GenomeNet

Database: UniProt
Entry: H9G3D0_ANOCA
LinkDB: H9G3D0_ANOCA
Original site: H9G3D0_ANOCA 
ID   H9G3D0_ANOCA            Unreviewed;       475 AA.
AC   H9G3D0;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=SAM-dependent MTase RsmB/NOP-type domain-containing protein {ECO:0000259|PROSITE:PS51686};
GN   Name=nsun5 {ECO:0000313|Ensembl:ENSACAP00000000181.3};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000000181.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000000181.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000000181.3};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000000181.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   RefSeq; XP_003226776.1; XM_003226728.3.
DR   AlphaFoldDB; H9G3D0; -.
DR   SMR; H9G3D0; -.
DR   STRING; 28377.ENSACAP00000000181; -.
DR   Ensembl; ENSACAT00000000184.3; ENSACAP00000000181.3; ENSACAG00000000193.3.
DR   GeneID; 100552807; -.
DR   KEGG; acs:100552807; -.
DR   CTD; 55695; -.
DR   eggNOG; KOG2360; Eukaryota.
DR   GeneTree; ENSGT00940000155974; -.
DR   HOGENOM; CLU_005316_7_4_1; -.
DR   InParanoid; H9G3D0; -.
DR   TreeFam; TF314285; -.
DR   Proteomes; UP000001646; Unplaced.
DR   Bgee; ENSACAG00000000193; Expressed in ovary and 12 other cell types or tissues.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000001646};
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          441..475
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         249..255
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         273
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         300
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         320
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   475 AA;  51725 MW;  550CBC8E2FC0C755 CRC64;
     MREKRGRAGV GKASGPGLYA AAASVLSGLE QRSGSLKALV YGSRFPGPRL LLALVSETLR
     FGPVLEALLE ASGLLRAEKK LPPHLAKVLA YDLLFGKGLR GGGPWKAPLL KHRARLQAEL
     ARLKVRRGVS RDEDLLPPPA GGGGNGTLPR YVRVNTIKTR FDDAVDYFKR QGFVYQGRAS
     PEMKGVASLS GKTFLLDPHL PGVLIFPPGT DLHEDQLYKA GHVILQDKAS CLPAFLLNPT
     PGSHVLDACA APGNKTSHLA AIMGNKGRIF AFDLDAKRLA TMSTMLARAG VTCHNLAHQD
     FLATDPGDPK YSHVEYILLD PSCSGSGIVG RLPYEEEERM DAQRLQALAG FQRRMLGHAL
     KFPALRRLVY STCSLHQEEN EEVVRDVLEQ HGRDFRLVEA LPSWTPRGLG VFAEAKCCLR
     ASPKETLTNG FFVAVMERRQ AETEDQSSLT VLPETGSQGG ADKPSKKKKK KQKLC
//
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