ID A0A182JTZ1_9DIPT Unreviewed; 1039 AA.
AC A0A182JTZ1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=Ribosomal RNA adenine methylase transferase N-terminal domain-containing protein {ECO:0000259|SMART:SM00650};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR001973-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA 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 christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR001973-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR001973-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; A0A182JTZ1; -.
DR STRING; 43041.A0A182JTZ1; -.
DR EnsemblMetazoa; ACHR001973-RA; ACHR001973-PA; ACHR001973.
DR VEuPathDB; VectorBase:ACHR001973; -.
DR OrthoDB; 3088211at2759; -.
DR Proteomes; UP000075881; 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 HAMAP; MF_00607; 16SrRNA_methyltr_A; 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; 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 770..939
FT /note="Ribosomal RNA adenine methylase transferase N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00650"
FT REGION 284..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 763
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 765
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 790
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 811
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 839
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
FT BINDING 854
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01026"
SQ SEQUENCE 1039 AA; 116071 MW; FCD1217F4A81E9AE CRC64;
MSKETMIIFV YDLTKKVEND DPTGSIIYFH PMWVSELQKK SLCGQLMCAS NVYLESNQIL
QSFLQNKGVL GGSIFYHNKV LASQLPTNLT KMFVYSDPYR MKLAEMITVT FHVPNGVSLI
SAYITKRDYT QLIDATKNIP IYFNNCATAA PPTGPVPFAI KKKLIPSKEL GGTVSGFPML
KSDKSIIFSN IPEEETVGAD GGLCEQTQSK KSFNTVSRPT FLPLKFKNLT SRDIIDSGVN
SINFDESDSF PNFIGKTSVC STPLTENKIV PNRNMMSICV TQDQPPAPAA KANDNSDVEE
EKPQPSVEAN GSIFKYFNAR KYSILNNPFM MPKNVRCSSM SNLTKIETGL DESGESSPAE
SNDVERNISN KHQFKFSNKY DPAKTISDPL YPIVDQRNRA MSYSLFRDFE QSRNERIAEL
VEQEAKQEAK GNEKCNKDVL QNSLTIDDLA PMVSAVASSA RKIELPLSEQ PESIKPATTP
KDRRALSLPI KSFNLNDDPP SSARGVGSGG TSNGQELFMR RKSTLELTPL MTKLTVLALN
DTESSGVSSW DTTPGCSYNM AISPQDYIPQ RRKSQDISQS VAPSNGVPAF DENALVKVDL
FVCVQQNMTL ILVMQEKNCK NQRLVQTLFE SCVSKFLRIE NDIQLAMNIN VDGFDKTDGY
SLIALDSDWD VAKKNGPWNA LEMQTAESLH THFKKSNIVT EVTLKSQETV LYGYQCGMRE
LFYTQIANAQ GGLPPPQDVM GAVPLCAKRR IERIVFNKDF GQHILKNPLV ITSMLEKAAL
RPTDVVLEIG PGTGNMTVKI LEKVKKVVAC EIDTRLVAEL QKRVQGTHLQ PKLQILIGDV
LKTDLPFFDI CVANMPYQIS SPFVFKLLLH RPFFRCAVLM FQREFAQRLV AKPGDKLYCR
LSINTQLLAR VDMLMKVGKN NFKPPPKVES SVVRIEPRNP PPPINYTEWD GLTRIAFLRK
NKTLAAAFKQ TTVLAALEDN YKLHCSLKNI DVPANLNVKE MVESILEKVD AGNKRARSMD
IDDFMAVLQA FNVEGFHFS
//
