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

1 structures for Q9FYR6

Entry ID Method Resolution Chain Position Source
AF-Q9FYR6-F1 Predicted AlphaFoldDB

28 variants for Q9FYR6

Variant ID(s) Position Change Description Diseaes Association Provenance
ENSVATH12719432 11 L>F No 1000Genomes
ENSVATH07402278 20 T>N No 1000Genomes
tmp_5_21311172_C_A 21 R>S No 1000Genomes
tmp_5_21311200_T_G 30 V>G No 1000Genomes
ENSVATH00729510 30 V>L No 1000Genomes
ENSVATH14628161 35 R>K No 1000Genomes
tmp_5_21311263_A_G 51 E>G No 1000Genomes
tmp_5_21311277_G_A 56 E>K No 1000Genomes
ENSVATH12719433 62 S>P No 1000Genomes
ENSVATH00729513 111 D>G No 1000Genomes
tmp_5_21311842_T_G 141 S>A No 1000Genomes
tmp_5_21312301_C_T 226 T>I No 1000Genomes
ENSVATH12719486 234 A>V No 1000Genomes
tmp_5_21312471_T_C 254 I>T No 1000Genomes
tmp_5_21312514_T_G 268 D>E No 1000Genomes
tmp_5_21312570_C_T 287 T>I No 1000Genomes
ENSVATH07402287 302 Q>R No 1000Genomes
ENSVATH12719492 304 A>S No 1000Genomes
tmp_5_21312801_C_T 304 A>V No 1000Genomes
ENSVATH12719493 351 I>V No 1000Genomes
ENSVATH00729525 387 T>A No 1000Genomes
ENSVATH14628166 413 R>L No 1000Genomes
ENSVATH14628167 418 N>S No 1000Genomes
ENSVATH00729527 427 V>I No 1000Genomes
ENSVATH12719526 437 I>M No 1000Genomes
tmp_5_21313528_C_T 457 T>I No 1000Genomes
ENSVATH03414942 486 S>L No 1000Genomes
ENSVATH12719527 486 S>T No 1000Genomes

No associated diseases with Q9FYR6

5 regional properties for Q9FYR6

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 160 - 329 IPR002314
domain Anticodon-binding 348 - 450 IPR004154
domain Aminoacyl-tRNA synthetase, class II 93 - 341 IPR006195
domain Proline-tRNA ligase, class II, C-terminal 477 - 543 IPR016061
domain Prolyl-tRNA synthetase, catalytic domain 72 - 331 IPR033721

Functions

Description
EC Number 6.1.1.15 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Plastid, chloroplast
  • Mitochondrion
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
aminoacyl-tRNA synthetase multienzyme complex A multienzyme complex found in all multicellular eukaryotes composed of eight proteins with aminoacyl-tRNA synthetase activities (abbreviated as: ArgRS, AspRS, GluProRS, GlnRS, IleRS, LeuRS, LysRS, MetRS where RS is the enzyme, preceded by the amino acid it uses as a substrate) as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. Several of these subunits are known dimers, so the total polypeptide count in the multisynthetase complex is at least fifteen. All of the enzymes in this assembly catalyze the same reaction, the covalent attachment of an amino acid to either the 2'- or 3'-hydroxyl of the 3'-terminal adenosine of tRNA, but using different substrates.
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
chloroplast stroma The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
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.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
proline-tRNA ligase activity Catalysis of the reaction: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).

5 GO annotations of biological process

Name Definition
embryo sac development The process whose specific outcome is the progression of the embryo sac over time, from its formation to the mature structure. The process begins with the meiosis of the megasporocyte to form four haploid megaspores. Three of the megaspores disintegrate, and the fourth undergoes mitosis giving rise to a binucleate syncytial embryo sac. The two haploid nuclei migrate to the opposite poles of the embryo sac and then undergo two rounds of mitosis generating four haploid nuclei at each pole. One nucleus from each set of four migrates to the center of the cell. Cellularization occurs, resulting in an eight-nucleate seven-celled structure. This structure contains two synergid cells and an egg cell at the micropylar end, and three antipodal cells at the other end. A binucleate endosperm mother cell is formed at the center. The two polar nuclei fuse resulting in a mononucleate diploid endosperm mother cell. The three antipodal cells degenerate.
plant ovule development The process whose specific outcome is the progression of the ovule over time, from its formation to the mature structure. The ovule is the structure in seed plants enclosing the female gametophyte, and is composed of the nucellus, one or two integuments, and the funiculus; it develops into the seed.
prolyl-tRNA aminoacylation The process of coupling proline to prolyl-tRNA, catalyzed by prolyl-tRNA synthetase. The prolyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a methionine-accetping tRNA.
regulation of photosynthesis Any process that modulates the frequency, rate or extent of photosynthesis.
seed development The process whose specific outcome is the progression of the seed over time, from its formation to the mature structure. A seed is a propagating organ formed in the sexual reproductive cycle of gymnosperms and angiosperms, consisting of a protective coat enclosing an embryo and food reserves.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVSSSLRLPS LTSLLFPATT RYPATLRRTV CLRNRPLSGF ATAPSGTASP ETKSSEVDRL
70 80 90 100 110 120
RSDRAVTPRS QDFNAWYLDV IASAELADYG PVRGTMVIRP YGYAIWEAIQ DYLNVKFKET
130 140 150 160 170 180
GHSNMYFPQF IPYSFIEKEA SHVEGFSPEL ALVTVGGGKE LEEKLVVRPT SETIVNHMFT
190 200 210 220 230 240
QWIHSYRDLP LMINQWANVT RWEMRTKPFI RTLEFLWQEG HTAHATPEEA EKEAKQMIEI
250 260 270 280 290 300
YTRFAFEQTA IPVIPGRKSK LETFAGADIT YTIEAMMGDR KALQAGTSHN LGQNFSRAFG
310 320 330 340 350 360
TQFADENGER QHVWQTSWAV STRFVGGIIM THGDDTGLML PPKIAPIQVV IVPIWKKDTE
370 380 390 400 410 420
KTGVLSAASS VKEALQTAGV RVKLDDTDQR TPGWKFNFWE MKGIPLRIEI GPRDVSSNSV
430 440 450 460 470 480
VVSRRDVPGK AGKVFGISME PSTLVAYVKE KLDEIQTSLL EKALSFRDSN IVDVNSYAEL
490 500 510 520 530 540
KDAISSGKWA RGPWSASDAD EQRVKEETGA TIRCFPFEQT QGTKTCLMTG NPAEEVAIFA
KSY