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Database: UniProt
Entry: A0A091DTL3_FUKDA
LinkDB: A0A091DTL3_FUKDA
Original site: A0A091DTL3_FUKDA 
ID   A0A091DTL3_FUKDA        Unreviewed;       462 AA.
AC   A0A091DTL3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Putative methyltransferase NSUN5 {ECO:0000313|EMBL:KFO35489.1};
GN   ORFNames=H920_03119 {ECO:0000313|EMBL:KFO35489.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO35489.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO35489.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO35489.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KN121778; KFO35489.1; -; Genomic_DNA.
DR   RefSeq; XP_010617300.1; XM_010618998.1.
DR   AlphaFoldDB; A0A091DTL3; -.
DR   SMR; A0A091DTL3; -.
DR   STRING; 885580.ENSFDAP00000018628; -.
DR   Ensembl; ENSFDAT00000013432; ENSFDAP00000018628; ENSFDAG00000009683.
DR   GeneID; 104858691; -.
DR   CTD; 55695; -.
DR   eggNOG; KOG2360; Eukaryota.
DR   OMA; SFKSRIY; -.
DR   OrthoDB; 102852at2759; -.
DR   Proteomes; UP000028990; 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   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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000028990};
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          126..425
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          429..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        359
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         234..240
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         258
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         285
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         305
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   462 AA;  50301 MW;  8841B12AA064F4FB CRC64;
     MALYAAAAAV LEGVENRKGS LKGLVYTSSF QNVKPLYALV CETQRYSAVL DAVIASAGLL
     RAEKKLRPHL AKVLVYELLL GKGFRGGGGR WKPLLGRHQA RLKAELARLK VHRGVSRNED
     LLEAGSRPGP ASQVPRFVRV NTLKTCPDDA VDYFKRKGFS YQGRASSLED LRALKGKHFF
     LDPLLPELLV FPAQTDLHEH PLYQAGHLIL QDKASCLPAM LLAPPPGSHV IDACAAPGNK
     TSHLAALLKN QGKIFAFDLD AKRLASMATL LARAGVSCCE LAEEDFLAVS PTDTRYARVQ
     YILLDPSCSG SGMLSRQLEE PGAEPPSKER LCALAAFQLR ALRHALTFPT VQRLVYSTCS
     LSQEENEDVV REALQQSSGA FRLAPILPSW PHRGLGTFPG AEHCLRASPT TTLTGGFFIA
     VIERTDVPSS PSLAEVPAPE PVPSPTLKRR KRRRKTAAHE ST
//
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