ID A0A0F7DC13_9EURY Unreviewed; 475 AA.
AC A0A0F7DC13;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=tRNA-guanine(15) transglycosylase {ECO:0000256|HAMAP-Rule:MF_01634};
DE EC=2.4.2.48 {ECO:0000256|HAMAP-Rule:MF_01634};
DE AltName: Full=7-cyano-7-deazaguanine tRNA-ribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01634};
DE AltName: Full=Archaeal tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_01634};
GN Name=tgtA {ECO:0000256|HAMAP-Rule:MF_01634};
GN ORFNames=GAH_00619 {ECO:0000313|EMBL:AKG92041.1};
OS Geoglobus ahangari.
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Geoglobus.
OX NCBI_TaxID=113653 {ECO:0000313|EMBL:AKG92041.1, ECO:0000313|Proteomes:UP000034723};
RN [1] {ECO:0000313|EMBL:AKG92041.1, ECO:0000313|Proteomes:UP000034723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=234 {ECO:0000313|EMBL:AKG92041.1,
RC ECO:0000313|Proteomes:UP000034723};
RA Manzella M.P., Holmes D.E., Rocheleau J.M., Chung A., Reguera G.,
RA Kashefi K.;
RT "The complete genome sequence of the hyperthermophilic, obligate iron-
RT reducing archaeon Geoglobus ahangari strain 234T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Exchanges the guanine residue with 7-cyano-7-deazaguanine
CC (preQ0) at position 15 in the dihydrouridine loop (D-loop) of archaeal
CC tRNAs. {ECO:0000256|HAMAP-Rule:MF_01634}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-cyano-7-deazaguanine + guanosine(15) in tRNA = 7-cyano-7-
CC carbaguanosine(15) in tRNA + guanine; Xref=Rhea:RHEA:43164,
CC Rhea:RHEA-COMP:10371, Rhea:RHEA-COMP:10372, ChEBI:CHEBI:16235,
CC ChEBI:CHEBI:45075, ChEBI:CHEBI:74269, ChEBI:CHEBI:82850; EC=2.4.2.48;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01634};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01634};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01634};
CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01634}.
CC -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_01634}.
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DR EMBL; CP011267; AKG92041.1; -; Genomic_DNA.
DR RefSeq; WP_048094636.1; NZ_CP011267.1.
DR AlphaFoldDB; A0A0F7DC13; -.
DR STRING; 113653.GAH_00619; -.
DR GeneID; 24803199; -.
DR KEGG; gah:GAH_00619; -.
DR PATRIC; fig|113653.22.peg.618; -.
DR HOGENOM; CLU_030083_0_0_2; -.
DR InParanoid; A0A0F7DC13; -.
DR OrthoDB; 6871at2157; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000034723; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016763; F:pentosyltransferase activity; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR Gene3D; 3.90.1020.10; ArcTGT, C1 domain; 1.
DR Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 1.
DR HAMAP; MF_01634; TgtA_arch; 1.
DR InterPro; IPR038370; ArcTGT_C1_sf.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR004804; TgtA.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR NCBIfam; TIGR00432; arcsn_tRNA_tgt; 1.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR PANTHER; PTHR46499; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR46499:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF88802; Pre-PUA domain; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01634}; Metal-binding {ECO:0000256|HAMAP-Rule:MF_01634};
KW Reference proteome {ECO:0000313|Proteomes:UP000034723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01634};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01634}; Zinc {ECO:0000256|HAMAP-Rule:MF_01634}.
FT DOMAIN 12..338
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
SQ SEQUENCE 475 AA; 54558 MW; 7B823AB97FE916E0 CRC64;
MRFEIVAKDA MGRIGRLQTP HGTVETPALL PVINPNIDFI PAHELRKYGA EMMITNSYII
YRSRNLRERA LKKGLHGLLG VDMPVMTDSG SFQLMVYGDV EVTNEEIVRF QNEIGSDIVT
PLDIPTPPDA EHETARKDLE ETIRREREAE EIHESYGHEN LLSIPIQGST HLDLRKRSAE
AANSINGDVF AVGAVVPLLD TYRFSDVAKI VLTAKSVLTP ARPVHLFGAG HPMIFALYAA
MGVDLFDSAA YALFAKDDRY LTPRGTLKLE ELQYFPCSCP VCLSHTPEEL RRMEKGERAR
LIAEHNLYVS FEEIRRVKQA IKSNELFELV ENRIRAHPYL VQAWREIRNF IDVMERHDPS
MKRVFFYLGR ESLYRPAIRR HHERVLNVKV DKDEIVISSD PGVKADFYLR PAFGVVPAEL
MESYPAGHAE MYDDVEDEAY EVAAEGLRRF MEKHRDKRIR LVLDDRWRRF VNVQD
//
