ID A0A2K5UCK9_MACFA Unreviewed; 844 AA.
AC A0A2K5UCK9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=NOP2 nucleolar protein {ECO:0000313|Ensembl:ENSMFAP00000010100.2};
GN Name=NOP2 {ECO:0000313|Ensembl:ENSMFAP00000010100.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000010100.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000010100.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000010100.2}
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; A0A2K5UCK9; -.
DR STRING; 9541.ENSMFAP00000010100; -.
DR Ensembl; ENSMFAT00000038678.2; ENSMFAP00000010100.2; ENSMFAG00000004333.2.
DR VEuPathDB; HostDB:ENSMFAG00000004333; -.
DR GeneTree; ENSGT00940000161554; -.
DR Proteomes; UP000233100; Chromosome 11.
DR Bgee; ENSMFAG00000004333; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
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:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IEA:Ensembl.
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; 2.
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:UP000233100};
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 332..619
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..161
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 549
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 424..430
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 448
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 475
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 492
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 844 AA; 92904 MW; 600B206A6EA07F09 CRC64;
MGRKLDPTKK EKRGPGRKAR KQKGAETELA RFLPAVSDEN SKRLSSRARK RAAKRRLGSA
EVPKTNKSPE AKPLPGKLPK GIFAGAVQTA GKKGPQSLFN AAQGKKRPAP SSDEEEEEED
SEEDDVVNQG DLWGSEDDAD MVDDYGADSN SEDEEEGEEA GVQWLDLGSL QPPPSGFKQF
SCLSFLSSWY LQLLPIERAA RKQKVREAAA GVQWSEEETE DEEEEVTPES GPSKEEEADG
GLQINVDEEP FVLPPAGEME QDAQAPDLQR VHKRIQDIVG ILRDFGAQRE EGRSRSEYLN
RLKKDLATYY SYGDFLLGKL MDLFPLSELV EFLEANEVPR PVTLRTNTLK TRRRDLAQAL
INRGVNLDPL GKWSKTGLVV YDSSVPIGAT PEYLAGHYML QGASSMLPVM ALAPQEHERI
LDMCCAPGGK TSYMAQLMKN TGVILANDAN AERLKSVVGN LHRLGVTNTV ISHYDGRQFP
KVVGGFDRVL LDAPCSGTGV ISKDPAVKTN KDEKDILRCA HLQKELLLSA IDSVNATSKT
GGYLVYCTCS IMVEENEWVV DYALKKRNVR LVPTGLDFGQ EGFTRFRERR FHPSLRSARR
FYPHTHNMDG FFIAKFKKFS NSIPQSETGN SETATPKNVD LPQVIPKSEN SSQPAKKAKG
AAKTKQPLQK QQRPKKASFQ KPNGTSKGAD SELSTVPSVR KTQASSRCQD SSQPAGKAEG
IRESKVTGKL KQRSPKLQSS KKVAFLKQNA PPKGTDTETP AVLSPSKTQA TLKPKDHHHP
LGRAKGVEKQ QLPEQPFKKA AFQKQNDTPK GPQPPTVSPI SSSRPPPAKR KKSQSRGNGQ
LLLS
//
