ID A0A2K6AH04_MANLE Unreviewed; 810 AA.
AC A0A2K6AH04;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000039305.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000039305.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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}.
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DR AlphaFoldDB; A0A2K6AH04; -.
DR Ensembl; ENSMLET00000062921.1; ENSMLEP00000039305.1; ENSMLEG00000043675.1.
DR GeneTree; ENSGT00940000155370; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
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; IPR031341; Methyltr_RsmF_N.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR011023; Nop2p.
DR InterPro; IPR012586; P120R_rpt.
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 Pfam; PF17125; Methyltr_RsmF_N; 1.
DR Pfam; PF08062; P120R; 3.
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:UP000233140};
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 298..585
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..159
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..196
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 515
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 390..396
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"
FT BINDING 441
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 458
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 810 AA; 89298 MW; 28DE152DF4065DC1 CRC64;
MGRKLDPTKK EKRGPGRKAR KQKGAETELA RFLPAEPGNI FSFLYSLNLL CLFRAAKRRL
GSAEVRKTNK SPEAKPLPGK LPKGAVQTAG KKGPQSLFNA AQGKKRPAPS SDEEEEEEDS
GEDDVVNQGD LWGSEDDADM VDDYGADSNS EDEEEGEELL PIERAARKQK VREAAAGVQW
SEEETEDEEE EVTPESGPSK EEEADGGLQI NVDEEPFVLP PAGEMEQDIL APDLQRVHKR
IQDIVGILRD FGAQREEGRS RSEYLNRLKK DLATYYSYGD FLLGKLMDLF PLSELVEFLE
ANEVPRPVTL RTNTLKTRRR DLAQALINRG VNLDPLGKWS KTGLVVYDSS VPIGATPEYL
AGHYMLQGAS SMLPVMALAP QEHERILDMC CAPGGKTSYM AQLMKNTGVI LANDANAERL
KSVVGNLHRL GVTNTVISHY DGRQFPKVVG GFDRVLLDAP CSGTGVISKD PAVKTNKDEK
DILRCAHLQK ELLLSAIDSV NATSKTGGYL VYCTCSIMVE ENEWVVDYAL KKRNVRLVPT
GLDFGQEGFT RFRERRFHPS LRSARRFYPH THNMDGFFIA KFKKFSNSIP QSETGDSETA
TPTNVDLPQV IPKSENSSQP AKKAKGAAKT KQQLQKQQHP KKASFQKPNG TSKGADSELS
TVPSVRKTQA SSRFQDSSQP AGKAEGIRES EVTGKLKQRS PKLQSSKKVA FLKQNAPPKG
TDTETLAVLS PAKTQATLKP KDHHHPLGRA KGVEKQQLPE QPFKKAAFQK QNDTPKGFQP
PTVSPISSSR PPPAKRKKSQ SRGNGQLLLS
//
