(data stored in SCRATCH zone)

SWISSPROT: Q4W9P0_ASPFU

ID   Q4W9P0_ASPFU            Unreviewed;       385 AA.
AC   Q4W9P0;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=Queuine tRNA-ribosyltransferase {ECO:0000256|RuleBase:RU003777};
DE            EC=2.4.2.29 {ECO:0000256|RuleBase:RU003777};
GN   ORFNames=AFUA_4G04260 {ECO:0000313|EMBL:EAL84573.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL84573.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL84573.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Catalyzes the base-exchange of a guanine (G) residue with the
CC       queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34
CC       (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -
CC       Asn, -His and -Tyr). Catalysis occurs through a double-displacement
CC       mechanism. The nucleophile active site attacks the C1' of nucleotide 34
CC       to detach the guanine base from the RNA, forming a covalent enzyme-RNA
CC       intermediate. The proton acceptor active site deprotonates the incoming
CC       PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form
CC       the product. After dissociation, two additional enzymatic reactions on
CC       the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified
CC       nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-
CC       yl)amino)methyl)-7-deazaguanosine). {ECO:0000256|RuleBase:RU003777}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7-
CC         aminomethyl-7-carbaguanosine(34) in tRNA + guanine;
CC         Xref=Rhea:RHEA:24104, Rhea:RHEA-COMP:10341, Rhea:RHEA-COMP:10342,
CC         ChEBI:CHEBI:16235, ChEBI:CHEBI:58703, ChEBI:CHEBI:74269,
CC         ChEBI:CHEBI:82833; EC=2.4.2.29;
CC         Evidence={ECO:0000256|RuleBase:RU003777};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003777};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003777};
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC       {ECO:0000256|RuleBase:RU003777}.
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:EAL84573.1}.
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DR   EMBL; AAHF01000016; EAL84573.1; -; Genomic_DNA.
DR   RefSeq; XP_746611.1; XM_741518.1.
DR   STRING; 746128.CADAFUBP00009597; -.
DR   EnsemblFungi; EAL84573; EAL84573; AFUA_4G04260.
DR   GeneID; 3504007; -.
DR   KEGG; afm:AFUA_4G04260; -.
DR   EuPathDB; FungiDB:Afu4g04260; -.
DR   HOGENOM; HOG000223473; -.
DR   InParanoid; Q4W9P0; -.
DR   KO; K00773; -.
DR   OMA; GIDLFDC; -.
DR   OrthoDB; 684306at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:InterPro.
DR   Gene3D; 3.20.20.105; -; 1.
DR   InterPro; IPR004803; TGT.
DR   InterPro; IPR036511; TGT-like_sf.
DR   InterPro; IPR002616; tRNA_ribo_trans-like.
DR   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4W9P0.
DR   SWISS-2DPAGE; Q4W9P0.
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU003777,
KW   ECO:0000313|EMBL:EAL84573.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|RuleBase:RU003777, ECO:0000313|EMBL:EAL84573.1};
KW   tRNA processing {ECO:0000256|RuleBase:RU003777};
KW   Zinc {ECO:0000256|RuleBase:RU003777}.
FT   DOMAIN          1..360
FT                   /note="TGT"
FT                   /evidence="ECO:0000259|Pfam:PF01702"
SQ   SEQUENCE   385 AA;  42442 MW;  0AC0F01FDA5AAFFB CRC64;
     MPVATQASLK GLTYDQLKQT GCMLCLNNTY HLGLKPGQEV LDQVGGAHKL QGWDRNILTD
     SGGFQMVSLL KLAKVTEEGV RFLSPHDGTP MLLTPEHSIS LQNSIGSDII MQLDDVIATT
     SPDHARIHEA MERSVRWLDR CIDAHKYPER QNLFCIIQGG LDLELRKQCC AEMVARDTPG
     IAIGGLSGGE AKEEFCKVVD TCTGLLPEHK PRYVMGVVST RWPIRLAVSF IDAAQGYPED
     LVVAVALGAD MFDCVWPTRT ARFGNAVVPS GNLNLRHKSF AEDFRPIQEG CSCSCCRPRD
     QGGLGITRAY LHHLAAKETV GAHLLTIHNV HYLLNLMGSA RQAILEDRYP AFLREFFDNL
     YGDKAKFPEW AVTALRGVGV DLLAD
//

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