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Database: UniProt
Entry: A0A093IQJ1_DRYPU
LinkDB: A0A093IQJ1_DRYPU
Original site: A0A093IQJ1_DRYPU 
ID   A0A093IQJ1_DRYPU        Unreviewed;       649 AA.
AC   A0A093IQJ1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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};
DE   Flags: Fragment;
GN   ORFNames=N307_12458 {ECO:0000313|EMBL:KFV68986.1};
OS   Dryobates pubescens (Downy woodpecker) (Picoides pubescens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Dryobates.
OX   NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV68986.1, ECO:0000313|Proteomes:UP000053875};
RN   [1] {ECO:0000313|EMBL:KFV68986.1, ECO:0000313|Proteomes:UP000053875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV68986.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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   EMBL; KL216285; KFV68986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093IQJ1; -.
DR   STRING; 118200.A0A093IQJ1; -.
DR   Proteomes; UP000053875; 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:0007610; P:behavior; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
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   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; 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.
PE   3: Inferred from homology;
KW   Behavior {ECO:0000256|ARBA:ARBA00022610};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU00958}; Reference proteome {ECO:0000313|Proteomes:UP000053875};
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|ARBA:ARBA00022833}.
FT   DOMAIN          108..128
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   REGION          521..547
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..547
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFV68986.1"
FT   NON_TER         649
FT                   /evidence="ECO:0000313|EMBL:KFV68986.1"
SQ   SEQUENCE   649 AA;  73518 MW;  8E1B4F081E5063BD CRC64;
     EKHISIQRDF AELEKLANLK EGEFTTAAPQ NTDLQVTDEK KPCPLCSEEK YKACYSHKLH
     RHLLNFHWKV SVEFEGYRMC ICYLPCHPVK PNLIGDQTFS KMGAHYHCII CSATITRRTD
     MISHINRHVN KGETESRFIT VPAPKNSHQV LKESATDVRV LPNYSTPQKT DSYFNPKMKL
     NRQLIFSALA VLAKERTPIE CLDAFGATGI MGLQWAKHLR SSVRVTINDC NENSVAMIQE
     NCHLNKMKVK LNTKEDDNDE AMRDGEDNTD TIEVTKMDAN VIMHLRSFDF IHLDPFGTTV
     NYLDSAFRNV RNLGIVSLTS TDISSLYSKA QHVALRHYGC NIVRTEYYKE LAARIVIAAV
     ARAAARCNKG IEVLLAVALE HFVLVVVRVL RGPSSADDSA QKIRYLIHCQ WCEERTFQKE
     GNMLEENPYQ QLPCDCHGSM PGKTAVVLGP LWSGALFNAG FLRRMYFESA QYGLDETQSL
     LKTLVCEAEC TTLKHYSIHT SCEETKQEEC GVYIKTPNTS PESLVHRKRK SDEVTRNTNK
     RQKAENSAEH PAFYYNIHRH SIKGMNMPKL NRFLNYLSEA GYRVSRTHFD PMGVRTNAPL
     AQFKTVLLKY STPTYGGGQA EDAEVLEEDR SGTAAIVFTK DCPPHCAAD
//
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