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Database: UniProt
Entry: A0A5J4NIC1_9TREM
LinkDB: A0A5J4NIC1_9TREM
Original site: A0A5J4NIC1_9TREM 
ID   A0A5J4NIC1_9TREM        Unreviewed;       768 AA.
AC   A0A5J4NIC1;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=tRNA (cytosine(34)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00012629};
DE            EC=2.1.1.203 {ECO:0000256|ARBA:ARBA00012629};
GN   ORFNames=DEA37_0007489 {ECO:0000313|EMBL:KAA3675315.1};
OS   Paragonimus westermani.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Troglotremata; Troglotrematidae; Paragonimus.
OX   NCBI_TaxID=34504 {ECO:0000313|EMBL:KAA3675315.1, ECO:0000313|Proteomes:UP000324629};
RN   [1] {ECO:0000313|EMBL:KAA3675315.1, ECO:0000313|Proteomes:UP000324629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IND2009 {ECO:0000313|EMBL:KAA3675315.1,
RC   ECO:0000313|Proteomes:UP000324629};
RX   PubMed=30520948;
RA   Oey H., Zakrzewski M., Narain K., Devi K.R., Agatsuma T., Nawaratna S.,
RA   Gobert G.N., Jones M.K., Ragan M.A., McManus D.P., Krause L.;
RT   "Whole-genome sequence of the oriental lung fluke Paragonimus westermani.";
RL   Gigascience 8:0-5232231(2019).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
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:KAA3675315.1}.
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DR   EMBL; QNGE01002590; KAA3675315.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5J4NIC1; -.
DR   Proteomes; UP000324629; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR023270; RCMT_NCL1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   PRINTS; PR02011; RCMTNCL1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000324629};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          42..442
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          733..768
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        325
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         167..173
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         206
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         233
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         266
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   768 AA;  88020 MW;  34130814F684BCAE CRC64;
     MVRKRRPRVG HHQFTPETRQ NFQFEQYYKG QGLIVDSEWP AFMHALQQEL PVTFRVTGFR
     EQNRELLRLI KHRYRNEIIK LQFPATDSGE VQQQHISFDS LSWYPNELAW QLDASRFVVR
     KTPELKVLHH FLVSETESGN ISRQEAVSML PPLLLDIRSY HSVLDLCAAP GSKSAQLVEL
     LHADAETKRT ADWSYTEPTG LVVANDVDQK RCYMMVHQVK RLQSPCTVIT QEDATCFPRL
     YVPDPSTLKT DKVEMTQFLF DRVLADVPCS GDGTLRKNPD LWLRWSPNLG IAEHYLQLRI
     LRRGLELLRD TTSDGDHGRL VYSTCSFNPL ENEAVIASML HACQGAVRLV GPDRLACVTR
     RGPDASRGRF QTRPGLTSWR VMNKKGCWFD KFEDVPQSQQ CNLRPSLFPP PNITELGLDR
     CFRVFPQDQN TGGFFLAVLE KVAPLPWMKP TGPRSYTFVG PIVSGICDQE EAEDASDLIE
     TDFPPEPNKQ TCENECSSAI ESKKPRVFNE NPFTYIDPSD DKDWANIRDY YGIMETSDHD
     AVDPKNGVIR NFCPANLLYR STGDELRRRQ FYYTNKLAKQ IIQSNLCRGI KIVNCGVRMF
     CIMEDKQFTG YRLLQDGVDL ADAFLPETGG RRIHLTWMQY SDLKLLLEEE MPLISRMTMT
     TQSQWNRLTP GPVLIDYSPS NTEVETEQNL PQCRLVFAGW RGIQSLRHYI GRHERLHLMR
     LANLDPKPAI MGHTVLDQKR PRDGASPIST EPDAYESDRD PDVISSAS
//
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