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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
 
 
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