ID A0A0V1H2V8_9BILA Unreviewed; 552 AA.
AC A0A0V1H2V8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=RNA methyltransferase {ECO:0000256|RuleBase:RU367087};
DE EC=2.1.1.- {ECO:0000256|RuleBase:RU367087};
GN Name=Mepce {ECO:0000313|EMBL:KRZ04643.1};
GN ORFNames=T11_6992 {ECO:0000313|EMBL:KRZ04643.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ04643.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ04643.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ04643.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000256|ARBA:ARBA00008361, ECO:0000256|RuleBase:RU367087}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ04643.1}.
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DR EMBL; JYDP01000159; KRZ04643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1H2V8; -.
DR STRING; 268475.A0A0V1H2V8; -.
DR Proteomes; UP000055024; 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; 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; PF06325; PrmA; 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:UP000055024};
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 265..498
FT /note="Bin3-type SAM"
FT /evidence="ECO:0000259|PROSITE:PS51515"
FT REGION 30..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 552 AA; 61966 MW; 4CA1E4F983D0AD54 CRC64;
MNKAEQSLAS KTAMKCSDQI PRCRSRTLSH NNPECEGTKS VRQPLPPGHN HVQRFRKRHG
SAGGCMRAKR ERIELPTKFL LGGNINDPLN LGGLASAGES NSLEPSPAAS PNKINDAIDI
IIPKNPKDPL NLDNDSEIFA SHKRYRKRKR HSSFKLDESS SLSRDESSHR SYDAESSSAC
KSLNSSSSKT NCDPVVSPVV DVPCSSSAIT ETPTGQLKNK MPSLKPAAAA AVKKEMSKEK
SRFRYGNYTS YYNKRLLSFD ANIADPRLNL LEKEWFFNKS VLDIGCNSGQ LTLAIAKKFS
PNVIIGIDID SALIGHARKN QRLAMDKHLL GKMNLKFPSS FSRSYGPLSA PPEAKYTKKF
PENVFFRQLN YVLSSDAFLE YEKAEYDTVI AFSITKWIHL NWGDEGIKRF FKRVYLNLKP
GGRLLLEPQA FSSYAKRRGL CQEIYDNYKS ITLMPDEFPK YLTSAEVGFA SYRTVGISRY
KSKGGFQRPI LLFEKNGEPH TFVDQKFTDL LKLICIELAR CMKCKKTGDA QFCGGQVGFH
WQTMMLLRTG LT
//
