ID A0A183N987_9TREM Unreviewed; 627 AA.
AC A0A183N987;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
DE EC=2.1.1.33 {ECO:0000256|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03055};
GN ORFNames=SMRZ_LOCUS24862 {ECO:0000313|EMBL:VDP53030.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0002486301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0002486301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP53030.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDP53030.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03055};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03055}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000256|HAMAP-Rule:MF_03055}.
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DR EMBL; UZAI01020752; VDP53030.1; -; Genomic_DNA.
DR STRING; 48269.A0A183N987; -.
DR WBParaSite; SMRZ_0002486301-mRNA-1; SMRZ_0002486301-mRNA-1; SMRZ_0002486301.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000277204; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd15844; SNARE_syntaxin5; 1.
DR Gene3D; 1.20.58.70; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_03055; tRNA_methyltr_TrmB_euk; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
DR InterPro; IPR025763; Trm8_euk.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR PANTHER; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23417:SF16; TRNA (GUANINE-N(7)-)-METHYLTRANSFERASE; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR SUPFAM; SSF47661; t-snare proteins; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03055};
KW Reference proteome {ECO:0000313|Proteomes:UP000277204};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03055};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_03055}.
FT DOMAIN 238..300
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 135..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 487
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 408
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 431..432
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 464..465
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 484
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
FT BINDING 603..605
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03055"
SQ SEQUENCE 627 AA; 71527 MW; 80CD3B5CDE3EF8BA CRC64;
MSEELKMTVS KMTKLRILFQ EPSHSSPETL SKLIEVIQYD IMDLNKTKLQ LKASVSEVKE
HSTAGVQHLK HIDLIVIGLE YHLSFLVSEF RVVLEEHKTS LSVDSRKSDA NIQMNDDLNS
LTEYASHSRI MKTNELSPIN PTSDNSIPNT HPVNDQLQGN KKQQCSSNPS NPTMSLLTPV
PYSHSTSSLP SVMPISKLND TPIVNRSEVY NSFQAETTSR TPEQLQIFAS NPHVSLIDQE
VRQRDAAIRR VESTIVQLGE IYQQFSTLVQ EQNDLVLRID SQTDNVEMNI SEAHAQLLVF
MRRISAQRGL LIKAFITLIL CFVMSECAMV LDSVDSCEKC PTDKNIRLPS KRHYRQRAHC
NPWSDHTLDY PLKPELMDWE KLFGGDSAFS LSVNNNSFDP IVRFLDVGCG YGGLLFNLST
FYPFTRSIGL EIRLKVCDFV QEKIKALRAK HSGQYNNIAC IRTNAMKFLP NFFHKEQLHK
IFFLYPDPHF KRVKHKWRII SPTLLDIYAY LLTPGGKIYS TTDVPDLGKW IVDCLCAHPL
FRPVCHVHLS PAVEKIQGAN ELLKISNYPD IFEENSHFVK DSESFQILKE SDPVLKLLEQ
GCTEEAHKAC REGRETFLVV YERISNP
//
