(data stored in ACNUC7421 zone)

SWISSPROT: Q4WDK6_ASPFU

ID   Q4WDK6_ASPFU            Unreviewed;       488 AA.
AC   Q4WDK6;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 109.
DE   RecName: Full=tRNA dimethylallyltransferase {ECO:0000256|PIRNR:PIRNR039110, ECO:0000256|RuleBase:RU003783};
DE            EC=2.5.1.75 {ECO:0000256|PIRNR:PIRNR039110, ECO:0000256|RuleBase:RU003783};
GN   ORFNames=AFUA_6G05070 {ECO:0000313|EMBL:EAL85532.1};
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:EAL85532.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85532.1, 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 transfer of a dimethylallyl group onto the
CC       adenine at position 37. {ECO:0000256|PIRNR:PIRNR039110}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate =
CC         diphosphate + N(6)-dimethylallyladenosine(37) in tRNA;
CC         Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411,
CC         ChEBI:CHEBI:74415; EC=2.5.1.75;
CC         Evidence={ECO:0000256|PIRNR:PIRNR039110,
CC         ECO:0000256|RuleBase:RU003783};
CC   -!- SIMILARITY: Belongs to the IPP transferase family.
CC       {ECO:0000256|PIRNR:PIRNR039110, ECO:0000256|RuleBase:RU003785}.
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:EAL85532.1}.
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DR   EMBL; AAHF01000012; EAL85532.1; -; Genomic_DNA.
DR   RefSeq; XP_747570.1; XM_742477.1.
DR   STRING; 746128.CADAFUBP00009058; -.
DR   EnsemblFungi; EAL85532; EAL85532; AFUA_6G05070.
DR   GeneID; 3505337; -.
DR   KEGG; afm:AFUA_6G05070; -.
DR   EuPathDB; FungiDB:Afu6g05070; -.
DR   HOGENOM; HOG000039995; -.
DR   InParanoid; Q4WDK6; -.
DR   KO; K00791; -.
DR   OMA; PFTVTHF; -.
DR   OrthoDB; 1003231at2759; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR   HAMAP; MF_00185; IPP_trans; 1.
DR   InterPro; IPR039657; Dimethylallyltransferase.
DR   InterPro; IPR030666; IPP_transferase_euk.
DR   InterPro; IPR018022; IPT.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR11088; PTHR11088; 1.
DR   Pfam; PF01715; IPPT; 1.
DR   PIRSF; PIRSF039110; IPP_transferase; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   TIGRFAMs; TIGR00174; miaA; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WDK6.
DR   SWISS-2DPAGE; Q4WDK6.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR039110, ECO:0000256|RuleBase:RU003785};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR039110};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR039110,
KW   ECO:0000256|RuleBase:RU003785};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|PIRNR:PIRNR039110, ECO:0000256|RuleBase:RU003785,
KW   ECO:0000313|EMBL:EAL85532.1};
KW   tRNA processing {ECO:0000256|PIRNR:PIRNR039110,
KW   ECO:0000256|RuleBase:RU003783}.
FT   DOMAIN          424..446
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   REGION          464..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..481
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  55773 MW;  A1BF653B64D550F7 CRC64;
     MLNFLRSFWR IKRPSTMEPL IAVVGATGTG KSKLAVDLAT RFNGEIINGD AMQMYRGLPI
     ITNQIPFEER NGIPHHLISC VDFEEEPWRI GHFKRECLRL IKDIHSRGKL PILVGGTHYY
     TQTVLFKDQL VEESLFSGDD DDAHFHKETK PTSAKWPILD APPDVVFQKL KEVDPVIASR
     WHPNDVRKIR RSLEIYFQTG KPASEIYAEQ KRQKYATGTN GESSPGIGQL RYPTLIFWVH
     SEKETLNCRL AKRVDSMVEQ GLMAEAQRMW AYIREKKGQG ITVDQTRGVW VSIGFKELAP
     YFDALENGEL SEGELEALKQ SSIELVKIAT RQYATSQIKW IRNKLWKALA DAGATKNLYL
     LDSTNVEDWQ RWVTEPSEHL TQALLNDEPR PDPKSLSDMA RETLCAREVQ AQTQRSDVLQ
     TFTCEICSRT MATQDQWNIH LNGRAHKRAI KNAAKRAERE KYLRNQQTLG VGQNCDNPTP
     TEQPSTPQ
//

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