ID A0A1H0Y1G9_9EURY Unreviewed; 496 AA.
AC A0A1H0Y1G9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=DWB78_11170 {ECO:0000313|EMBL:RDI72225.1}, SAMN05216278_0342
GN {ECO:0000313|EMBL:SDQ09017.1};
OS Halopelagius longus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae.
OX NCBI_TaxID=1236180 {ECO:0000313|EMBL:SDQ09017.1, ECO:0000313|Proteomes:UP000199289};
RN [1] {ECO:0000313|Proteomes:UP000199289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|Proteomes:UP000199289};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SDQ09017.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12397 {ECO:0000313|EMBL:SDQ09017.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RDI72225.1, ECO:0000313|Proteomes:UP000255421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC12-B1 {ECO:0000313|EMBL:RDI72225.1,
RC ECO:0000313|Proteomes:UP000255421};
RA Zhang X.;
RT "Genome sequence of extremly halophilic archaeon Halopelagius longus strain
RT BC12-B1.";
RL Submitted (JUL-2018) 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; QQST01000001; RDI72225.1; -; Genomic_DNA.
DR EMBL; FNKQ01000001; SDQ09017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0Y1G9; -.
DR OrthoDB; 6871at2157; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000199289; Unassembled WGS sequence.
DR Proteomes; UP000255421; Unassembled WGS sequence.
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; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 1.
DR HAMAP; MF_01634; TgtA_arch; 1.
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 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 14..340
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 196
FT /ligand="substrate"
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 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
SQ SEQUENCE 496 AA; 54532 MW; 74F060461FE7FA26 CRC64;
MRDHFEIRDG DVAGRIGELT VPRAGVTVET PALLPVVNPN IVTVSPARLE SEFGAEILIT
NSYIIKTNEH LREEALDVGL HEMLDFDGAI MTDSGSFQLA EYGDIDVTTK QILQFQRDIG
TDIATPVDIP TPPDVSREQA ERELDVTEEA LRDAEDAETG EMLVNAPVQG STYPDLRERG
GRTADATDLD VFPVGAVVPL MNAYRYDDMV DAVAAAKRGL GADAPVHLFG AGHPMMFALA
VALGCDLFDS AAYALYARDG RYLTVHGTEH LGELDYFPCS CAVCSAYSPE ELRETEGEER
ERLLAEHNLH VSFAEIRRVK QAIRAGELLE LVEERARSHP AMLDGYRALL DHADQLERED
PASKGSFFYL SSESARRPEV LRHHRRLERL EAEGRILLTQ GGKASGDRFD ASWRVVPPFG
PFPRALSETY PLTAEVPERT DPAAYEMAAE GVARLAESHP DTEFVLAHDG WPETALSKVP
DSVTAELLGR VPSDDD
//
