ID A0A0D2X256_CAPO3 Unreviewed; 829 AA.
AC A0A0D2X256;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=tRNA (Cytosine-5-)-methyltransferase NSUN2 {ECO:0000313|EMBL:KJE91974.1};
GN ORFNames=CAOG_003017 {ECO:0000313|EMBL:KJE91974.1};
OS Capsaspora owczarzaki (strain ATCC 30864).
OC Eukaryota; Filasterea; Capsaspora.
OX NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE91974.1, ECO:0000313|Proteomes:UP000008743};
RN [1] {ECO:0000313|Proteomes:UP000008743}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KE346363; KJE91974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2X256; -.
DR STRING; 595528.A0A0D2X256; -.
DR EnsemblProtists; KJE91974; KJE91974; CAOG_003017.
DR eggNOG; KOG2198; Eukaryota.
DR InParanoid; A0A0D2X256; -.
DR PhylomeDB; A0A0D2X256; -.
DR Proteomes; UP000008743; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0016428; F:tRNA (cytidine-5-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR InterPro; IPR023267; RCMT.
DR InterPro; IPR023270; RCMT_NCL1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22808; NCL1 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22808:SF1; RNA CYTOSINE C(5)-METHYLTRANSFERASE NSUN2; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR PRINTS; PR02011; RCMTNCL1.
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}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008743};
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}; tRNA processing {ECO:0000256|ARBA:ARBA00022694};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 149..511
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT REGION 27..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 401
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 267..273
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 324
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 348
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 829 AA; 90978 MW; B9FDB88556C99B28 CRC64;
MEQSALPQPQ TATTHVTHTS ASIFALCGDQ QPSKRGRGED DVAAADDAAP EQDAAAAAAA
AGATDDKDGS AGPSRRKQNK RAYLDNKKNR KLRQQKERAA KKAEEGIPAD PAQRAEYHRH
QPIEMTNARF EAFYKGLSQI IPENEWDAFM ETIRKPLPTS FRITGNSKKA AEMKRLLHQF
YFPSIETVEI AGERVSRPEC LSFYPDERAY QLDTSRKIFR SHPALSAFHK FLTVEVEMGN
FCRQEAVSMI PPLFLDVQPH HKVLDMCAAP GSKTGQLVEM LHQNDELMPS GFVVANDANY
KRCYLLIHQT KRLCSPSLLV TNLDASLFPT ILPGNRQPPV LFDRILCDAP CSGDGTMRKN
LDVWKNWRPS SGSNMHRLQI RILRRAVQLL EIGGMMVYST CSMHPGENEA VVAAILQQMP
GALELVDVSD KLPGLKRIPG LHTWKLMDGE GNWYSDASEV PVGHKEKRAL RGSLFPPPPE
VAAALHLERC VRVTPQLQNT GGFFIALLRK TSSVVKFFAT PGGRPARSAP SDAKADEAVG
EVIPEDAVPI VGEDEEDEAE DAADKAAAAA AVAGDNADDD DAAAPADDQK EVAMHVETVF
PKNTRTEAGY YFLTPEDPVV KLIVDYFDIS PEFDVTKLAS RSEAGKRTIY LVNDSLKQVM
NAVNASKLNL IMSGVKLFEK ASSTNGRFPY RVTNDGVQLI LPYLRKRVVH MTYPDVLVIA
KGDRTPFFDR MAPSTREQLQ ALAAVEQGAG VLVFDPQLNP HPDNTEIVER VCISTWIGKV
SLNVMVSKED MASLKNLIVV PDLAALSATA ATTDSTASSE AAPMDVVAE
//
