO:0000313|Proteomes:UP000075903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles merus MAF (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEM004186-PA}
RP   IDENTIFICATION.
RC   STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM004186-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A182UV50; -.
DR   EnsemblMetazoa; AMEM004186-RA; AMEM004186-PA; AMEM004186.
DR   VEuPathDB; VectorBase:AMEM004186; -.
DR   VEuPathDB; VectorBase:AMEM21_009848; -.
DR   Proteomes; UP000075903; Unassembled WGS sequence.
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:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.8.480; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR043987; CCZ1/INTU/HSP4_longin_1.
DR   InterPro; IPR043989; CCZ1/INTU/HSP4_longin_3.
DR   InterPro; IPR026091; HPS4.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR011530; rRNA_adenine_dimethylase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00755; ksgA; 1.
DR   PANTHER; PTHR14407:SF9; HERMANSKY-PUDLAK SYNDROME 4 PROTEIN; 1.
DR   PANTHER; PTHR14407; HERMANSKY-PUDLAK SYNDROME 4 PROTEIN LIGHT-EAR PROTEIN-RELATED; 1.
DR   Pfam; PF19031; Intu_longin_1; 1.
DR   Pfam; PF19033; Intu_longin_3; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01026};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}; rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01026};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01026}.
FT   DOMAIN          885..1054
FT                   /note="Ribosomal RNA adenine methylase transferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00650"
FT   REGION          457..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         878
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         880
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         905
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         926
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         954
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT   BINDING         969
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ   SEQUENCE   1154 AA;  129163 MW;  0803DE7DB3685147 CRC64;
     LAEMSKETMI IFVYDLTKKV ENDDPTGSII YFHPMWVSEL QKKSLCGQLM GSTYFLGETL
     STVRFLSLQN GKFALRSHGR FMLAVGSDRN IAESILEYRA SLLSSLIELY HGDFNTLYNV
     YVEKEQKNGF NEKVFCLMES TLPLLQFNGN ILQNMPLLRL PKCASNVYLE SNQILQSFLQ
     NKGVLGGSIF YHNKVLASQL PTNLTKMFVY SDPYRMKLAE MIAVTFHVPN GVSLISAYIT
     KRDYTQLIDA TKNIPIYFNN CATAAPPTGS VPFAIKKKLI PSKELGGTVS GFPMLKSDKS
     IIFSNIPEEE TVGADGGLCE QTQSKKSFST VSRPTFLPLK FKNLTSRDII DSGVNSINFD
     ESDSFPNFIG KTSVCSTPLT ENKIVPNRNM MSICVTQDQP SAPPAEENDN IGVEEEKPPI
     AVEANGRSSL KYFNARKYSI LNNPFMMPKH IRCSSMSNLT EQQSNETEEN SPAEDTGGVD
     RHIKNKRQFK FSNNYDPAKT ISDPLYPLVD QRKRAMSYSL FQDFERSRNE RIAELVEQEA
     KQEPKGNDKC NQVTQQQPSA IDDRIPTVGA ISTTARKVEL PLSENPELVK GAATPKDRRA
     LSLPIKSFNL NDDAPSTARA GGNGGTSSGQ ELFTRRKSTL ELTPLMTKLT VLALNDTESS
     GVSSWDTTPG CSYNMAISPQ DYIPQRRKSQ DISQSVAPPL GVLAGDENAL VKVDLFVCVQ
     QNMTLILVMQ EKNCKNQRLV QTLFESCVSK FLRIENDIQL AMNINVDGFD KTDGYSLIAL
     DSDWDVAKKN GPWNALEMQT AESLHTHFKK SNIVTEVTLK SQETVLYGYQ CGMRELFYTQ
     AANAQGGLPP PQDVMGSVPL CAKRRIERIV FNKDFGQHIL KNPLVITSML EKAALRPTDV
     VLEIGPGTGN MTVKILEKVK KVVACEIDTR LVAELQKRVQ GTHMQPKLQI LIGDVLKTDL
     PFFDICVANM PYQISSPFVF KLLLHRPFFR CAVLMFQREF AQRLVAKPGD KLYCRLSINT
     QLLARVDMLM KVGKNNFKPP PKVESSVVRI EPRNPPPPIN YTEWDGLTRI AFLRKNKTLA
     AAFKQTTVLT TLEENFKLHC SLKNIDVPAD LNVKEMVEKI LEKADASDKR ARSMDIDDFM
     AVLQAFNAEG FHFS
//
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