GenomeNet

Database: UniProt
Entry: W5J8Q2_ANODA
LinkDB: W5J8Q2_ANODA
Original site: W5J8Q2_ANODA 
ID   W5J8Q2_ANODA            Unreviewed;       312 AA.
AC   W5J8Q2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=RNA methyltransferase {ECO:0000256|RuleBase:RU367087};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU367087};
GN   ORFNames=AND_007525 {ECO:0000313|EMBL:ETN60837.1};
OS   Anopheles darlingi (Mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43151 {ECO:0000313|EMBL:ETN60837.1};
RN   [1] {ECO:0000313|EMBL:ETN60837.1, ECO:0000313|Proteomes:UP000000673}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20920257; DOI=10.1186/1471-2164-11-529;
RA   Mendes N.D., Freitas A.T., Vasconcelos A.T., Sagot M.F.;
RT   "Combination of measures distinguishes pre-miRNAs from other stem-loops in
RT   the genome of the newly sequenced Anopheles darlingi.";
RL   BMC Genomics 11:529-529(2010).
RN   [2] {ECO:0000313|EMBL:ETN60837.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida L.G., Nicolas M.F., Souza R.C., Vasconcelos A.T.R.;
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ETN60837.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23761445;
RA   Marinotti O., Cerqueira G.C., de Almeida L.G., Ferro M.I., Loreto E.L.,
RA   Zaha A., Teixeira S.M., Wespiser A.R., Almeida E Silva A.,
RA   Schlindwein A.D., Pacheco A.C., Silva A.L., Graveley B.R., Walenz B.P.,
RA   Lima Bde A., Ribeiro C.A., Nunes-Silva C.G., de Carvalho C.R., Soares C.M.,
RA   de Menezes C.B., Matiolli C., Caffrey D., Araujo D.A., de Oliveira D.M.,
RA   Golenbock D., Grisard E.C., Fantinatti-Garboggini F., de Carvalho F.M.,
RA   Barcellos F.G., Prosdocimi F., May G., Azevedo Junior G.M., Guimaraes G.M.,
RA   Goldman G.H., Padilha I.Q., Batista Jda S., Ferro J.A., Ribeiro J.M.,
RA   Fietto J.L., Dabbas K.M., Cerdeira L., Agnez-Lima L.F., Brocchi M.,
RA   de Carvalho M.O., Teixeira Mde M., Diniz Maia Mde M., Goldman M.H.,
RA   Cruz Schneider M.P., Felipe M.S., Hungria M., Nicolas M.F., Pereira M.,
RA   Montes M.A., Cantao M.E., Vincentz M., Rafael M.S., Silverman N.,
RA   Stoco P.H., Souza R.C., Vicentini R., Gazzinelli R.T., Neves Rde O.,
RA   Silva R., Astolfi-Filho S., Maciel T.E., Urmenyi T.P., Tadei W.P.,
RA   Camargo E.P., de Vasconcelos A.T.;
RT   "The genome of Anopheles darlingi, the main neotropical malaria vector.";
RL   Nucleic Acids Res. 41:7387-7400(2013).
RN   [4] {ECO:0000313|EnsemblMetazoa:ADAC007525-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000256|ARBA:ARBA00008361, ECO:0000256|RuleBase:RU367087}.
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DR   EMBL; ADMH02001856; ETN60837.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5J8Q2; -.
DR   STRING; 43151.W5J8Q2; -.
DR   EnsemblMetazoa; ADAC007525-RA; ADAC007525-PA; ADAC007525.
DR   VEuPathDB; VectorBase:ADAC007525; -.
DR   VEuPathDB; VectorBase:ADAR2_011103; -.
DR   eggNOG; KOG2899; Eukaryota.
DR   HOGENOM; CLU_004729_0_0_1; -.
DR   OMA; ELFRGKQ; -.
DR   OrthoDB; 1130801at2759; -.
DR   Proteomes; UP000000673; Unassembled WGS sequence.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:GOC.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR039772; Bin3-like.
DR   InterPro; IPR010675; Bin3_C.
DR   InterPro; IPR024160; BIN3_SAM-bd_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12315:SF0; 7SK SNRNA METHYLPHOSPHATE CAPPING ENZYME; 1.
DR   PANTHER; PTHR12315; BICOID-INTERACTING PROTEIN RELATED; 1.
DR   Pfam; PF06859; Bin3; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51515; BIN3_SAM; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU367087};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000673};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU00848};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367087}.
FT   DOMAIN          96..312
FT                   /note="Bin3-type SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS51515"
FT   REGION          18..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   312 AA;  35523 MW;  5F2043EB4C1FA022 CRC64;
     MGLPVAAQKF VPEVTTITGR VEEDVQKAST ECKPALGKRK PEPESEPKRE SQAEQERERE
     PQQQTQAAKR PRKIFPYGNY DRYYGYRNFN ATPADDPRLE AFMQRRELFL GKRVLDIGCN
     NGALTIQLAA ACQPSAIFGI DIDGGLIAQA RRHCKQALIN GVKVPRVEER RHVLNRGQVE
     FLRANYILED AALLEAEQPK FDVVLCLSVT KWIQLNFGDD GLRLAFRRMF RQLKPGGVLI
     LEAQPWSSYK RRKKLTETIA ANFARIKLLP AMFQQYLLGN EVGFASCTEL PLPRTSTKGF
     QRPIQLYRKS ND
//
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