TRM10_SULAC
ID TRM10_SULAC Reviewed; 292 AA.
AC Q4J894;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=tRNA (adenine(9)-N1)-methyltransferase;
DE EC=2.1.1.218;
DE AltName: Full=tRNA(m1A9)-methyltransferase;
DE Short=tRNA(m1A9)MTase;
GN OrderedLocusNames=Saci_1677;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20525789; DOI=10.1093/nar/gkq451;
RA Kempenaers M., Roovers M., Oudjama Y., Tkaczuk K.L., Bujnicki J.M.,
RA Droogmans L.;
RT "New archaeal methyltransferases forming 1-methyladenosine or 1-
RT methyladenosine and 1-methylguanosine at position 9 of tRNA.";
RL Nucleic Acids Res. 38:6533-6543(2010).
CC -!- FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent formation of
CC N(1)-methyladenine at position 9 (m1A9) in tRNA.
CC {ECO:0000269|PubMed:20525789}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43148, Rhea:RHEA-COMP:10363, Rhea:RHEA-COMP:10364,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.218;
CC Evidence={ECO:0000269|PubMed:20525789};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
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DR EMBL; CP000077; AAY80987.1; -; Genomic_DNA.
DR RefSeq; WP_011278489.1; NC_007181.1.
DR PDB; 5A7T; X-ray; 2.40 A; A=1-249.
DR PDB; 5A7Y; X-ray; 2.50 A; A/B=1-292.
DR PDB; 5A7Z; X-ray; 2.10 A; A=1-249.
DR PDBsum; 5A7T; -.
DR PDBsum; 5A7Y; -.
DR PDBsum; 5A7Z; -.
DR AlphaFoldDB; Q4J894; -.
DR SMR; Q4J894; -.
DR STRING; 330779.Saci_1677; -.
DR EnsemblBacteria; AAY80987; AAY80987; Saci_1677.
DR GeneID; 3474107; -.
DR KEGG; sai:Saci_1677; -.
DR PATRIC; fig|330779.12.peg.1612; -.
DR eggNOG; arCOG00967; Archaea.
DR HOGENOM; CLU_061952_0_0_2; -.
DR OMA; GVEKRCR; -.
DR BioCyc; MetaCyc:SACI_1677-MON; -.
DR BRENDA; 2.1.1.218; 6160.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR016742; tRNA_m1G_mtfrase_arc.
DR PIRSF; PIRSF018978; tRNA_m1G_mtfrase_arc_prd; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..292
FT /note="tRNA (adenine(9)-N1)-methyltransferase"
FT /id="PRO_0000407927"
FT DOMAIN 72..253
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:5A7Z"
FT HELIX 28..37
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 38..55
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 58..75
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:5A7Z"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5A7Z"
FT HELIX 102..122
FT /evidence="ECO:0007829|PDB:5A7Z"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:5A7Z"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:5A7T"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5A7Z"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5A7Y"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:5A7Z"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:5A7Z"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:5A7Z"
FT HELIX 249..263
FT /evidence="ECO:0007829|PDB:5A7Y"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:5A7Y"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:5A7Y"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:5A7Y"
SQ SEQUENCE 292 AA; 33153 MW; BA8D4E480797D5C4 CRC64;
MTLAKVFSQK LRELGISSIY IGHERPSLQS LAIKMLLKNY GLVEERREGM LITQDHGIKL
ISGKGTETSR YTFRKGGKKV SIHLPEYPKM VIDLGLFEFL NEEEKEKTLL QVDLCLSVIR
KFLWDGNLTV VGKADYVLGR ANIVQSLSLS DEDNPVILDP YGDVVATDQI LRDHNVFVIG
GIVDKGRRLD RATERLALSR GYSFPRVKIQ LRGSIIGVPD EINKILEIIL RVKELDQSLE
EAIISLQSKS DKISRLLHDV QLYGMEVLEE EARWLRADDK VIEIVRSRLG KN
