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Database: UniProt
Entry: A0A0Q0JKK2_9GAMM
LinkDB: A0A0Q0JKK2_9GAMM
Original site: A0A0Q0JKK2_9GAMM 
ID   A0A0Q0JKK2_9GAMM        Unreviewed;       242 AA.
AC   A0A0Q0JKK2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   ECO:0000313|EMBL:KPZ55765.1};
GN   ORFNames=AN393_01538 {ECO:0000313|EMBL:KPZ55765.1};
OS   Pseudoalteromonas sp. P1-25.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1723758 {ECO:0000313|EMBL:KPZ55765.1, ECO:0000313|Proteomes:UP000050552};
RN   [1] {ECO:0000313|EMBL:KPZ55765.1, ECO:0000313|Proteomes:UP000050552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-25 {ECO:0000313|EMBL:KPZ55765.1,
RC   ECO:0000313|Proteomes:UP000050552};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) 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}.
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:KPZ55765.1}.
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DR   EMBL; LKDW01000009; KPZ55765.1; -; Genomic_DNA.
DR   RefSeq; WP_055016630.1; NZ_LKDW01000009.1.
DR   AlphaFoldDB; A0A0Q0JKK2; -.
DR   PATRIC; fig|1723758.3.peg.1571; -.
DR   OrthoDB; 9806346at2; -.
DR   Proteomes; UP000050552; Unassembled WGS sequence.
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   PIRSF; PIRSF004808; LasT; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU362024};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU362024};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU362024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPZ55765.1};
KW   tRNA processing {ECO:0000256|RuleBase:RU362024}.
FT   DOMAIN          6..154
FT                   /note="tRNA/rRNA methyltransferase SpoU type"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
SQ   SEQUENCE   242 AA;  26304 MW;  7F5DA04D29C8B351 CRC64;
     MILDDIRIVL VNTSHSGNIG SAARAMKTMG LSKLYLVDPA CEVDSHASAL AAGATDVLGN
     AVIVDTVADA IADCALTIGT SARSRTLSWP MVEPRECGEK LVAEAANGPV ALVFGRENSG
     LTNEELQLCN YHVCIPANPE YSSLNLAMAV QTLSYETRMA FLNQQPKAEQ ADDETAYPSS
     KQTELFYEHL EQTLDNTGFI IKQHPGLVMT KLRRLFNRAR PEEAELNILR GILTSINKSI
     PK
//
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