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 Q9CDP6

Entry ID Method Resolution Chain Position Source
AF-Q9CDP6-F1 Predicted AlphaFoldDB

No variants for Q9CDP6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9CDP6

No associated diseases with Q9CDP6

5 regional properties for Q9CDP6

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 46 - 57 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 18 - 560 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 610 - 754 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 813 - 878 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 559 - 701 IPR033705

Functions

Description
EC Number 6.1.1.9 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
valine-tRNA ligase activity Catalysis of the reaction: L-valine + ATP + tRNA(Val) = L-valyl-tRNA(Val) + AMP + diphosphate + 2 H(+).

1 GO annotations of biological process

Name Definition
valyl-tRNA aminoacylation The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-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
MTNELTPKFN PTEVEAGRYE KWLEADVFKP SGNPDAEPYS IVIPPPNVTG KLHLGHAWDT
70 80 90 100 110 120
TLQDIIIRQK RMQGFDTLWL PGMDHAGIAT QAKVAARLAE DGILPQDLGR EKFLDKVWEW
130 140 150 160 170 180
KDEYATTIKE QWGKMGISVD YSRERFTLDE GLSQAVRKVF VQLYNKGWIY RGEKLINWDP
190 200 210 220 230 240
KAMTALSDIE VIHKEIDGAF YHITYQIEGS DEFVEIATTR PETFLGDTAV IVNEKDERYK
250 260 270 280 290 300
HLVGKNVILP IINRVIPILT DDHADMEKGT GVVKITPAHD PNDFEVAMRH DLPMINMMNN
310 320 330 340 350 360
DGTINENGGK YEGLDRFEAR KQIVADLKEL GQLVDIKPVR HEVGHSERTG VVVEPRLSTQ
370 380 390 400 410 420
WFVKMDELAK NAIANQTTED AVEFYPPRFN DTFMQWMENV HDWVISRQLW WGHQIPAWYN
430 440 450 460 470 480
EAGEMYVGEE APEGEGWTQD EDVLDTWFSS ALWPFSTMGW PDENSADFIR YFPTSTLVTG
490 500 510 520 530 540
YDIIFFWVSR MIFQSLEFTG KSPFHNVLIH GLIRDEEGRK MSKSLGNGID PMDVIEKYGA
550 560 570 580 590 600
DALRWFLSNG SAPGQDVRFS YDKMDAAWNF INKIWNVSRY ILMNAEDISA DAVSSALTKV
610 620 630 640 650 660
ANKTAGNVTD RWILTRLNDT VERVTEQMDK FEFGVAGHIL YNFIWDEFAN WYLELTKEVM
670 680 690 700 710 720
FGEDEAEKDI TRAVLLHVLD QVLRLLHPIM PFFTEEIFEK LPNTSGSIVV AEYPKVRPEF
730 740 750 760 770 780
NDDKASEGVA MLIELITAVR NIRAEVNTPL SKAVPMLIKS EHADFLNAVS PYISRFTNPS
790 800 810 820 830 840
ELTIAKDLAV PEQAMSAVIT GAELYLPLAG LINIEEEIAR LEKELAKWQK ELDLVNKKLG
850 860 870
NERFVANAKA EVVQKEKDKL ADYQEKFDTV KARIAELKEN