MOD5_SCHPO
ID MOD5_SCHPO Reviewed; 434 AA.
AC Q9UT75;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=tRNA dimethylallyltransferase;
DE EC=2.5.1.75;
DE AltName: Full=Isopentenyl-diphosphate: tRNA isopentenyltransferase;
DE Short=IPP transferase;
DE Short=IPPT;
DE AltName: Full=tRNA isopentenyltransferase;
DE Short=IPTase;
GN Name=tit1; Synonyms=mod5; ORFNames=SPAC343.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the
CC adenine at position 37 of both cytosolic and mitochondrial tRNAs,
CC leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB52278.1; -; Genomic_DNA.
DR PIR; T38664; T38664.
DR RefSeq; NP_593436.1; NM_001018869.2.
DR AlphaFoldDB; Q9UT75; -.
DR SMR; Q9UT75; -.
DR BioGRID; 279498; 3.
DR STRING; 4896.SPAC343.15.1; -.
DR MaxQB; Q9UT75; -.
DR PaxDb; Q9UT75; -.
DR EnsemblFungi; SPAC343.15.1; SPAC343.15.1:pep; SPAC343.15.
DR GeneID; 2543065; -.
DR KEGG; spo:SPAC343.15; -.
DR PomBase; SPAC343.15; tit1.
DR VEuPathDB; FungiDB:SPAC343.15; -.
DR eggNOG; KOG1384; Eukaryota.
DR HOGENOM; CLU_032616_2_3_1; -.
DR InParanoid; Q9UT75; -.
DR OMA; YAKRQYT; -.
DR PhylomeDB; Q9UT75; -.
DR BRENDA; 2.5.1.75; 5613.
DR PRO; PR:Q9UT75; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0005730; C:nucleolus; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; ISO:PomBase.
DR GO; GO:0006400; P:tRNA modification; ISO:PomBase.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00185; IPP_trans; 1.
DR InterPro; IPR039657; Dimethylallyltransferase.
DR InterPro; IPR018022; IPT.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11088; PTHR11088; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00174; miaA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Nucleus; Reference proteome; Transferase; tRNA processing; Zinc;
KW Zinc-finger.
FT CHAIN 1..434
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_0000316242"
FT ZN_FING 380..416
FT /note="Matrin-type"
FT REGION 35..38
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 166..170
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 211..233
FT /note="Interaction with isopentenylpyrophosphate
FT transferase"
FT /evidence="ECO:0000250"
FT REGION 256..258
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 281..299
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT REGION 291..298
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 12..17
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 101
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
FT SITE 189
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 434 AA; 50121 MW; FCFD5101DF95F34D CRC64;
MLKPLCVVIG TTGAGKSDLA VQLAKRFGSQ VINADSMQIY RGFDTITNKI TVEEQENVHH
RLMSFLNFDK EYSVPEFERD ASRVIDEIHS QGKIPIVVGG THYYLQSLLF EDTTLSAIDK
LTNDSSPSKP PHPDSHILDD DPSAMLSYLK KIDPVMAEQW HPRDTRKIRR SLEIYFHTGR
PPSEIYSEQK MKSSGSKLRY KSLIFWAFAD SLVLMPRLDK RVDKMLSHGL VDEIKSMKSL
AESEKFSPDF TRGIWQCIGF KEFMPWFEAP SDIVFNDCLE RMKVSTRQYA KSQKKWIQSR
FLPMCLAQQD LSPSSILFST TNTTDLNNWE EQVEKACRVF QYFFYNGDAI APSADDQHAF
EKARDYLSIM NGRQSQKKKF VCEECLDKRG DPFTVIGEDA FNVHIKSRKH KTTVRRKKER
AERQIRLKNI GILK