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Database: UniProt
Entry: H0W2B3_CAVPO
LinkDB: H0W2B3_CAVPO
Original site: H0W2B3_CAVPO 
ID   H0W2B3_CAVPO            Unreviewed;       461 AA.
AC   H0W2B3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=NOP2/Sun RNA methyltransferase 5 {ECO:0000313|Ensembl:ENSCPOP00000017105.1};
GN   Name=NSUN5 {ECO:0000313|Ensembl:ENSCPOP00000017105.1};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000017105.1, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000017105.1}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000017105.1};
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   EMBL; AAKN02032057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005003723.1; XM_005003666.2.
DR   AlphaFoldDB; H0W2B3; -.
DR   SMR; H0W2B3; -.
DR   STRING; 10141.ENSCPOP00000017105; -.
DR   Ensembl; ENSCPOT00000025170.2; ENSCPOP00000017105.1; ENSCPOG00000023149.2.
DR   GeneID; 100716640; -.
DR   KEGG; cpoc:100716640; -.
DR   CTD; 55695; -.
DR   VEuPathDB; HostDB:ENSCPOG00000023149; -.
DR   eggNOG; KOG2360; Eukaryota.
DR   GeneTree; ENSGT00940000155974; -.
DR   HOGENOM; CLU_005316_7_4_1; -.
DR   InParanoid; H0W2B3; -.
DR   OMA; SFKSRIY; -.
DR   OrthoDB; 102852at2759; -.
DR   TreeFam; TF314285; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000023149; Expressed in cerebellum and 13 other cell types or tissues.
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   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000005447};
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          435..461
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   461 AA;  50196 MW;  7361FDCF1C98EFEF CRC64;
     MALYAAAAAV LAGVENRQGS LKGLVYASNF QNVKQLYALV CETQRYSAVL DAVIASAGLL
     RAEKKLRPHL AKVLVFELLL GKGFRGGGGR WKPLLARHQA RLKAELARLK VHRGVSRNED
     LLEVGSKLGP ASQVPRFVRV NTLKTCPDDV VDYFKRQGFS YQGRASSLEE LRALKGKHFA
     LDLLLPELLV FPAQTDLHEH PLYQAGHLIL QDKASCLPAM LLAPPPGSHV IDACAAPGNK
     TSHLAAILKN QGKIFAFDLD AKRLASMATL LARAGVSCCE LAEEDFLAVS PSDTRYAQVQ
     YILLDPSCSG SGMLSRQLEE PAAEPPSKER LCALSAFQLR VLRHALSFPA LQRLVYSTCS
     LCQEENEDVV RDALQQSLRP FRLVPILPSW PHRGLDTFPG AEHCLRASPE TTLTGGFFVA
     VIERAEVLSS ASLAEVPTPA PVPSPVPKRK RRRKAVASEG T
//
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