Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Tyrosine--tRNA ligase, mitochondrial (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS)

 SYYM_NEUCR              Reviewed;         669 AA.
P12063; Q7RVM4;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
18-JUL-2018, entry version 155.
RecName: Full=Tyrosine--tRNA ligase, mitochondrial;
EC=6.1.1.1;
AltName: Full=Tyrosyl-tRNA synthetase;
Short=TyrRS;
Flags: Precursor;
Name=cyt-18; ORFNames=B18P24.070, NCU03030;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3607872; DOI=10.1016/0092-8674(87)90488-0;
Akins R.A., Lambowitz A.M.;
"A protein required for splicing group I introns in Neurospora
mitochondria is mitochondrial tyrosyl-tRNA synthetase or a derivative
thereof.";
Cell 50:331-345(1987).
[2]
SEQUENCE REVISION.
Lambowitz A.M.;
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12655011; DOI=10.1093/nar/gkg293;
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
Schulte U.;
"What's in the genome of a filamentous fungus? Analysis of the
Neurospora genome sequence.";
Nucleic Acids Res. 31:1944-1954(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[5]
FUNCTION.
PubMed=2143700; DOI=10.1016/0092-8674(90)90119-Y;
Cherniack A.D., Garriga G., Kittle J.D. Jr., Akins R.A.,
Lambowitz A.M.;
"Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA
splicing requires an idiosyncratic domain not found in other
synthetases.";
Cell 62:745-755(1990).
-!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a
two-step reaction: tyrosine is first activated by ATP to form Tyr-
AMP and then transferred to the acceptor end of tRNA(Tyr). Has
both an aminoacyl-tRNA synthetase activity and is involved in the
splicing of group I introns. It acts in intron splicing by
stabilizing the catalytically active structure of the intron.
{ECO:0000269|PubMed:2143700}.
-!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP +
diphosphate + L-tyrosyl-tRNA(Tyr).
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15678762, EBI-15678762;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M17118; AAA33620.1; -; Genomic_DNA.
EMBL; BX842626; CAE76265.1; -; Genomic_DNA.
EMBL; CM002236; EAA36180.1; -; Genomic_DNA.
PIR; A27158; SYNCYT.
RefSeq; XP_965416.1; XM_960323.2.
PDB; 1Y42; X-ray; 1.95 A; X=33-423.
PDB; 2RKJ; X-ray; 4.50 A; A/B/E/F/I/J/M/N=33-423.
PDB; 4OJM; X-ray; 1.95 A; X=33-423.
PDBsum; 1Y42; -.
PDBsum; 2RKJ; -.
PDBsum; 4OJM; -.
ProteinModelPortal; P12063; -.
SMR; P12063; -.
DIP; DIP-59835N; -.
MoonDB; P12063; Curated.
MoonProt; P12063; -.
PRIDE; P12063; -.
EnsemblFungi; EAA36180; EAA36180; NCU03030.
GeneID; 3881566; -.
KEGG; ncr:NCU03030; -.
EuPathDB; FungiDB:NCU03030; -.
HOGENOM; HOG000242790; -.
InParanoid; P12063; -.
KO; K01866; -.
OMA; MHMQLKK; -.
OrthoDB; EOG092C2LDP; -.
BRENDA; 6.1.1.1; 3627.
EvolutionaryTrace; P12063; -.
Proteomes; UP000001805; Chromosome 1, Linkage Group I.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0003723; F:RNA binding; IDA:CAFA.
GO; GO:0004831; F:tyrosine-tRNA ligase activity; IBA:GO_Central.
GO; GO:0000372; P:Group I intron splicing; IDA:CAFA.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0033120; P:positive regulation of RNA splicing; IDA:CAFA.
GO; GO:0034337; P:RNA folding; IDA:CAFA.
GO; GO:0043039; P:tRNA aminoacylation; IBA:GO_Central.
GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro.
CDD; cd00805; TyrRS_core; 1.
Gene3D; 3.10.290.10; -; 1.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR001412; aa-tRNA-synth_I_CS.
InterPro; IPR002305; aa-tRNA-synth_Ic.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR036986; S4_RNA-bd_sf.
InterPro; IPR002307; Tyr-tRNA-ligase.
InterPro; IPR024088; Tyr-tRNA-ligase_bac-type.
InterPro; IPR032005; TyrRSs_C.
PANTHER; PTHR11766; PTHR11766; 1.
Pfam; PF00579; tRNA-synt_1b; 1.
Pfam; PF16714; TyrRSs_C; 1.
PRINTS; PR01040; TRNASYNTHTYR.
TIGRFAMs; TIGR00234; tyrS; 1.
PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
1: Evidence at protein level;
3D-structure; Aminoacyl-tRNA synthetase; ATP-binding;
Complete proteome; Ligase; Mitochondrion; mRNA processing;
Nucleotide-binding; Protein biosynthesis; Reference proteome;
Transit peptide.
TRANSIT 1 32 Mitochondrion.
CHAIN 33 669 Tyrosine--tRNA ligase, mitochondrial.
/FTId=PRO_0000035833.
REGION 33 75 Involved in splicing. {ECO:0000305}.
MOTIF 104 113 "HIGH" region.
MOTIF 324 328 "KMSKS" region.
BINDING 99 99 Tyrosine. {ECO:0000250|UniProtKB:Q9Y2Z4}.
BINDING 103 103 ATP. {ECO:0000250|UniProtKB:Q9Y2Z4}.
BINDING 143 143 Tyrosine. {ECO:0000250|UniProtKB:Q9Y2Z4}.
BINDING 247 247 Tyrosine. {ECO:0000250|UniProtKB:Q9Y2Z4}.
BINDING 251 251 Tyrosine. {ECO:0000250|UniProtKB:Q9Y2Z4}.
BINDING 254 254 Tyrosine. {ECO:0000250|UniProtKB:Q9Y2Z4}.
BINDING 273 273 Tyrosine. {ECO:0000250|UniProtKB:Q9Y2Z4}.
BINDING 327 327 ATP. {ECO:0000250}.
MUTAGEN 127 127 G->E: Splicing and aminoacylation defects
(mutants C-18-1 and C-18-2).
HELIX 40 60 {ECO:0000244|PDB:1Y42}.
HELIX 67 74 {ECO:0000244|PDB:1Y42}.
STRAND 80 82 {ECO:0000244|PDB:1Y42}.
HELIX 84 93 {ECO:0000244|PDB:1Y42}.
STRAND 97 102 {ECO:0000244|PDB:1Y42}.
STRAND 106 108 {ECO:0000244|PDB:1Y42}.
HELIX 111 113 {ECO:0000244|PDB:1Y42}.
HELIX 114 126 {ECO:0000244|PDB:1Y42}.
STRAND 129 134 {ECO:0000244|PDB:1Y42}.
TURN 136 141 {ECO:0000244|PDB:1Y42}.
HELIX 159 183 {ECO:0000244|PDB:1Y42}.
STRAND 193 198 {ECO:0000244|PDB:1Y42}.
HELIX 200 203 {ECO:0000244|PDB:1Y42}.
HELIX 208 215 {ECO:0000244|PDB:1Y42}.
TURN 216 218 {ECO:0000244|PDB:1Y42}.
HELIX 221 225 {ECO:0000244|PDB:1Y42}.
HELIX 228 232 {ECO:0000244|PDB:1Y42}.
STRAND 235 238 {ECO:0000244|PDB:1Y42}.
HELIX 242 262 {ECO:0000244|PDB:1Y42}.
STRAND 264 269 {ECO:0000244|PDB:1Y42}.
HELIX 274 290 {ECO:0000244|PDB:1Y42}.
HELIX 294 300 {ECO:0000244|PDB:1Y42}.
HELIX 305 307 {ECO:0000244|PDB:1Y42}.
STRAND 310 313 {ECO:0000244|PDB:1Y42}.
STRAND 329 332 {ECO:0000244|PDB:1Y42}.
STRAND 334 336 {ECO:0000244|PDB:1Y42}.
TURN 337 339 {ECO:0000244|PDB:1Y42}.
HELIX 342 350 {ECO:0000244|PDB:1Y42}.
TURN 354 356 {ECO:0000244|PDB:1Y42}.
HELIX 357 364 {ECO:0000244|PDB:1Y42}.
HELIX 369 381 {ECO:0000244|PDB:1Y42}.
HELIX 383 385 {ECO:0000244|PDB:1Y42}.
HELIX 387 401 {ECO:0000244|PDB:1Y42}.
HELIX 403 413 {ECO:0000244|PDB:1Y42}.
