UniProt: A0A3Q3ESD7

Database: UniProt
Entry: A0A3Q3ESD7_9LABR

LinkDB:  A0A3Q3ESD7_9LABR 
Original site:  A0A3Q3ESD7_9LABR

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (8)   
   InterPro (3)   
   Pfam (1)   
   PROSITE (3)   
   SMART (1)   
All databases (17)   

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ID   A0A3Q3ESD7_9LABR        Unreviewed;       613 AA.
AC   A0A3Q3ESD7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000256|PROSITE-ProRule:PRU00958};
DE            EC=2.1.1.216 {ECO:0000256|PROSITE-ProRule:PRU00958};
GN   Name=TRMT1L {ECO:0000313|Ensembl:ENSLBEP00000010299.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000010299.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000010299.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May play a role in motor coordination and exploratory
CC       behavior. {ECO:0000256|ARBA:ARBA00003652}.
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   AlphaFoldDB; A0A3Q3ESD7; -.
DR   Ensembl; ENSLBET00000010862.1; ENSLBEP00000010299.1; ENSLBEG00000007982.1.
DR   GeneTree; ENSGT00530000063646; -.
DR   InParanoid; A0A3Q3ESD7; -.
DR   Proteomes; UP000261660; Unplaced.
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:0007610; P:behavior; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002905; Trm1.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR10631; N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10631:SF1; TRMT1-LIKE PROTEIN; 1.
DR   Pfam; PF02005; TRM; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51626; SAM_MT_TRM1; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   3: Inferred from homology;
KW   Behavior {ECO:0000256|ARBA:ARBA00022610};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00958}; Reference proteome {ECO:0000313|Proteomes:UP000261660};
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}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          146..173
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   613 AA;  67400 MW;  331DDDFB5A03137A CRC64;
     MAELKEADAA QLHQEDVDIK RGAAGDAPSV DDQTADQTAK NEAASDSDSK PSTTTPERHI
     SIQTKLEGFE MLVDLNGAGR KSCPLCPEEK FKACYSHKLR RHLQNLHWKV YVEFEGQRMC
     ICHLPCRNLK PSLSGDQASG RHVAHYHCVV CSVTIARKTD MVSHLKRHVN KGETEASYSG
     SSDAQIEEPA PSGQAFEIMK ELGTNVQLLP NHTTPQKSDT YFNRKMRPNR QLVFCSLAVL
     AEERNPLECL DAFGATGIMG LQWAKHLRSA VKVTITDISD TCVKMIKENC ELNNMRVDGS
     PRAPRGGPDG AAGEVKGAPI ATVEVAKMDA NVIMHLRSFD YIHLDPYGTA VNYLDAAFRN
     VRNLGIISVT STDTGSLYSK SPNVTLRHYG CHIVRTEYYK ELAARMVVAT VARAAARCNK
     GIEVLLAVAL EHFVLVVVRV LRGPTQADES AKKLRKLVHC QWCEERVFLK LGNMTDDTLP
     CNCHGSLPGR TAVQLGPLWC GPLFNTGFLR RMLSAAVQHS MDDIQGLVKT LICESECTVL
     KSSALTNQAE CGVVIKTPPN GEESGPADQS GKRKSGEESG NVVKKLKSDA SLEHPPFYYS
     IHRHSIRGMN MPK
//

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