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

2 regional properties for P12063

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 104 - 114 IPR001412
domain Tyrosyl-tRNA synthetase, C-terminal 448 - 567 IPR032005

Functions

Description
EC Number 6.1.1.1 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Mitochondrion matrix
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