P12063
Gene name |
cyt-18 (B18P24.070, NCU03030) |
Protein name |
Tyrosine--tRNA ligase, mitochondrial |
Names |
Tyrosyl-tRNA synthetase, TyrRS |
Species |
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
KEGG Pathway |
ncr:NCU03030 |
EC number |
6.1.1.1: Ligases forming aminoacyl-tRNA and related compounds |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
4 structures for P12063
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1Y42 | X-ray | 195 A | X | 33-423 | PDB |
| 2RKJ | X-ray | 450 A | A/B/E/F/I/J/M/N | 33-423 | PDB |
| 4OJM | X-ray | 195 A | X | 33-423 | PDB |
| AF-P12063-F1 | Predicted | AlphaFoldDB |
No variants for P12063
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P12063 | |||||
No associated diseases with P12063
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.1 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| identical protein binding | Binding to an identical protein or proteins. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| tyrosine-tRNA ligase activity | Catalysis of the reaction: L-tyrosine + ATP + tRNA(Tyr) = L-tyrosyl-tRNA(Tyr) + AMP + diphosphate + 2 H(+). |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| Group I intron splicing | The splicing of Group I introns. This occurs by a ribozymic mechanism where the intron sequence forms a distinct 3D structure, characteristic of Group I introns and involved in determining the locations of the splice sites (there do not appear to be consensus splice site sequences) as well as having a role in catalyzing the splicing reactions, though protein factors are also required in vivo. Splicing occurs by a series of two transesterification reactions, generally with exogenous guanosine as the initiating nucleophile. The intron is excised as a linear piece (though it may subsequently circularize). |
| mRNA processing | Any process involved in the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide. |
| positive regulation of RNA splicing | Any process that activates or increases the frequency, rate or extent of RNA splicing. |
| RNA folding | The process of assisting in the covalent and noncovalent assembly of single or multimeric RNAs into the correct tertiary structure. |
| tRNA aminoacylation | The chemical reactions and pathways by which the various amino acids become bonded to their corresponding tRNAs. The most common route for synthesis of aminoacyl tRNA is by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules. |
| tyrosyl-tRNA aminoacylation | The process of coupling tyrosine to tyrosyl-tRNA, catalyzed by tyrosyl-tRNA synthetase. The tyrosyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tyrosine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 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 |