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Database: UniProt
Entry: A0A0V0QIJ6_PSEPJ
LinkDB: A0A0V0QIJ6_PSEPJ
Original site: A0A0V0QIJ6_PSEPJ 
ID   A0A0V0QIJ6_PSEPJ        Unreviewed;       545 AA.
AC   A0A0V0QIJ6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|ARBA:ARBA00039099, ECO:0000256|PROSITE-ProRule:PRU00958};
DE            EC=2.1.1.216 {ECO:0000256|ARBA:ARBA00039099, ECO:0000256|PROSITE-ProRule:PRU00958};
GN   ORFNames=PPERSA_05753 {ECO:0000313|EMBL:KRX01914.1};
OS   Pseudocohnilembus persalinus (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC   Pseudocohnilembus.
OX   NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX01914.1, ECO:0000313|Proteomes:UP000054937};
RN   [1] {ECO:0000313|EMBL:KRX01914.1, ECO:0000313|Proteomes:UP000054937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=36N120E {ECO:0000313|EMBL:KRX01914.1};
RX   PubMed=26486372; DOI=10.1038/srep15470;
RA   Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA   Miao W.;
RT   "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT   persalinus provides insight into its virulence through horizontal gene
RT   transfer.";
RL   Sci. Rep. 5:15470-15470(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU00958};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Trm1 family. {ECO:0000256|PROSITE-ProRule:PRU00958}.
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:KRX01914.1}.
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DR   EMBL; LDAU01000161; KRX01914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0QIJ6; -.
DR   EnsemblProtists; KRX01914; KRX01914; PPERSA_05753.
DR   InParanoid; A0A0V0QIJ6; -.
DR   OMA; CCYSRSP; -.
DR   OrthoDB; 942596at2759; -.
DR   Proteomes; UP000054937; Unassembled WGS sequence.
DR   GO; GO:0160102; F:tRNA (guanine(10)-N2)-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0160104; F:tRNA (guanine(26)-N2)-dimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProt.
DR   Gene3D; 3.30.56.70; N2,N2-dimethylguanosine tRNA methyltransferase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002905; Trm1.
DR   InterPro; IPR042296; tRNA_met_Trm1_C.
DR   PANTHER; PTHR10631; N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10631:SF3; TRNA (GUANINE(26)-N(2))-DIMETHYLTRANSFERASE; 1.
DR   Pfam; PF02005; TRM; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51626; SAM_MT_TRM1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00958}; Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00958};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU00958};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00958}; tRNA processing {ECO:0000256|PROSITE-ProRule:PRU00958};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|PROSITE-
KW   ProRule:PRU00958}.
FT   REGION          235..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  63496 MW;  9923464674B04CE7 CRC64;
     MYKIFFQGKE YFQGVTILDA LSASGLRTIR FLKELKDVKK VYANDLSEAS HKLMMDNFKL
     NELDLNKIQM TNKDANELMY MLKFQPQKEG DREEVIDVID LDPYGSSVPF LDAAIQCAKT
     DSLLCITCTD SKVLCGPDQQ KCFYQYGTSR AKVPAFQENA LRIVLYTVQN IASKYGKSIV
     PLFSYMQKEF YCRLFIQIKN SRSEAAKTYA QVGNVYYCEQ CYNYHTHTYG KEKNFKQDQQ
     EQQQVQNNKK KDDDKEEVKE KKQDAKQENK QYLKYNANYL KLPSNVCEMC GSYYHINGPL
     WLGELHNKEF INKLLHSLES EEMELQSSKK ITGLLKSVLN EFETFHDQVP PLGISPQRVL
     KLMRTQQPSK KELESAFKSL GYQFCPTFTN PDIYKTDAPN NIIYDIVKKY KIKLVGEENL
     FNKIEQDKLP VPYKLLSREV EIDPKFDLQI AKQSHYAVFL PNPKNFGPLS RATVQNQNSL
     FFKLKKNNYE KYLIRQVIDE EKQSNVQVIT KNEIGQQQEE QQIDEKNISQ DNEENGEKVT
     KKVKL
//
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