ATGT_KORCO
ID ATGT_KORCO Reviewed; 590 AA.
AC B1L6M8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=tRNA-guanine(15) transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
DE EC=2.4.2.48 {ECO:0000255|HAMAP-Rule:MF_01634};
DE AltName: Full=7-cyano-7-deazaguanine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01634};
DE AltName: Full=Archaeal tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634};
GN Name=tgtA {ECO:0000255|HAMAP-Rule:MF_01634}; OrderedLocusNames=Kcr_1361;
OS Korarchaeum cryptofilum (strain OPF8).
OC Archaea; Candidatus Korarchaeota; Candidatus Korarchaeum.
OX NCBI_TaxID=374847;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF8;
RX PubMed=18535141; DOI=10.1073/pnas.0801980105;
RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L.,
RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A.,
RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G.,
RA Richardson P., Keller M., Stetter K.O.;
RT "A korarchaeal genome reveals new insights into the evolution of the
RT Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_01634};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01634};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01634};
CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01634}.
CC -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01634}.
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DR EMBL; CP000968; ACB08107.1; -; Genomic_DNA.
DR RefSeq; WP_012310004.1; NC_010482.1.
DR AlphaFoldDB; B1L6M8; -.
DR SMR; B1L6M8; -.
DR STRING; 374847.Kcr_1361; -.
DR EnsemblBacteria; ACB08107; ACB08107; Kcr_1361.
DR GeneID; 6094638; -.
DR KEGG; kcr:Kcr_1361; -.
DR eggNOG; arCOG00989; Archaea.
DR HOGENOM; CLU_030083_0_0_2; -.
DR InParanoid; B1L6M8; -.
DR OMA; FPCSCPV; -.
DR OrthoDB; 10236at2157; -.
DR PhylomeDB; B1L6M8; -.
DR UniPathway; UPA00393; -.
DR Proteomes; UP000001686; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0008616; P:queuosine biosynthetic process; IBA:GO_Central.
DR GO; GO:0002099; P:tRNA wobble guanine modification; IBA:GO_Central.
DR Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.10.450.90; -; 1.
DR Gene3D; 3.20.20.105; -; 1.
DR Gene3D; 3.90.1020.10; -; 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 Pfam; PF01472; PUA; 1.
DR Pfam; PF01702; TGT; 1.
DR Pfam; PF14810; TGT_C2; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00432; arcsn_tRNA_tgt; 1.
DR TIGRFAMs; TIGR00449; tgt_general; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Metal-binding; Reference proteome; Transferase;
KW tRNA processing; Zinc.
FT CHAIN 1..590
FT /note="tRNA-guanine(15) transglycosylase"
FT /id="PRO_1000215800"
FT DOMAIN 502..577
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT ACT_SITE 90
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01634"
SQ SEQUENCE 590 AA; 67149 MW; 079DD75D622447CC CRC64;
MGLYFRVRKS DASARLSELK TKSGTLILPE FFPVYNPNKP VITPREMSEM GIKAIITNSY
LIYRSPELRE AAIERGIHSL LGFDGVVMTD SGAYQIYRYG RVDVTNSEIL RFQHSIGSDI
GSILDVPMSS EIGREEAESG VERTIRNAEE WASMREELSN TLWVGTPQGS IYRDLVIKCS
ERIRELDFDY NGVGSIKVAL EKYDFVTQVD HFMSIRSILR AGKPFHFWGI GHPSTFAFFA
AIGADSFDSA SYSLYAEQGR YMTPHGTLLL DEIEEFPCSC PVCSSHDPKE VKAMSKEERT
KLLAKHNLYI SISEIKKVRE AIRGEWLWEL VQERSRFHPN LYFALMHLLR RYSSLLEARE
PLFKSSGLQC SGPESFLRPE VVRARNRLKY IHYNGKFRRV LYGDVPLGLK YLYPFGQTIC
PYDEEVQDEP EDDEIITCVL SYQYEFPFPK LPAIMRRSKS TGTLREVSLE GKVIGHFRPN
DGAFIPTLDG ASLILSHLPY PKGRVVVKGL FSDTVARGTT VFVKFVKEAD PSIRPKSEVI
VVNESDELLA TGKAVLSGVE YHQYHPDHPF IIIRRHVKPR SEEKPPEVDS
