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Database: UniProt
Entry: A0A1I7Z0V1_9BILA
LinkDB: A0A1I7Z0V1_9BILA
Original site: A0A1I7Z0V1_9BILA 
ID   A0A1I7Z0V1_9BILA        Unreviewed;       507 AA.
AC   A0A1I7Z0V1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=NOL1/NOP2/Sun domain family member 4 {ECO:0000256|ARBA:ARBA00042050};
OS   Steinernema glaseri.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g21698.t2};
RN   [1] {ECO:0000313|WBParaSite:L893_g21698.t2}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in rRNA + S-adenosyl-L-methionine = a 5-
CC         methylcytidine in rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:61484, Rhea:RHEA-COMP:15836, Rhea:RHEA-COMP:15837,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC         Evidence={ECO:0000256|ARBA:ARBA00036484};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a cytidine in tRNA + S-adenosyl-L-methionine = a 5-
CC         methylcytidine in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:61468, Rhea:RHEA-COMP:13670, Rhea:RHEA-COMP:15827,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74483, ChEBI:CHEBI:82748;
CC         Evidence={ECO:0000256|ARBA:ARBA00036266};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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   WBParaSite; L893_g21698.t2; L893_g21698.t2; L893_g21698.
DR   Proteomes; UP000095287; Unplaced.
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; 6.20.240.40; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR46955:SF6; 5-METHYLCYTOSINE RRNA METHYLTRANSFERASE NSUN-4; 1.
DR   PANTHER; PTHR46955; PROTEIN CBG01349-RELATED; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 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}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
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          155..506
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        431
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         266..272
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         324
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         357
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         376
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   507 AA;  56126 MW;  3DEA2C7D0DA1CA6A CRC64;
     MLALDHFDFY YAPLFGKRWP SMRLGLVSQN KFVAVANRFS HSFDTNQQIL KDIGAEDLIA
     KLTSGKHASE RIAEKKKATE SKPVAADSYG TVEHEVYEHN EELLDDRSDA SIGEFTAPTQ
     SITPGELQLG KNEDAHLKRL DIKVTGLEGQ FANLPSKEDF IFYPRELKVF TFPRGSTSDF
     PXXXXRAFEA VTGLEGQFAN LPSKEDFIFY PRELKVFTFP RGSTSDFPFP SKDAEGVPGW
     WLLDGGSLVP VLALDLAKGD IVLDMCAAPG GKSLLMLQTG LVGKPSRLPF AELILRYXXX
     XAAPGGKSLL MLQTGLVDKL VCNDFKLSRL GQLQKALSMY VPGTSEAADR VILKRRDATS
     VEAWDEDAKY DKVLVDAPCT TDRLAAQQDE GNLFSATMTN ERLNLPQIQT KILLNALRSV
     KVGGYVVYST CALSPVQNES VVENAVAIAA DKMGIEVIER DLVQLRRHLT SAGYYKFSDQ
     CRRGSLVIPF LPSNFGPMYV CKLQRLK
//
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