UniProt: A7THP9

Database: UniProt
Entry: A7THP9_VANPO

LinkDB:  A7THP9_VANPO 
Original site:  A7THP9_VANPO

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (16)   

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ID   A7THP9_VANPO            Unreviewed;       559 AA.
AC   A7THP9;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
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=Kpol_543p45 {ECO:0000313|EMBL:EDO18215.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO18215.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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}.
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DR   EMBL; DS480392; EDO18215.1; -; Genomic_DNA.
DR   RefSeq; XP_001646073.1; XM_001646023.1.
DR   AlphaFoldDB; A7THP9; -.
DR   STRING; 436907.A7THP9; -.
DR   GeneID; 5546490; -.
DR   KEGG; vpo:Kpol_543p45; -.
DR   eggNOG; KOG1253; Eukaryota.
DR   HOGENOM; CLU_010862_4_1_1; -.
DR   InParanoid; A7THP9; -.
DR   OMA; MKCCHEM; -.
DR   OrthoDB; 942596at2759; -.
DR   PhylomeDB; A7THP9; -.
DR   Proteomes; UP000000267; 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   CDD; cd02440; AdoMet_MTases; 1.
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   NCBIfam; TIGR00308; TRM1; 1.
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:UP000000267};
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}.
SQ   SEQUENCE   559 AA;  62869 MW;  3CA4ED6C00203895 CRC64;
     MLQAVASKIK SKIFDSEPKR IEINPDDYNI VKEGKAEILF PKKETVFYNP VQQFNRDLSV
     TCIKAWDNLY GPKSSGNGKK SKKAQNKRSI EEDEDIAKIR RLADGSKQEI STSKHAPYLK
     ILEALSATGL RAIRYAHEIP NVKEIVANDL LPEAVDSIRR NAEYNKVENI VKPNIDDANV
     LMYRNKSTNT RYHVIDLDPY GTVTPFVDAA LQTIEDDGLM LVTCTDLSVL AGNGYPEKCF
     ALYGGVNMVS HEATHESALR LVLNLLSQSA AKYKKTIEPL LSLSIDFYVR VFIKVKTSPI
     NVKNLQSNTM ITYHCSQCGS YHNQHLGRIQ ERSGKNGKPF KKYLVAQGPP VDSKCKFCKG
     TYHLAGPMYA GALHNKEFLD EVLRINKVEH ANMGDVYGTR KRIEGMVTLA SKELADAPFY
     FSPNNISSIL KLQVPPLKKV VAGLGSLGYN CSLSHAQPSS LKTDAPWEAI WYVMKECDDK
     EVNLEKMNPN TAGYKILSTF DQWMPEEEDG REPMFKKSDL SFKENEQSGA VEKLRKLKIV
     RYQENPTKNW GPKARPNSS
//

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