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Database: UniProt
Entry: A0A0B2V8B6_TOXCA
LinkDB: A0A0B2V8B6_TOXCA
Original site: A0A0B2V8B6_TOXCA 
ID   A0A0B2V8B6_TOXCA        Unreviewed;      1004 AA.
AC   A0A0B2V8B6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=NOL1/NOP2/Sun domain family member 4 {ECO:0000256|ARBA:ARBA00042050};
GN   Name=nsun4 {ECO:0000313|EMBL:KHN77768.1};
GN   ORFNames=Tcan_14499 {ECO:0000313|EMBL:KHN77768.1};
OS   Toxocara canis (Canine roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX   NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN77768.1, ECO:0000313|Proteomes:UP000031036};
RN   [1] {ECO:0000313|EMBL:KHN77768.1, ECO:0000313|Proteomes:UP000031036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN77768.1};
RA   Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA   von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA   Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA   Gasser R.B.;
RT   "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KHN77768.1}.
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DR   EMBL; JPKZ01002233; KHN77768.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2V8B6; -.
DR   STRING; 6265.A0A0B2V8B6; -.
DR   Proteomes; UP000031036; 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   CDD; cd00200; WD40; 1.
DR   Gene3D; 6.20.240.40; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
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   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SMART; SM00320; WD40; 8.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031036};
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}; WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT   REPEAT          131..172
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          173..214
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          215..256
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   DOMAIN          695..1003
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        928
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         798..804
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         821
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         854
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         873
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   1004 AA;  110119 MW;  94B42C5470BD978F CRC64;
     MRAFGRDRWL NYKATESSFL SFGGIEKEAH AERMSGEGSL ADDKYLTENA VVVQHDWFSC
     VRSDQTDSSF FVGIREYGSP SSFIDVRHKG GKLFPATPDK VHVEKLDARR LAVQFKNMAP
     TTFVAPRIEF TTVHSTSVQS VDVSPSGRLV VSSDSNGQLV VWHADTAEII RNFVGHALDV
     NRCRFFPSGL VVLSAGMDMS VRIWSVETGQ CPRVLKGHRQ GVVDLGIIDR GKEILSCSKD
     GTAKMWNCGS AECLRTWCPE AGLGATISID KEEGTSVAFG TSEGANLYIG TAGGSVISYD
     MKAGKTFAKL KTSRGAVTKL CVRESLGLFS SFCVVDLGII DRGKEILSCS KDGTAKMWNC
     GSAECLRTWC PEAGLVNAIA VTPSSSGVFS VACEMGKAEV YDIRSSEPGA TISIDKEEGT
     SVAFGTSEGA NLYIGTAGGS VISYDMKAGK TFAKLKTSRG AVTKLCVRES LGLFSSFYDG
     TVSCYDLPLN SKMAKLEFSG ADCDPVYDMS TAAEGQLYTA CRDRIMLRRI CSSCSSTVSS
     TSSTCSKLCS PPNLCKERVR HKRLKFKPKV ARTRPMKTPS ALAIEHFDFY YGPMYGKRWP
     SIRLGLLTPN KYVAVVNTFS KAWETNEYIL QDMGAVDVIK TLTGTTATER IEKKRKLIEA
     KGIRTPDAER DEHEQANSDE MEDLAMRGEA GLNEFRRSGQ MLTRGELQMG QKPDSRDQHD
     ITITGLEGQY VQLPKKEDFI VYPRKLKLYS MPRGSLVDFP SPIKDEQGIP SWWLLDGGSI
     IPVLALDLSE GETLLDMCAA PGGKSLLAIQ TGLPEKMVCN DYKLSRLGQL RRALSMFIPL
     DSDAADRVIL KRKDASDLQR WDELAVYDKV LVDAPCSTDR LAANQDEGNM FAVSMTTERL
     NLPELQAKLL INALRSVRVG GSVVYSTCTL SPIQNETVVE NAVAVATERF GLKVIEQTLE
     QLERHLSSSG LFRFGESCRR GSLVVPFLPS NFGPMYVCKL RRTL
//
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