TRMJ_SULAC
ID TRMJ_SULAC Reviewed; 235 AA.
AC Q4JB16;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=tRNA (cytidine-2'-O-)-methyltransferase TrmJ {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:24951554};
DE AltName: Full=tRNA (cytidine(32)-2'-O)-methyltransferase {ECO:0000305};
DE AltName: Full=tRNA Cm32 methyltransferase {ECO:0000305};
GN Name=trmJ {ECO:0000303|PubMed:24951554};
GN OrderedLocusNames=Saci_0621 {ECO:0000312|EMBL:AAY80013.1};
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] {ECO:0007744|PDB:4CNF, ECO:0007744|PDB:4CNG}
RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEXES WITH
RP 5'-DEOXY-5'-METHYLTHIOADENOSINE AND S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF GLU-11; TYR-14; ARG-21;
RP LYS-45; PHE-46; SER-47; LYS-49; SER-79; ILE-80; LYS-84; ARG-89; SER-114;
RP ARG-119; TYR-137; PRO-138 AND VAL-139.
RX PubMed=24951554; DOI=10.1261/rna.044503.114;
RA Somme J., Van Laer B., Roovers M., Steyaert J., Versees W., Droogmans L.;
RT "Characterization of two homologous 2'-O-methyltransferases showing
RT different specificities for their tRNA substrates.";
RL RNA 20:1257-1271(2014).
CC -!- FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32) at
CC position 32 in tRNA. Is specific for cytidine.
CC {ECO:0000269|PubMed:24951554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42932, Rhea:RHEA-COMP:10288, Rhea:RHEA-COMP:10289,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000269|PubMed:24951554};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24951554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family. {ECO:0000305}.
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DR EMBL; CP000077; AAY80013.1; -; Genomic_DNA.
DR RefSeq; WP_011277515.1; NC_007181.1.
DR PDB; 4CNF; X-ray; 1.40 A; A/B=1-235.
DR PDB; 4CNG; X-ray; 1.10 A; A/B=1-235.
DR PDBsum; 4CNF; -.
DR PDBsum; 4CNG; -.
DR AlphaFoldDB; Q4JB16; -.
DR SMR; Q4JB16; -.
DR STRING; 330779.Saci_0621; -.
DR EnsemblBacteria; AAY80013; AAY80013; Saci_0621.
DR GeneID; 3474207; -.
DR KEGG; sai:Saci_0621; -.
DR PATRIC; fig|330779.12.peg.600; -.
DR eggNOG; arCOG01018; Archaea.
DR HOGENOM; CLU_056931_3_0_2; -.
DR OMA; PIMNLSH; -.
DR BRENDA; 2.1.1.200; 6160.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR004384; RNA_MeTrfase_TrmJ/LasT.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR42786; PTHR42786; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR PIRSF; PIRSF004808; LasT; 1.
DR SUPFAM; SSF75217; SSF75217; 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..235
FT /note="tRNA (cytidine-2'-O-)-methyltransferase TrmJ"
FT /id="PRO_0000442205"
FT BINDING 77..79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:24951554"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:24951554"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:24951554"
FT BINDING 138..140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000305|PubMed:24951554"
FT MUTAGEN 11
FT /note="E->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 14
FT /note="Y->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 21
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 45
FT /note="K->E: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 46
FT /note="F->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 47
FT /note="S->L: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 49
FT /note="K->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 49
FT /note="K->G: No change in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 79
FT /note="S->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 80
FT /note="I->R: No change in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 84
FT /note="K->E: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 89
FT /note="R->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 114
FT /note="S->R: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 119
FT /note="R->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 119
FT /note="R->N: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 137
FT /note="Y->F: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 138
FT /note="P->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT MUTAGEN 139
FT /note="V->S: No change in activity."
FT /evidence="ECO:0000269|PubMed:24951554"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:4CNG"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:4CNG"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4CNG"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:4CNG"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4CNG"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:4CNG"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:4CNG"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:4CNG"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:4CNG"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:4CNG"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4CNG"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:4CNG"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:4CNG"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:4CNG"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:4CNG"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:4CNG"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:4CNG"
SQ SEQUENCE 235 AA; 26902 MW; A5B925CFBA819DCF CRC64;
MTIRLVIVEP EGAYNLGFIA RLVKNFLIDE FYVVNPKCDI NEAIKFSAKG SEVIEKMMKI
TNNFDDAIRD VDLKIATSSI ADIKGDLLRK SIRPIDLERL IKDKKVAFIF GRESVGLTRE
EIAKSDFLLF IPANPEYPVL NLSHAVGIVL YELWRNRDNK VPTVSSEPIK LIDDYSKKIT
DILVNKEATK SMYLVLKRVL IKGIEDNEEA MTIVRILRKI YVRLAKKENE SDKLL
