ID K9SGE9_9CYAN Unreviewed; 404 AA.
AC K9SGE9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ {ECO:0000256|RuleBase:RU362024};
DE EC=2.1.1.200 {ECO:0000256|RuleBase:RU362024};
DE AltName: Full=tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase {ECO:0000256|RuleBase:RU362024};
DE AltName: Full=tRNA Cm32/Um32 methyltransferase {ECO:0000256|RuleBase:RU362024};
GN Name=trmJ {ECO:0000256|RuleBase:RU362024};
GN ORFNames=Pse7367_0536 {ECO:0000313|EMBL:AFY68844.1};
OS Pseudanabaena sp. PCC 7367.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY68844.1, ECO:0000313|Proteomes:UP000010386};
RN [1] {ECO:0000313|EMBL:AFY68844.1, ECO:0000313|Proteomes:UP000010386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY68844.1,
RC ECO:0000313|Proteomes:UP000010386};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or
CC 2'O-methylated uridine (Um32) at position 32 in tRNA.
CC {ECO:0000256|RuleBase:RU362024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-
CC methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42936, Rhea:RHEA-COMP:10107, Rhea:RHEA-COMP:10290,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.200;
CC Evidence={ECO:0000256|RuleBase:RU362024};
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; EC=2.1.1.200;
CC Evidence={ECO:0000256|RuleBase:RU362024};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362024}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362024}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family.
CC {ECO:0000256|ARBA:ARBA00007228}.
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DR EMBL; CP003592; AFY68844.1; -; Genomic_DNA.
DR AlphaFoldDB; K9SGE9; -.
DR STRING; 82654.Pse7367_0536; -.
DR KEGG; pseu:Pse7367_0536; -.
DR PATRIC; fig|82654.3.peg.614; -.
DR eggNOG; COG0565; Bacteria.
DR HOGENOM; CLU_056931_3_0_3; -.
DR Proteomes; UP000010386; 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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd18093; SpoU-like_TrmJ; 1.
DR Gene3D; 1.10.8.590; -; 1.
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 NCBIfam; TIGR00050; rRNA_methyl_1; 1.
DR PANTHER; PTHR42786:SF2; TRNA (CYTIDINE_URIDINE-2'-O-)-METHYLTRANSFERASE TRMJ; 1.
DR PANTHER; PTHR42786; TRNA/RRNA METHYLTRANSFERASE; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU362024};
KW Methyltransferase {ECO:0000256|RuleBase:RU362024,
KW ECO:0000313|EMBL:AFY68844.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010386};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU362024};
KW Transferase {ECO:0000313|EMBL:AFY68844.1};
KW tRNA processing {ECO:0000256|RuleBase:RU362024}.
FT DOMAIN 45..195
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 404 AA; 44561 MW; CD8ACF910B8026B1 CRC64;
MVDNIKNNLT NDLHKDSSGD RHSALNNDLN DLNDLNDLND LNLDVRIVLV EPAGELNLGS
VARVMKNMGL SQLYLVNPHA DRHSEDAQHM AVHAKDILDT AQVVTSLPEA LAGCQRAIAT
VGRIDFTDQM LAEAKDVITG IEWLAAVSSS AIVFGPEDRG LSNREIAYCQ AILTIPTSAT
YPSLNLAQAV GICCYQLKLL AIQILVRDSD IPEPTTDRNN NQQGNSAITN SDYQPAAPIA
DISRRKPLSL KNQSRSPKTN ANLQLDSSEQ SNAITEIGQD VNIDQNIDQN VDRLDQANRH
APNLTNPNHL DREEHNASKF GQNTSQNDKD LLDSASIDAI EAYYQHLETV LLEIGFLYPH
TAFSRMKKLR RIFNKAALTE SEVTMLRGML SQIAWAAKHG DRDT
//
