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Database: UniProt
Entry: A0A087GUT6_ARAAL
LinkDB: A0A087GUT6_ARAAL
Original site: A0A087GUT6_ARAAL 
ID   A0A087GUT6_ARAAL        Unreviewed;       515 AA.
AC   A0A087GUT6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Methyltransferase small domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=AALP_Aa5g039700 {ECO:0000313|EMBL:KFK33638.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK33638.1, ECO:0000313|Proteomes:UP000029120};
RN   [1] {ECO:0000313|Proteomes:UP000029120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX   PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA   Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA   Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA   Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA   Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA   Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA   Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA   Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA   Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT   "Genome expansion of Arabis alpina linked with retrotransposition and
RT   reduced symmetric DNA methylation.";
RL   Nat. Plants 1:14023-14023(2015).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
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DR   EMBL; CM002873; KFK33638.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087GUT6; -.
DR   EnsemblPlants; KFK33638; KFK33638; AALP_AA5G039700.
DR   Gramene; KFK33638; KFK33638; AALP_AA5G039700.
DR   eggNOG; ENOG502QTKF; Eukaryota.
DR   OMA; WRLEKAH; -.
DR   OrthoDB; 1215241at2759; -.
DR   Proteomes; UP000029120; Chromosome 5.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   PANTHER; PTHR47548; BNAA06G32370D PROTEIN; 1.
DR   PANTHER; PTHR47548:SF1; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1.
DR   Pfam; PF03602; Cons_hypoth95; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000029120};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}.
FT   ACT_SITE        454
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         309
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         332
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         380
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   515 AA;  57492 MW;  3E12B545F0C609C3 CRC64;
     MHSSSLFSFG ARYPIISCRV SPPPPSPSLV ASLPLPSISS DSDVDSQAKS LACSLQCPHF
     QSCSGCTQEF NLHRPNVVDE ASGFFKRYGV EDFTFDSCRL WGWRCRAKLA VRGSSDNALI
     GLYQEGTHTV VDIPDCKSHH PNINAAIELL REGIKVFDVE PFDEDQNTGD LRYVQMAVTT
     HSTSLRAPER YKNGKVQVSL VWNSRNEKSH NADKLQALSS YLWRKGGPNS KFHLIHSVWA
     NFQTSTNNII FGNRWRHLLG ERDFWEHVGG IDISLDPSSF GQANTRAFDS LLWKLHKYVP
     GGSSVADLYA GAGVIGLSLA TSRKCSSVKC IEVNKEARLS FEKSIQRLPN SLNCSISWHH
     ADASVNPLSW IIGTDVVVVD PPRRGLDASL RQILESVPSI EKRMRSSSPS SSSTAKEEKR
     PWILRAKELS IQAGNKLIPE ESKTLPQRLI YISCGWESFK EDCKSLLSSR AWELENAHGF
     NFFPGTDSIE VLAIFKRRVV TKKKKKSGIK KVRSK
//
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