ID A0A219AJK7_9EURY Unreviewed; 659 AA.
AC A0A219AJK7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=BGI41_07165 {ECO:0000313|EMBL:OWT32533.1};
OS Methanobrevibacter sp. 87.7.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=387957 {ECO:0000313|EMBL:OWT32533.1, ECO:0000313|Proteomes:UP000197485};
RN [1] {ECO:0000313|EMBL:OWT32533.1, ECO:0000313|Proteomes:UP000197485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.7 {ECO:0000313|EMBL:OWT32533.1,
RC ECO:0000313|Proteomes:UP000197485};
RA Yeoman C., Mosoni P., White B.;
RT "De novo assembly of methanobrevibacter sp 87.7.";
RL Submitted (DEC-2016) 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|ARBA:ARBA00005030, ECO:0000256|HAMAP-Rule:MF_01634}.
CC -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.
CC {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:OWT32533.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MRCT01000169; OWT32533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A219AJK7; -.
DR OrthoDB; 6871at2157; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000197485; 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:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR CDD; cd21149; PUA_archaeosine_TGT; 1.
DR Gene3D; 3.90.1020.10; ArcTGT, C1 domain; 1.
DR Gene3D; 3.10.450.90; ArcTGT, C2 domain; 1.
DR Gene3D; 2.30.130.10; PUA 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; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR029402; TGT_C2.
DR InterPro; IPR038250; TGT_C2_sf.
DR InterPro; IPR004804; TgtA.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR InterPro; IPR004521; Uncharacterised_CHP00451.
DR NCBIfam; TIGR00432; arcsn_tRNA_tgt; 1.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR NCBIfam; TIGR00451; unchar_dom_2; 1.
DR PANTHER; PTHR46499; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR46499:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE; 1.
DR Pfam; PF01472; PUA; 1.
DR Pfam; PF01702; TGT; 1.
DR Pfam; PF14810; TGT_C2; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF88802; Pre-PUA domain; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
DR PROSITE; PS50890; PUA; 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 584..658
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01634"
SQ SEQUENCE 659 AA; 74687 MW; 758E85C09C98EDF9 CRC64;
MFEIKAKDNR GRVGVLKTKH GNVTTPALMP VIHPGKQTID VKKYGADIVI TNSYIIFKDE
ELKQKALEEG VHKLINFDGP IMTDSGSFQL SVYGDIDIGN KEVIDFQEKI GTDIGTSLDI
PTGPFVKRED AERDLEITIN RAKEAVEYKK ENNISMLLNS VVQGSTFLDL REKCADELTK
LDADLYPIGA VVPLMEMYKY SDLVDVVMHS VSHLPDSVPR HLMGAGHPMI FALCAAMGCD
LFDSAAYILY AEDDRLLSTR GTYRLEDLNE MPCSCEVCSK YTPDELRALP KEERVKLIAQ
HNLNVSFAEL RTVRQAIYDG TLMELVEERC RVHPALLNAL RELGNYTDDL EVYDPRSKKS
AFFYTGPESL KRPEIKRHLN KIRKMPKKSN LILLPPTRKP YSKNISGKLG RFYVYDKEED
IDLDDCDFMV LDVPFGLIPL DIDEVYPLSQ NESPKIKDTD AINFIKDCLN EFSKYYNSVL
IHQSLANHYG LEFDKIHHQS DDIRYHKDDI RKIKAIADYQ FGEGAGEALF DGKVKFEKSK
KTGKIRHVSV NGKMVANMRA SDAFLILTKE GARRLHSATE YPNNRVVVNE DSEPFTRDGK
SVFCQFVVEC DENIRANDEV LLVNKDDDLL GIGKALLNPN EIKSFNKGQA IKTRKGFKN
//
