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 Q06817

Entry ID Method Resolution Chain Position Source
AF-Q06817-F1 Predicted AlphaFoldDB

13 variants for Q06817

Variant ID(s) Position Change Description Diseaes Association Provenance
s16-703863 36 F>L No SGRP
s16-703372 199 L>F No SGRP
s16-703280 230 R>K No SGRP
s16-703257 238 E>K No SGRP
s16-703204 255 E>D No SGRP
s16-703155 272 G>S No SGRP
s16-703028 314 K>R No SGRP
s16-702996 325 N>D No SGRP
s16-702660 437 Q>E No SGRP
s16-702576 465 I>V No SGRP
s16-702423 516 G>S No SGRP
s16-702401 523 R>K No SGRP
s16-702122 616 V>A No SGRP

No associated diseases with Q06817

1 regional properties for Q06817

Type Name Position InterPro Accession
domain Domain unknown function DUF295 349 - 395 IPR005174

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
glycine-tRNA ligase activity Catalysis of the reaction: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).
protein dimerization activity The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.
transferase activity Catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

3 GO annotations of biological process

Name Definition
diadenosine tetraphosphate biosynthetic process The chemical reactions and pathways resulting in the formation of diadenosine tetraphosphate, a derivative of the nucleoside adenosine with four phosphate groups attached.
glycyl-tRNA aminoacylation The process of coupling glycine to glycyl-tRNA, catalyzed by glycyl-tRNA synthetase. The glycyll-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a glycine-accepting tRNA.
mitochondrial glycyl-tRNA aminoacylation The process of coupling glycine to glycyl-tRNA in a mitochondrion, catalyzed by glycyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P38088 GRS1 Glycine--tRNA ligase 1, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P41250 GARS1 Glycine--tRNA ligase Homo sapiens (Human) PR
Q9CZD3 Gars1 Glycine--tRNA ligase Mus musculus (Mouse) PR
Q10039 gars-1 Glycine--tRNA ligase Caenorhabditis elegans PR
10 20 30 40 50 60
MPLMSNSERD KLESTLRRRF FYTPSFEIYG GVSGLFDLGP PGCQLQNNLI RLWREHFIME
70 80 90 100 110 120
ENMLQVDGPM LTPYDVLKTS GHVDKFTDWM CRNPKTGEYY RADHLIEQTL KKRLLDKDVN
130 140 150 160 170 180
PQDMKNMEKI LTTIDGFSGP ELNLVMQEYN INDPVTNDVL DALTSFNLMF ETKIGASGQL
190 200 210 220 230 240
KAFLRPETAQ GQFLNFNKLL EINQGKIPFA SASIGKSFRN EISPRSGLLR VREFLMAEIE
250 260 270 280 290 300
HFVDPLNKSH AKFNEVLNEE IPLLSRRLQE SGEVQLPVKM TIGEAVNSGM VENETLGYFM
310 320 330 340 350 360
ARVHQFLLNI GINKDKFRFR QHLKNEMAHY ATDCWDGEIL TSYGWIECVG CADRAAFDLT
370 380 390 400 410 420
VHSKKTGRSL TVKQKLDTPK ERTEWVVEVN KKFFGSKFKQ KAKLIESVLS KFSQDELIRR
430 440 450 460 470 480
HEELEKNGEF TCQVNGQIVK LDSSLVTIKM KTTLQHIREY IPNVIEPSFG LGRIIYCIFD
490 500 510 520 530 540
HCFQVRVDSE SRGFFSFPLQ IAPIKVFVTT ISNNDGFPAI LKRISQALRK REIYFKIDDS
550 560 570 580 590 600
NTSIGKKYAR NDELGTPFGI TIDFETIKDQ TVTLRERNSM RQVRGTITDV ISTIDKMLHN
610
PDESDWDKST FGLSPVKI