ID A0A0P9I330_9ARCH Unreviewed; 540 AA.
AC A0A0P9I330;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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_1 {ECO:0000313|EMBL:KPV63363.1};
GN Synonyms=tgtA {ECO:0000256|HAMAP-Rule:MF_01634};
GN ORFNames=AOA65_1371 {ECO:0000313|EMBL:KPV63363.1};
OS Candidatus Bathyarchaeota archaeon BA1.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1700835 {ECO:0000313|EMBL:KPV63363.1, ECO:0000313|Proteomes:UP000050312};
RN [1] {ECO:0000313|EMBL:KPV63363.1, ECO:0000313|Proteomes:UP000050312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA1 {ECO:0000313|EMBL:KPV63363.1};
RX PubMed=26494757; DOI=10.1126/science.aac7745;
RA Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA Golding S.D., Tyson G.W.;
RT "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT genome-centric metagenomics.";
RL Science 350:434-438(2015).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01634}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPV63363.1}.
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DR EMBL; LIHJ01000055; KPV63363.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9I330; -.
DR STRING; 1700835.AOA65_1371; -.
DR KEGG; barc:AOA65_1371; -.
DR PATRIC; fig|1700835.3.peg.1151; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000050312; 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 Gene3D; 3.40.50.10630; Uracil-DNA glycosylase-like; 1.
DR HAMAP; MF_01634; TgtA_arch; 1.
DR InterPro; IPR040777; DUF5591.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR004804; TgtA.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
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; PF17884; DUF5591; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
DR SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 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 12..335
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT DOMAIN 376..510
FT /note="DUF5591"
FT /evidence="ECO:0000259|Pfam:PF17884"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 276
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"
SQ SEQUENCE 540 AA; 61585 MW; ADDA9C4281BD47B1 CRC64;
MSFEIKDRDL LARIGRFETK SGAIETPLLL PVINPTIQPV TPRTMQKEFS CPALITNAYI
VRKHFKDEAV QKGIHHFLDF NGVVMTDSGA YQILVYGGVE VTPDEIVQYQ EEINADIATI
LDVPTGWGVS EQYARQTVDE TLRRARGLAK IKTRDDIAWV GPVQGGQYLD LVARSAREMG
KLPFQIHALG SPTPVMEQYL FDILVDMIMA AKMNLPLERP LHLFGAGHPF MFALAISLGC
DLFDSAAYAM YARDDRYMTE YGTIKLDELQ YLPCSCPMCV KIDPKSMMTM PKTERQERLA
QHNLHVSFSE LRRIKQAIME GRLWEHLELR AHGHPALLQA LKNLRKYSGY VERHSPVTKK
SGLFFFSSLG MHRPEVVRHR KKLLERYSPP KGAKILILLP QTQMKPFHKS REYRRVLKEI
QQKLGDKVDE IHVCTYAAPF GVIPTELDEV YPLSQYEIAT PLDAETIRYT AKQAANYIAS
TSYKEIILLQ NAEMWKEQFV TACRRACKKG RIPLTVLRWE KTWGEDTLKT LVAAIQDALA
//
