ID A0A1Q8B332_9CREN Unreviewed; 527 AA.
AC A0A1Q8B332;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=AUF79_15590 {ECO:0000313|EMBL:OLE86396.1};
OS Crenarchaeota archaeon 13_1_20CM_2_51_8.
OC Archaea; Thermoproteota.
OX NCBI_TaxID=1805093 {ECO:0000313|EMBL:OLE86396.1, ECO:0000313|Proteomes:UP000186073};
RN [1] {ECO:0000313|EMBL:OLE86396.1, ECO:0000313|Proteomes:UP000186073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLE86396.1}.
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DR EMBL; MNKD01000700; OLE86396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8B332; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000186073; 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; 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 12..333
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT ACT_SITE 85
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
SQ SEQUENCE 527 AA; 59465 MW; BC4EEA65EE3E8DAC CRC64;
MSFQVHCKDL LGRIGTINTK SGAFATPHMF PVLDPHHRIL GRKFFDRVGI NAVMTNAYLL
KRGRQGLDPV DVHGTLDYPH TVATDSGAYQ ILEYGYVGVT PEEIVAYQEK INTDIGVILD
FPTGFKSDAS RARWTVDETV RRADQALEVI TRKDILWVGP VQGGVHLKEV ERSARLMADR
DFDIFALGSP TELMETQRYD LLVDMIVAAK KALPKGKPFH LFGAGHPVLF PFLVALGCDL
FDSAAYALYA RAGRYLTPEG TLLLRDMVEF ACPCPACVDT SPDELMKSQD NEGETRLAQH
NLWTCNSELR RVREAIRRGR LWELLELRSQ AHPALKECFT RIVQYAEILE RSTPAVKPCG
IFYLGLSSNN RPEKLRFVSK LPGSVEERRK LVLVLPGRWR RPFHEDPRYE SVTKAFDDHP
KVSICFYSLS WGPVPIELDE TFPIAQTEGP DSGDYLVLEE RAKKVSDFVR SLHPKRVVLV
SDGDYGRAVT EELSKRFAKR ILAVLNGEKM KPDAIIKSLE RKIVLKA
//
