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Database: UniProt
Entry: A0A1R2C041_9CILI
LinkDB: A0A1R2C041_9CILI
Original site: A0A1R2C041_9CILI 
ID   A0A1R2C041_9CILI        Unreviewed;       601 AA.
AC   A0A1R2C041;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   ORFNames=SteCoe_16914 {ECO:0000313|EMBL:OMJ82378.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ82378.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ82378.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ82378.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA   Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA   Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA   Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
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:OMJ82378.1}.
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DR   EMBL; MPUH01000342; OMJ82378.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2C041; -.
DR   OrthoDB; 1268at2759; -.
DR   Proteomes; UP000187209; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR011023; Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR023273; RCMT_NOP2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00446; nop2p; 1.
DR   PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   PRINTS; PR02012; RCMTNOP2.
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}; Reference proteome {ECO:0000313|Proteomes:UP000187209};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
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          81..368
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          374..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..505
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..562
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        298
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         173..179
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         197
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         224
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         241
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   601 AA;  68003 MW;  365DDC1FDBB7C5E3 CRC64;
     MEEDISIHVD DSHAQADLGL MHMKLQEVVQ ILTNYKSQPQ EKSRAAYLDE LTDLVSKYYE
     YNQELAEYLV SLFPPSELVN FLEASQAPRP MIIRTNTLRT KRRELAQSLI QKGVNLDPAG
     DWNKVGLKII DSQVPIGATT EYLAGQYMLQ SASSFLPVMA LAPKPGEKIL DLCAAPGGKT
     THIGQIMKNQ GIIVANEFNP DRCASIKGNI HRMGLSNVVI TNYDGRKIGK HIAGFDRALV
     DAPCSGLGVI WKDPSVKAMR TLKDIKRNAH IQKELLLSAI DVVSANSSTG GYIVYSTCSI
     SVEENEEVVN YALKNRKVKV VDTGLSIGEP GLHKFRGKIY HPSLVNCKRI YPHVYNMEGF
     FIAKLKKIEN FVPDEASKPH TGEKREKAWK VKRREHEEEE EMEKEWKKNL KEKRGSKEVK
     MKKGQEKGDE EKEKEEKGKE KKGDFKKNEG NEDKKKLGGI KVDEKNKKGN KEEEQKRGRT
     KSLETGKERK KENDTPVKEK VMKKSLSQEP ALTKESKNAK KDMKSKPEIK GKKKSEEDFV
     EKPQKTTKKV KKVEKDDENV ITDLKQALST SKQGKKFVTP ELPEKRAKKS SKTPEKKMKK
     S
//
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