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


Related products :

Catalog number Product name Quantity
EIAAB40951 Rat,Rattus norvegicus,Tyrosine--tRNA ligase,Tyrosyl-tRNA synthetase, mitochondrial,TyrRS,Yars2
EIAAB40952 Mouse,Mus musculus,Tyrosine--tRNA ligase,Tyrosyl-tRNA synthetase, mitochondrial,TyrRS,Yars2
EIAAB40950 CGI-04,Homo sapiens,Human,Tyrosine--tRNA ligase,Tyrosyl-tRNA synthetase, mitochondrial,TyrRS,YARS2
EIAAB40949 Homo sapiens,Human,Tyrosyl--tRNA ligase,Tyrosyl-tRNA synthetase, cytoplasmic,TyrRS,YARS
EIAAB40945 Bos taurus,Bovine,Tyrosyl--tRNA ligase,Tyrosyl-tRNA synthetase, cytoplasmic,TyrRS,TYRS,YARS
EIAAB40947 Rat,Rattus norvegicus,Tyrosyl--tRNA ligase,Tyrosyl-tRNA synthetase, cytoplasmic,TyrRS,Yars
EIAAB40948 Mouse,Mus musculus,Tyrosyl--tRNA ligase,Tyrosyl-tRNA synthetase, cytoplasmic,TyrRS,Yars
18-003-44187 Tyrosyl-tRNA synthetase. cytoplasmic - EC 6.1.1.1; Tyrosyl--tRNA ligase; TyrRS Polyclonal 0.1 mg Protein A
EIAAB40946 Chicken,Gallus gallus,RCJMB04_21p3,Tyrosyl--tRNA ligase,Tyrosyl-tRNA synthetase, cytoplasmic,TyrRS,YARS
20-372-60005 tyrosyl-tRNA synthetase (YARS) - Mouse monoclonal anti-human YARS antibody; EC 6.1.1.1; Tyrosyl--tRNA ligase; TyrRS Monoclonal 0.1 mg
EIAAB40771 Homo sapiens,Human,MARS2,Methionine--tRNA ligase 2,Methionyl-tRNA synthetase, mitochondrial,Mitochondrial methionine--tRNA ligase,MtMetRS
EIAAB40769 Mars2,Methionine--tRNA ligase 2,Methionyl-tRNA synthetase, mitochondrial,Mitochondrial methionine--tRNA ligase,Mouse,MtMetRS,Mus musculus
EIAAB40770 Bos taurus,Bovine,MARS2,Methionine--tRNA ligase 2,Methionyl-tRNA synthetase, mitochondrial,Mitochondrial methionine--tRNA ligase,MtMetRS
EIAAB40853 Homo sapiens,Human,SARS2,SARSM,Serine--tRNA ligase,SerRS,SerRSmt,Seryl-tRNA synthetase, mitochondrial,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40938 Homo sapiens,Human,KIAA1885,Valine--tRNA ligase,ValRS,Valyl-tRNA synthetase, mitochondrial,Valyl-tRNA synthetase-like,VARS2,VARS2L,VARSL
EIAAB40855 Bos taurus,Bovine,SARS2,SARSM,Serine--tRNA ligase,SerRS,SerRSmt,Seryl-tRNA synthetase, mitochondrial,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40844 Arginine--tRNA ligase,Arginyl-tRNA synthetase-like,ArgRS,Homo sapiens,Human,Probable arginyl-tRNA synthetase, mitochondrial,RARS2,RARSL
EIAAB40854 Mouse,Mus musculus,Sars2,Sarsm,Serine--tRNA ligase,SerRS,SerRSmt,Seryl-tRNA synthetase, mitochondrial,Seryl-tRNA(Ser_Sec) synthetase
EIAAB40750 HARS2,HARSL,HARSR,HisRS,Histidine--tRNA ligase,Histidine--tRNA ligase-like,HO3,Homo sapiens,Human,Probable histidyl-tRNA synthetase, mitochondrial
EIAAB40842 Arginine--tRNA ligase,Arginyl-tRNA synthetase-like,ArgRS,Mouse,Mus musculus,Probable arginyl-tRNA synthetase, mitochondrial,Rars2,Rarsl
EIAAB40843 Arginine--tRNA ligase,Arginyl-tRNA synthetase-like,ArgRS,Bos taurus,Bovine,Probable arginyl-tRNA synthetase, mitochondrial,RARS2,RARSL
EIAAB40928 Homo sapiens,Human,TARS2,TARSL1,Threonine--tRNA ligase,Threonyl-tRNA synthetase, mitochondrial,Threonyl-tRNA synthetase-like 1,ThrRS
EIAAB40751 Hars2,Harsl,HisRS,Histidine--tRNA ligase,Histidine--tRNA ligase-like,Mouse,Mus musculus,Probable histidyl-tRNA synthetase, mitochondrial
EIAAB40927 Rat,Rattus norvegicus,Tars2,Tarsl1,Threonine--tRNA ligase,Threonyl-tRNA synthetase, mitochondrial,Threonyl-tRNA synthetase-like 1,ThrRS
EIAAB40926 Mouse,Mus musculus,Tars2,Tarsl1,Threonine--tRNA ligase,Threonyl-tRNA synthetase, mitochondrial,Threonyl-tRNA synthetase-like 1,ThrRS


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur