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Database: UniProt
Entry: H2KQ68_CLOSI
LinkDB: H2KQ68_CLOSI
Original site: H2KQ68_CLOSI 
ID   H2KQ68_CLOSI            Unreviewed;       547 AA.
AC   H2KQ68;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Putative methyltransferase NSUN5 {ECO:0000313|EMBL:GAA29579.2};
GN   ORFNames=CLF_103354 {ECO:0000313|EMBL:GAA29579.2};
OS   Clonorchis sinensis (Chinese liver fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Clonorchis.
OX   NCBI_TaxID=79923 {ECO:0000313|EMBL:GAA29579.2, ECO:0000313|Proteomes:UP000008909};
RN   [1] {ECO:0000313|EMBL:GAA29579.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Henan {ECO:0000313|EMBL:GAA29579.2};
RX   PubMed=22023798; DOI=10.1186/gb-2011-12-10-r107;
RA   Wang X., Chen W., Huang Y., Sun J., Men J., Liu H., Luo F., Guo L., Lv X.,
RA   Deng C., Zhou C., Fan Y., Li X., Huang L., Hu Y., Liang C., Hu X., Xu J.,
RA   Yu X.;
RT   "The draft genome of the carcinogenic human liver fluke Clonorchis
RT   sinensis.";
RL   Genome Biol. 12:R107-R107(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Henan;
RA   Wang X., Huang Y., Chen W., Liu H., Guo L., Chen Y., Luo F., Zhou W.,
RA   Sun J., Mao Q., Liang P., Zhou C., Tian Y., Men J., Lv X., Huang L.,
RA   Zhou J., Hu Y., Li R., Zhang F., Lei H., Li X., Hu X., Liang C., Xu J.,
RA   Wu Z., Yu X.;
RT   "The genome and transcriptome sequence of Clonorchis sinensis provide
RT   insights into the carcinogenic liver fluke.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; DF142974; GAA29579.2; -; Genomic_DNA.
DR   AlphaFoldDB; H2KQ68; -.
DR   Proteomes; UP000008909; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR049561; NSUN5_7_fdxn-like.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF4; 28S RRNA (CYTOSINE-C(5))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 2.
DR   Pfam; PF21148; NSUN5_fdxn-like; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000008909};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          164..517
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          518..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..538
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        444
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         275..281
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         299
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         355
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         375
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   547 AA;  61815 MW;  B9C6E32E55F22DB7 CRC64;
     MSMSESNNPN ALLYSEASFL VCNVLGKKCR LKSALYENDF TTDLRKLYAL ACKTLDSFSL
     LHETVKQSKL VHRHPVEHIP TKSIEGRGSS SEPRLTGCHH CLLYVTLHDL LLGSSRSNYK
     IWAKELYLVT QDTGAISRFR RAYKVVKKAR KKENEHTACI RPGNQNDTRL LLPCYARVNR
     LRADLESVLK ELQSEQYTEL QTTGKRTRKM LRKLEDNQFY VDYHLSDNLL IFTHGSLLYK
     LPAVTSRKLI IQDKASCIVP EVVRPNPNAD VLDACAAPGN KTLQLIEMMS PQATVFAIDR
     DPTRFRTLCN NLHSSGVQRL SISGSIIVDN LPDPENATTT KRPCSQPRVE AICQDFLSLD
     PMDSKFSRVE SILLDPSCSG SGLVARQPEG TGSVLSSGYS NMGEDDMKGE DISRRLERLS
     NLQAQLLRHA LSFQNVRRVV YSTCSVRSEE NEAVVLENLE RFRGQFKLET IWPAGNSDAR
     RRWLHRGLSE MGCEACLRAS PESDLTNGFF IASFVRVSES HTESESKRPD DEKPISGEKK
     KRKKRKK
//
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