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Database: UniProt
Entry: A0A199W6N6_ANACO
LinkDB: A0A199W6N6_ANACO
Original site: A0A199W6N6_ANACO 
ID   A0A199W6N6_ANACO        Unreviewed;       659 AA.
AC   A0A199W6N6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Putative methyltransferase NSUN6 {ECO:0000313|EMBL:OAY85137.1};
GN   ORFNames=ACMD2_04041 {ECO:0000313|EMBL:OAY85137.1};
OS   Ananas comosus (Pineapple) (Ananas ananas).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC   Bromelioideae; Ananas.
OX   NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY85137.1, ECO:0000313|Proteomes:UP000092600};
RN   [1] {ECO:0000313|EMBL:OAY85137.1, ECO:0000313|Proteomes:UP000092600}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC   TISSUE=Leaf {ECO:0000313|EMBL:OAY85137.1};
RX   PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA   Redwan R.M., Saidin A., Kumar S.V.;
RT   "The draft genome of MD-2 pineapple using hybrid error correction of long
RT   reads.";
RL   DNA Res. 0:0-0(2016).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAY85137.1}.
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DR   EMBL; LSRQ01000122; OAY85137.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A199W6N6; -.
DR   STRING; 4615.A0A199W6N6; -.
DR   Proteomes; UP000092600; 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; cd21150; PUA_NSun6-like; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
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; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF34; TRNA (CYTOSINE(72)-C(5))-METHYLTRANSFERASE NSUN6; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 2.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS50890; PUA; 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:UP000092600};
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          239..614
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        533
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         335..341
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         359
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         386
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         482
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   659 AA;  72691 MW;  E1A06E0E2ADAD094 CRC64;
     MKRASASFFS SLLGIRTFLL LRRRRRLSAA AAPLSFLRRS SFPHMVSSSS SSSSSMAKVA
     EEAAEGRYSY NPELRWNTQV EAYFAHAYGA EHFARISKAL TRPSCYSCIR VNTLKSSVDA
     VVEKLKNILD GNDMCNGIEA NQVNNQERVS NCNSTSGEAE TPIQFLGSSP ISKCQYPGLD
     NVVLVRGSGP HILCYDLTGE PMKEVIVSRK CAEAVLRGAQ VYVPGVLACS SHVEKGDKVA
     VSVAIEQPVE YGGWSVDPLY RERSGLYIGQ GVTSMSRAGI FRASEGVGVE MEDRVYKLPS
     FNDVLEGEIF LQNLPSIITA RVLDPQQGER ILDMCAAPGG KTTAIAILMR DKGEVVAIDR
     SHNKVMEILK LAAEMDLHCI KAYKLDALKS VRRTNEETDV EATVTEDDKS YKPAVGDQVS
     NTEKCCPNSK IEQNDRKLLS KADLMKNARK MKNGPGRNNS MGGRVEKSKG FMPNSFDRVL
     LDAPCSALGL RPRLFAGEET LESLRNHAKY QRRMFDQAIQ LVRAGGVIVY STCTINPGEN
     EALVRYALDT YKFLSLASQQ PKIGGPGIVG HCELFKETYV EGWLTKSEAE LVQRFDPSSS
     IDTIGFFIAK FDDNEFHSLT KLFIATGNDQ KSIAGAHYRG GTSFIFPRTS FFFSFFLRG
//
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