SYYM_NEUCR
ID SYYM_NEUCR Reviewed; 669 AA.
AC P12063; Q7RVM4;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Tyrosine--tRNA ligase, mitochondrial;
DE EC=6.1.1.1;
DE AltName: Full=Tyrosyl-tRNA synthetase;
DE Short=TyrRS;
DE Flags: Precursor;
GN Name=cyt-18; ORFNames=B18P24.070, NCU03030;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3607872; DOI=10.1016/0092-8674(87)90488-0;
RA Akins R.A., Lambowitz A.M.;
RT "A protein required for splicing group I introns in Neurospora mitochondria
RT is mitochondrial tyrosyl-tRNA synthetase or a derivative thereof.";
RL Cell 50:331-345(1987).
RN [2]
RP SEQUENCE REVISION.
RA Lambowitz A.M.;
RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [5]
RP FUNCTION.
RX PubMed=2143700; DOI=10.1016/0092-8674(90)90119-y;
RA Cherniack A.D., Garriga G., Kittle J.D. Jr., Akins R.A., Lambowitz A.M.;
RT "Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA
RT splicing requires an idiosyncratic domain not found in other synthetases.";
RL Cell 62:745-755(1990).
CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-
CC step reaction: tyrosine is first activated by ATP to form Tyr-AMP and
CC then transferred to the acceptor end of tRNA(Tyr). Has both an
CC aminoacyl-tRNA synthetase activity and is involved in the splicing of
CC group I introns. It acts in intron splicing by stabilizing the
CC catalytically active structure of the intron.
CC {ECO:0000269|PubMed:2143700}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + H(+) + L-
CC tyrosyl-tRNA(Tyr); Xref=Rhea:RHEA:10220, Rhea:RHEA-COMP:9706,
CC Rhea:RHEA-COMP:9707, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58315, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78536, ChEBI:CHEBI:456215; EC=6.1.1.1;
CC -!- INTERACTION:
CC P12063; P12063: cyt-18; NbExp=2; IntAct=EBI-15678762, EBI-15678762;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; M17118; AAA33620.1; -; Genomic_DNA.
DR EMBL; BX842626; CAE76265.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA36180.1; -; Genomic_DNA.
DR PIR; A27158; SYNCYT.
DR RefSeq; XP_965416.1; XM_960323.2.
DR PDB; 1Y42; X-ray; 1.95 A; X=33-423.
DR PDB; 2RKJ; X-ray; 4.50 A; A/B/E/F/I/J/M/N=33-423.
DR PDB; 4OJM; X-ray; 1.95 A; X=33-423.
DR PDBsum; 1Y42; -.
DR PDBsum; 2RKJ; -.
DR PDBsum; 4OJM; -.
DR AlphaFoldDB; P12063; -.
DR SMR; P12063; -.
DR DIP; DIP-59835N; -.
DR STRING; 5141.EFNCRP00000002425; -.
DR MoonDB; P12063; Curated.
DR MoonProt; P12063; -.
DR EnsemblFungi; EAA36180; EAA36180; NCU03030.
DR GeneID; 3881566; -.
DR KEGG; ncr:NCU03030; -.
DR VEuPathDB; FungiDB:NCU03030; -.
DR HOGENOM; CLU_024003_4_0_1; -.
DR InParanoid; P12063; -.
DR OMA; MHMQLKK; -.
DR BRENDA; 6.1.1.1; 3627.
DR EvolutionaryTrace; P12063; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IDA:CAFA.
DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000372; P:Group I intron splicing; IDA:CAFA.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IDA:CAFA.
DR GO; GO:0034337; P:RNA folding; IDA:CAFA.
DR GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central.
DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00805; TyrRS_core; 1.
DR Gene3D; 3.10.290.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002305; aa-tRNA-synth_Ic.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR002307; Tyr-tRNA-ligase.
DR InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
DR InterPro; IPR032005; TyrRSs_C.
DR PANTHER; PTHR11766; PTHR11766; 1.
DR Pfam; PF00579; tRNA-synt_1b; 1.
DR Pfam; PF16714; TyrRSs_C; 1.
DR PRINTS; PR01040; TRNASYNTHTYR.
DR TIGRFAMs; TIGR00234; tyrS; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Mitochondrion; mRNA processing; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..32
FT /note="Mitochondrion"
FT CHAIN 33..669
FT /note="Tyrosine--tRNA ligase, mitochondrial"
FT /id="PRO_0000035833"
FT REGION 33..75
FT /note="Involved in splicing"
FT /evidence="ECO:0000305"
FT REGION 596..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 104..113
FT /note="'HIGH' region"
FT MOTIF 324..328
FT /note="'KMSKS' region"
FT COMPBIAS 596..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 143
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 247
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 251
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 254
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 273
FT /ligand="L-tyrosine"
FT /ligand_id="ChEBI:CHEBI:58315"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2Z4"
FT BINDING 327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 127
FT /note="G->E: Splicing and aminoacylation defects (mutants
FT C-18-1 and C-18-2)."
FT HELIX 40..60
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:1Y42"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:1Y42"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1Y42"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:1Y42"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:1Y42"
FT TURN 136..141
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 159..183
FT /evidence="ECO:0007829|PDB:1Y42"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:1Y42"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:1Y42"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 242..262
FT /evidence="ECO:0007829|PDB:1Y42"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 274..290
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1Y42"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:1Y42"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:1Y42"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:1Y42"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 342..350
FT /evidence="ECO:0007829|PDB:1Y42"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 387..401
FT /evidence="ECO:0007829|PDB:1Y42"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:1Y42"
SQ SEQUENCE 669 AA; 75422 MW; DD136CAC9AD1BEB5 CRC64;
MLLRTKALIR SGGSIAKYAA ANPSCFILQR RGLRREFGPK YTAKINEAEE NWQARAEAIK
KGKKQNTWDL FEERGYVKDT AGTKEHIAEL MRTRRIGAYV GIDPTAPSLH VGHLLPLMPL
FWMYLEGYKA FTLIGGSTAK IGDPTGRLKS RDHLSSSDAT MNMTKIHYQL KKLWENVDTQ
MRARGYEADW ARKRGIVNNN HWWNKQPMLE VLRRVGHALR IGPMLSRDTV KNKMTQGDGV
SFAEFTYPIM QGWDWFELFY QQGVQMQIGG SDQYGNIISG LEVVKAARES EPDPQERKYV
TPKTALDECV GFTVPLLTDS SGAKFGKSAG NAIWLDPYQT SVFDFYGYFV RRSDQEVENL
LKLFTFMPIS EITKTMEEHI KDPSKRVAQH TLAREVVTLV HGKQEASAAE DQHRMMYTGQ
MTIPQVSRAK DAATGGDQYK TISDQPVTLN NAPRIDMILP ESLIMGKSIG RILYAAGLAS
STTEGHKLAA AQGCYVGGAH RAGGENVTMN PDLISFMPVK LWFPGETQRY LINGNLLILR
KGKHNVRVIQ MVSDVEYAAS GQTYPGQSFT GAVRKLNEIM KNLKEKKLTP EEAKNAVNEL
QKSSQEKQQG QQIIFPEEKS RQKKDMETKL KQEMIASVKT IDGMMDEKPS VRGDGVKKQT
QDDRDPYKW
