ID A0A5A8C677_CAFRO Unreviewed; 1215 AA.
AC A0A5A8C677;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN ORFNames=FNF29_06594 {ECO:0000313|EMBL:KAA0148536.1};
OS Cafeteria roenbergensis (Marine flagellate).
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Bicosoecida;
OC Cafeteriaceae; Cafeteria.
OX NCBI_TaxID=33653 {ECO:0000313|EMBL:KAA0148536.1, ECO:0000313|Proteomes:UP000323011};
RN [1] {ECO:0000313|EMBL:KAA0148536.1, ECO:0000313|Proteomes:UP000323011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BVI {ECO:0000313|EMBL:KAA0148536.1,
RC ECO:0000313|Proteomes:UP000323011};
RA Fischer M.G., Hackl T., Roman M.;
RT "Genomes of Cafeteria roenbergensis.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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:KAA0148536.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VLTN01000052; KAA0148536.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A8C677; -.
DR Proteomes; UP000323011; 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 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; 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; 2.
DR PRINTS; PR02008; RCMTFAMILY.
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000323011};
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 142..691
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 96..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..806
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 467
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 242..248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 307
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 414
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 1215 AA; 124258 MW; 5AE5F417C68EE183 CRC64;
MPIRGSKKKR GGRQARKPQV DIVMHNETFE AYYKAQNIVP EGEWDAFMAA LREQLPTNFR
VSAISPNADI LAGKVRDEYS PDEDLVRAAI KEATEAAEAN ADKRRDERQA ARGDAAAAAP
AAPAAGPSSS SAAAPAAPPA PAAAAAAAAP SEGGRLLPGR GNAADGPAGS VTPAALPWFP
DGYAFQLDLP RRFVKKVPPL KALLDLVIHC NDAGSMSRSE AVSMIPPVVL QVEPGHRVLD
MCAAPGSKTV QLLEAVQSAE RDVDASGVPA LPTGLVVANE MNPRRAYLLA SQAERLGSPA
LVVVTHDGRT LPDFNSLAWR GQAPDTPELR AAIARALGRA EHGGVALPHK EGSAAPMTSA
ASGESSSSSS SSSSSSSSSS SSSAAAAAAT AGPRTVWEAA TTERGSFFDR VLADVPCSGD
GTMRKNLSVW KTFTPGDGLA LHPMQLAIGA RGLQLLRTGG LMVYSTCTFN PIEDEAVVAS
LLRWAKGAVE VVDPRETVPG LRCHPGISSW KVLDRNLGDW SSFGAVEEAL RAKRRARLAN
RRRLVEARML KEAEAEAERS AKLAESLKAA AETAAAGAAA VSADSAEAKA AAEAKASEAA
AAAASAAAAA ATAAAAAAAA VAPDTPAIRA RDAANSAGGT SLNERSLLKM TSTLFPPSPE
EAASMHLDRC VRILPHDANT GGFFVCLLRK VAPTPAEPFS MAGFGPFPET NGFAPDDEAM
IADKEFLAEH DVDAGKSLGD DGSVRSGNHR TIKKRPRPGQ RGNGSHGGTP TASGDADDDA
DGTPRAGGGD DDDDAPFDDD DDAAGADDGS AAAAAKVARP DGDAAGSSSA PAASAAAAAA
AAAAAAASTA AAAAAADADQ RVSAEGYTPV SDRRLPVREG APVWVGTRHH PTLLALPDPG
NLMVVLQRAP PLVVDVFADA YGLGTSFPRD RIFLRNGSVT TLYYHSAGLA NDILAPLDHA
CAVQDALELR TRTRVKVVSA GVKLAEARGS IRTENATVSD AESVRRLGLR PNQAGLHLMA
CHATRRVLDL STSLFGEILE KTSDNLPVPL HGLSAELRAV VTGTLTAAVD AETARIAAAE
GSATSTSTSA AAAAAAAAGG GGAADGDSDE ETAPGQVSSA RNGSLIVRLD DAMLAAAASA
DGAHPATAAL SNAALRAHFI ARTAFTVWVS KGSVLVHVRK GAALALRQTL HERALGPAVD
LARPSQGGGR DDRDD
//