ID A0A1B8FLQ9_9PEZI Unreviewed; 485 AA.
AC A0A1B8FLQ9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Queuine tRNA-ribosyltransferase accessory subunit 2 {ECO:0000256|HAMAP-Rule:MF_03043};
DE AltName: Full=Queuine tRNA-ribosyltransferase domain-containing protein 1 {ECO:0000256|HAMAP-Rule:MF_03043};
GN ORFNames=VE02_06437 {ECO:0000313|EMBL:OBT84453.1};
OS Pseudogymnoascus sp. 03VT05.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622148 {ECO:0000313|EMBL:OBT84453.1};
RN [1] {ECO:0000313|EMBL:OBT84453.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03VT05 {ECO:0000313|EMBL:OBT84453.1};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-catalytic subunit of the queuine tRNA-ribosyltransferase
CC (TGT) that catalyzes the base-exchange of a guanine (G) residue with
CC queuine (Q) at position 34 (anticodon wobble position) in tRNAs with
CC GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the
CC hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000256|HAMAP-
CC Rule:MF_03043}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03043};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03043};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit and an accessory subunit.
CC {ECO:0000256|HAMAP-Rule:MF_03043}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03043}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC QTRT2 subfamily. {ECO:0000256|HAMAP-Rule:MF_03043}.
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DR EMBL; KV459475; OBT84453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8FLQ9; -.
DR Proteomes; UP000091872; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008479; F:tRNA-guanosine(34) queuine transglycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 1.
DR HAMAP; MF_03043; QTRT2; 1.
DR InterPro; IPR028592; QTRTD1.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR PANTHER; PTHR46064; QUEUINE TRNA-RIBOSYLTRANSFERASE ACCESSORY SUBUNIT 2; 1.
DR PANTHER; PTHR46064:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE ACCESSORY SUBUNIT 2; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03043};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03043};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_03043};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_03043}.
FT DOMAIN 28..414
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT REGION 420..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
SQ SEQUENCE 485 AA; 52621 MW; BEF3244602EBA76E CRC64;
MAGGAFDQPF FTLHDETSID AAPSDPRGAR LGRISVKGRR TLDTPNFLAI TSRGVVPHIS
PDVLGEQTEF AGVYTAIEDY VEKATRGGVP PIMGMPARNS TPLHSFTALP PSLITVLSPR
RSPAVSSPQG NPDSGLSIFT STGFQSLSTQ RYAEYANYIK PDITIALGDL PYGPMPGKKR
ASKMSERTTI WVDKFLSELS KSPESPDAPA TATAVFAPIL TRDYQSQFEY IEHISEDLAP
SLSGLAFYSS SLLPDIPQTP SLNRLVRLSL DEPSSPHEIL RQVSLGMDVF TIPYLTFATD
SGLALTYEFP RPAAPDSSNP SVEGASLLPL AIDLFSTAYS TAVTPLIPSC TCYACTSHHR
AYIQHLLCAK EMLAWTLLAL HNHHSTSTFF ANVRKSIAAG TFEADKEVFE RTYETELPEA
TGHKPRARGY HFKSGAAEPK RNKPAWGALS EGVGATTQTP PLMPDEDART LDEKGFAEDL
ADRPE
//
