P12063 (SYYM_NEUCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine--tRNA ligase, mitochondrial
EC=6.1.1.1

Alternative name(s):
Tyrosyl-tRNA synthetase
Short name=TyrRS

Gene names

Name:	cyt-18
ORF Names:	B18P24.070, NCU03030

Organism

Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

Taxonomic identifier

367110 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	669 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5
Catalytic activity	ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis mRNA processing
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW tyrosyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW tyrosine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 32

32

Mitochondrion

Chain

33 – 669

637

Tyrosine--tRNA ligase, mitochondrial

PRO_0000035833

Regions

Region

33 – 75

43

Involved in splicing Probable

Motif

104 – 113

10

"HIGH" region

Motif

324 – 328

5

"KMSKS" region

Sites

Binding site

327

1

ATP By similarity

Experimental info

Mutagenesis

127

1

G → E: Splicing and aminoacylation defects (mutants C-18-1 and C-18-2).

Secondary structure

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669

Helix Strand Turn

Details...

Helix

40 – 60

21

Helix

67 – 74

8

Beta strand

80 – 82

3

Helix

84 – 93

10

Beta strand

97 – 102

6

Beta strand

106 – 108

3

Helix

111 – 113

3

Helix

114 – 126

13

Beta strand

129 – 134

6

Turn

136 – 141

6

Helix

159 – 183

25

Beta strand

193 – 198

6

Helix

200 – 203

4

Helix

208 – 215

8

Turn

216 – 218

3

Helix

221 – 225

5

Helix

228 – 232

5

Beta strand

235 – 238

4

Helix

242 – 262

21

Beta strand

264 – 269

6

Helix

274 – 290

17

Helix

294 – 300

7

Helix

305 – 307

3

Beta strand

310 – 313

4

Beta strand

329 – 332

4

Beta strand

334 – 336

3

Turn

337 – 339

3

Helix

342 – 350

9

Turn

354 – 356

3

Helix

357 – 364

8

Helix

369 – 381

13

Helix

383 – 385

3

Helix

387 – 401

15

Helix

403 – 413

11

Sequences

	Sequence		Length	Mass (Da)
	P12063 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: DD136CAC9AD1BEB5	FASTA	669	75,422
	10 20 30 40 50 60 MLLRTKALIR SGGSIAKYAA ANPSCFILQR RGLRREFGPK YTAKINEAEE NWQARAEAIK 70 80 90 100 110 120 KGKKQNTWDL FEERGYVKDT AGTKEHIAEL MRTRRIGAYV GIDPTAPSLH VGHLLPLMPL 130 140 150 160 170 180 FWMYLEGYKA FTLIGGSTAK IGDPTGRLKS RDHLSSSDAT MNMTKIHYQL KKLWENVDTQ 190 200 210 220 230 240 MRARGYEADW ARKRGIVNNN HWWNKQPMLE VLRRVGHALR IGPMLSRDTV KNKMTQGDGV 250 260 270 280 290 300 SFAEFTYPIM QGWDWFELFY QQGVQMQIGG SDQYGNIISG LEVVKAARES EPDPQERKYV 310 320 330 340 350 360 TPKTALDECV GFTVPLLTDS SGAKFGKSAG NAIWLDPYQT SVFDFYGYFV RRSDQEVENL 370 380 390 400 410 420 LKLFTFMPIS EITKTMEEHI KDPSKRVAQH TLAREVVTLV HGKQEASAAE DQHRMMYTGQ 430 440 450 460 470 480 MTIPQVSRAK DAATGGDQYK TISDQPVTLN NAPRIDMILP ESLIMGKSIG RILYAAGLAS 490 500 510 520 530 540 STTEGHKLAA AQGCYVGGAH RAGGENVTMN PDLISFMPVK LWFPGETQRY LINGNLLILR 550 560 570 580 590 600 KGKHNVRVIQ MVSDVEYAAS GQTYPGQSFT GAVRKLNEIM KNLKEKKLTP EEAKNAVNEL 610 620 630 640 650 660 QKSSQEKQQG QQIIFPEEKS RQKKDMETKL KQEMIASVKT IDGMMDEKPS VRGDGVKKQT QDDRDPYKW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A protein required for splicing group I introns in Neurospora mitochondria is mitochondrial tyrosyl-tRNA synthetase or a derivative thereof." Akins R.A., Lambowitz A.M. Cell 50:331-345(1987) [PubMed: 3607872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Lambowitz A.M. Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence." Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U. Nucleic Acids Res. 31:1944-1954(2003) [PubMed: 12655011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[4]	"The genome sequence of the filamentous fungus Neurospora crassa." 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. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[5]	"Function of Neurospora mitochondrial tyrosyl-tRNA synthetase in RNA splicing requires an idiosyncratic domain not found in other synthetases." Cherniack A.D., Garriga G., Kittle J.D. Jr., Akins R.A., Lambowitz A.M. Cell 62:745-755(1990) [PubMed: 2143700] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M17118 Genomic DNA. Translation: AAA33620.1.
BX842626 Genomic DNA. Translation: CAE76265.1.
AABX02000007 Genomic DNA. Translation: EAA36180.1.

PIR

SYNCYT. A27158.

RefSeq

XP_965416.1. XM_960323.1.

UniGene

Ncr.20469.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y42	X-ray	1.95	X	33-423	[»]
2RKJ	X-ray	4.50	A/B/E/F/I/J/M/N	33-423	[»]

ProteinModelPortal

P12063.

SMR

P12063. Positions 39-419.

ModBase

Search...

Protein-protein interaction databases

STRING

P12063.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

EFNCRT00000002425; EFNCRP00000002425; EFNCRG00000002422.

GeneID

3881566.

KEGG

ncr:NCU03030.

NMPDR

fig|5141.1.peg.8150.

Phylogenomic databases

eggNOG

fuNOG04332.

GeneTree

EFGT00050000005158.

OMA

PLMPLFW.

OrthoDB

EOG41K2N3.

Enzyme and pathway databases

BioCyc

NCRA-XX3-01:NCRA-XX3-01-006778-MONOMER.

Family and domain databases

InterPro

IPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002307. Tyr-tRNA-synth.
IPR024088. Tyr-tRNA-synth_bac-type.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

KO

K01866.

PANTHER

PTHR11766. Tyr_tRNA-synt_1b. 1 hit.

Pfam

PF00579. tRNA-synt_1b. 1 hit.
[Graphical view]

PRINTS

PR01040. TRNASYNTHTYR.

TIGRFAMs

TIGR00234. TyrS. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SYYM_NEUCR

Accession

Primary (citable) accession number: P12063
Secondary accession number(s): Q7RVM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	February 1, 1996
Last modified:	January 25, 2012
This is version 111 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program