ID   A0A0L7QU51_9HYME        Unreviewed;       817 AA.
AC   A0A0L7QU51;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=RNA methyltransferase {ECO:0000256|RuleBase:RU367087};
DE            EC=2.1.1.- {ECO:0000256|RuleBase:RU367087};
GN   ORFNames=WH47_03931 {ECO:0000313|EMBL:KOC62173.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC62173.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC62173.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC62173.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000256|ARBA:ARBA00008361, ECO:0000256|RuleBase:RU367087}.
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DR   EMBL; KQ414735; KOC62173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L7QU51; -.
DR   STRING; 597456.A0A0L7QU51; -.
DR   Proteomes; UP000053825; 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:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR041698; Methyltransf_25.
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   Pfam; PF13649; Methyltransf_25; 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:UP000053825};
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          316..565
FT                   /note="Bin3-type SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS51515"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..42
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        686..725
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..809
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   817 AA;  93469 MW;  8A8BFF46FF2E2A0B CRC64;
     MSSAQVDRST KVGNITKKEN EKSRKTFNSS HKKHKHEDSR HFKFGRKRLQ SFTSNGKFFP
     PYKRRKKEGV IIPPTKFLLG GNICDPLNLN SMQDEEINRA MNAVTPKSSP LPTPKHKKEV
     IEVIIPPNIC DPLNLSNCND NDNDEYEKQL ISPTKKGSKR RNRKKKRASS GSGNDASDLI
     EIKTKDCDTT DIAEPIEQSA PENVETEQQP APSNSPADNQ PKESKPESPQ KDKNKLRLKG
     LEEPKDKRLR KVDVKDKIVS PVIPQPGAWK PRPQHRPSQD KKKNQKMPNF REKDSRYQYG
     NYNRYYGYRN SLHEMDTRLT VFAQRKHLFF GKDVLDIGCN IGHITLSVAR DFSARSVTGI
     DIDRTLINIA RKNIKHYVNC VQSPAGNEDS HHQDVNFFPM SMPINYGPVD IPGFTKNKNH
     KGFPYNVTFV QGNYVLEDDS LLCTEQPQFD TILCLSITKW IHLNFGDAGL KQAFKRMYAQ
     LRPGGVLVLE PQGWSSYTKK KNLTVNTLFN SLSKIYLKFE FRPHSFTQYL LSPEVGFSKC
     EVLSIPPHPS KGFQRPIHLF TKAGPIQESP DNSIVNALKR QERIDEEKRK MEQKEYEQKL
     FKKGETKEGN LSEISQQSNE SMSQYDQLEN VYAPSATPCY DTPGHNSDNQ PPDASKMCYI
     DVSMENDKVE AESQGESNST ENQTSRKRNM EVDDRTIVTK RPKPEIEAFK SITNEGKRKT
     EAKEQQTSQE SVNESGNKTE VELRKNNESN TQSVTEKNHA SCRSKQKNDT DEKVSSFTEN
     KEDSRSEEWK EKGKGSRSRC EEKQTERQRC QLTSDNT
//