ID A0A452RPB6_URSAM Unreviewed; 485 AA.
AC A0A452RPB6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=NOP2/Sun RNA methyltransferase 5 {ECO:0000313|Ensembl:ENSUAMP00000021085.1};
GN Name=NSUN5 {ECO:0000313|Ensembl:ENSUAMP00000021085.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000021085.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000021085.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR AlphaFoldDB; A0A452RPB6; -.
DR SMR; A0A452RPB6; -.
DR STRING; 9643.ENSUAMP00000021085; -.
DR Ensembl; ENSUAMT00000023554.1; ENSUAMP00000021085.1; ENSUAMG00000016585.1.
DR GeneTree; ENSGT00940000155974; -.
DR OMA; AVLKHYS; -.
DR OrthoDB; 102852at2759; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0050890; P:cognition; IEA:Ensembl.
DR GO; GO:0022038; P:corpus callosum development; IEA:Ensembl.
DR GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
DR GO; GO:0045727; P:positive regulation of translation; IEA:Ensembl.
DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
DR GO; GO:0070475; P:rRNA base methylation; IEA:Ensembl.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR049561; NSUN5_7_fdxn-like.
DR InterPro; IPR048889; NSUN5_RCM1_N.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22807:SF4; 28S RRNA (CYTOSINE-C(5))-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF21148; NSUN5_fdxn-like; 1.
DR Pfam; PF21153; NSUN5_N; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000291022};
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 140..439
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 373
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 248..254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 272
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 299
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 319
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 485 AA; 52604 MW; 1EE82BB750D06D14 CRC64;
MLARRRVGIQ SSAGEQPWGG GSGPGSKARG SALLSAINLF CGLGRNISFL PVTACLSGLL
SSSSSTLWSS KTLMLRVFFS FFPHPQVLVY ELLLGKGFRG GGGRWKPLLD RHRARLKAEL
ARLKVQRCVS RNEDLLQVGS RPGTASQLPR FVRVNTLKTN SDDAVDYFKR QGFSYQGRAS
SLEDLRALKG KCFFLDPLLP ELLVFPAQTD LHDHPLYRAG HLILQDKASC LPAMLLAPPP
GSHVIDACAA PGNKTSHLAA LLKNQGKIFA FDLDAGRLAS MATLLARAGV SCCELAEQDF
LAVSPSDQRY RQVQYILLDP SCSGSGMPAR QLEEPGAGTP SQARLQALAG FQQRALRHAL
TFPSLQRLVY STCSLCQEEN EDVVRDALQQ NPGTFRLAPV LPSWPHRGLG TFPGAEHCLR
ASPETTLTGG FFVAVLERVE VPSSVPQAAA AAPELTPSTA PRRKKRRRRA AAPGLLPRTQ
QEGKR
//
