TILS_SCHPO
ID TILS_SCHPO Reviewed; 456 AA.
AC Q10441;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable tRNA(Ile)-lysidine synthase;
DE EC=6.3.4.19;
DE AltName: Full=tRNA(Ile)-2-lysyl-cytidine synthase;
DE AltName: Full=tRNA(Ile)-lysidine synthetase;
GN ORFNames=SPAC12B10.08c;
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: Ligates lysine onto the cytidine present at position 34 of
CC the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an
CC ATP-dependent manner. Cytidine is converted to lysidine, thus changing
CC the amino acid specificity of the tRNA from methionine to isoleucine
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP +
CC diphosphate + H(+) + lysidine(34) in tRNA(Ile2);
CC Xref=Rhea:RHEA:43744, Rhea:RHEA-COMP:10625, Rhea:RHEA-COMP:10670,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:82748, ChEBI:CHEBI:83665,
CC ChEBI:CHEBI:456215; EC=6.3.4.19;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The N-terminal region contains the highly conserved SGGXDS
CC motif, predicted to be a P-loop motif involved in ATP binding.
CC -!- SIMILARITY: Belongs to the tRNA(Ile)-lysidine synthase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA94698.1; -; Genomic_DNA.
DR PIR; T37575; T37575.
DR RefSeq; NP_594640.1; NM_001020068.2.
DR AlphaFoldDB; Q10441; -.
DR SMR; Q10441; -.
DR STRING; 4896.SPAC12B10.08c.1; -.
DR SwissPalm; Q10441; -.
DR PaxDb; Q10441; -.
DR EnsemblFungi; SPAC12B10.08c.1; SPAC12B10.08c.1:pep; SPAC12B10.08c.
DR GeneID; 2543003; -.
DR KEGG; spo:SPAC12B10.08c; -.
DR PomBase; SPAC12B10.08c; -.
DR VEuPathDB; FungiDB:SPAC12B10.08c; -.
DR eggNOG; ENOG502QQNE; Eukaryota.
DR HOGENOM; CLU_015599_1_0_1; -.
DR InParanoid; Q10441; -.
DR OMA; YSTLKHY; -.
DR PhylomeDB; Q10441; -.
DR PRO; PR:Q10441; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:InterPro.
DR GO; GO:0032543; P:mitochondrial translation; IC:PomBase.
DR GO; GO:0002127; P:tRNA wobble base cytosine methylation; IC:PomBase.
DR CDD; cd01992; PP-ATPase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_01161; tRNA_Ile_lys_synt; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR011063; TilS/TtcA_N.
DR InterPro; IPR012094; tRNA_Ile_lys_synt.
DR InterPro; IPR012795; tRNA_Ile_lys_synt_N.
DR PANTHER; PTHR43033; PTHR43033; 1.
DR Pfam; PF01171; ATP_bind_3; 1.
DR TIGRFAMs; TIGR02432; lysidine_TilS_N; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Reference proteome;
KW tRNA processing.
FT CHAIN 1..456
FT /note="Probable tRNA(Ile)-lysidine synthase"
FT /id="PRO_0000181822"
FT BINDING 30..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 456 AA; 52362 MW; 24B18EB8DF1441E0 CRC64;
MDTIKLKEFY NSLVSIRRRV GHRRLGIAVS GGVDSMLLSW FMKESQIMFG WPNQFIAFVV
DHRIRKNSTE EALQTIWNLN RMLIPNVYLN INWGNDDVHS LTNLETIARE HRYQVLTRAC
ITHNIRHICT AHHANDQAET IFMRLLRRKP GTWGGLCAMK PVSQIPESDS ICGASNIELL
RPLLPYYKNQ ILNTAKQHGI AWEEDPTNAD INLTPRNAIR RFLNQHAALT VEATKLATAF
QSLQVNIDNK VDEILKDNIV SYHQPSGTLS LCFSKNELKK HSNLTKEELL LRCLTLTTSC
RQIKRSSVVS LCNSVFDGKK LTIAKCLLTS SSIKDDTKLQ LQISRQPFSK AELKKKTITI
NPDRYVLWDH RFWIKYSCKN TQTTLILRPL LSKDLNSLKG FLSKEEFLKF CIQVPGHIRF
TIPVLSEEND KLVGIPTFGF NFRSDIISNC LHKFKL
