ID K0RT01_THAOC Unreviewed; 1051 AA.
AC K0RT01;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN ORFNames=THAOC_24770 {ECO:0000313|EMBL:EJK55499.1};
OS Thalassiosira oceanica (Marine diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK55499.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK55499.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK55499.1,
RC ECO:0000313|Proteomes:UP000266841};
RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA Rosenstiel P., Hippler M., Laroche J.;
RT "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT limitation.";
RL Genome Biol. 13:R66-R66(2012).
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:EJK55499.1}.
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DR EMBL; AGNL01033900; EJK55499.1; -; Genomic_DNA.
DR AlphaFoldDB; K0RT01; -.
DR EnsemblProtists; EJK55499; EJK55499; THAOC_24770.
DR eggNOG; KOG2198; Eukaryota.
DR OMA; SGDIMQK; -.
DR Proteomes; UP000266841; 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; 2.
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:UP000266841};
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 313..741
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 98..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..161
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 551
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 406..412
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 444
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 471
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 498
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 1051 AA; 115961 MW; 47E734256F3FC288 CRC64;
MQYGLRCCAR KTTRPTVANR VLDLNDCARK RRSIVCSLAL TPATGKRASS VSESEELPSS
ADARWCRPML FLASQPKTLA RWDFGLRRLR TRFARAPRTR PFGDVGDGDG NRSPDLCTPI
RNSPAPSLIA SLLDPRSPKR TRNGTMGKKW SRKRKAQERA AKSGKARRDS SGDGGNSKPG
TWAAAPTSNA KLESYYSLVG LHDTRYDADR KEFVPCETDG EKTAERDRFM SSLRTILPTS
FRVDRSLDPT IQESVLRELN DFAGKEMEVE IELPRHSAAI GGRKQLVDDV RVDEPGGGEQ
DNGPDEAKQA SSADAANGEY KPVVVKRKIA PAVQIPFIRD ARSGVVLGYQ ISVDKRTLRR
NQSLAPFHAW MKVQTDCGHI TRQEQVSMIP PVVLDAKPGM AVLDMCAAPG SKTCQILEVV
GELRGDGDGG EGRSEPAGYV VANDADPKRA YMLVNQLRRM NNPAAFVTSC DGQYFPVLDS
KSDRGTEREG SFDRVLADVP CSGDGTVRKN PGIWRQWNHL GSLALHPLQL SIALRGARLT
KVGGYLVYST CSMNPAENES VVAELLRLGE GSLVLADPRS RMDGLVARPG WKTWRVLRES
KSRTRKAIKD QKKKRNAKMM AKKKEWDEKV ERGEAPPPKE RSDGDPDDKC DAVEPSPYDT
DPYVAPSDWS YESLSERTKS LGFVEYASFE DVEDDWRKRV RRSLFPPTEE EAGRFELHKC
LRCLPQDMDT GGFFVALLKK VGPLGKNATE RMDSMAREMR GLGEGEGPAA VGAETSCSGK
GDGKAKEEDP TPPPAEKSAA EEGGKEKDDD AKPKEVIERA PIGKAGQAQN KLGDYSQEDF
VAADPDIWPA VVEEYGLSPS FPRDQFMCRS TPAAKVIYFV TDRIKSDLMD RGVQDRVTVI
NSGVKSFERC KMGPREENDP RPAKGSYRVA QEGVHFVVPH MTKRVVSADA DDFAKCLREG
FLRLDAFGDE FAGKLGGLEQ GSFVVALRGH ENDLVRKMFL VMWRRRDVVN CFVSKIEKEA
IRSKLRALGY VESSEGKEGG KGEEAPDAGA G
//
