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 Q38XD1

Entry ID Method Resolution Chain Position Source
AF-Q38XD1-F1 Predicted AlphaFoldDB

No variants for Q38XD1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q38XD1

No associated diseases with Q38XD1

5 regional properties for Q38XD1

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 48 - 59 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 20 - 564 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 608 - 755 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 814 - 879 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 563 - 699 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
MTDHKEMSTK YDPNQVEDGR YQDWLKEDLF KPNANPDAKP YSIVIPPPNV TGKLHLGHAW
70 80 90 100 110 120
DTTLQDMLIR QKRMQGYDVL WLPGMDHAGI ATQAKVEAKL AEQGISRYDL GREKFIDQVW
130 140 150 160 170 180
EWKDEYAATI HDQWAKMGLS LDYSRERFTL DDGLSDAVRK VFVNLYNKGL IYRGEYIINW
190 200 210 220 230 240
DPKARTALSD IEVLHQDDEG AFYHVSYPLT DGSGSIEIAT TRPETLPGDT AIAVHPDDER
250 260 270 280 290 300
YADLVGKTVT LPLMNREIPI IADHYVDKDF GTGALKITPA HDPNDFEVGN RHDLPRINVM
310 320 330 340 350 360
NEDASMNESA GKYNGMDRFE ARKAIVADLK EQGFLIKVDP MTHSVGHSER TGVQVEARLS
370 380 390 400 410 420
TQWFVKMKPL AEMALKNQET DQKVNFVPER FENTFTQWME NVHDWVISRQ LWWGHQIPAW
430 440 450 460 470 480
YHKQTGEMYV GEEAPEDIEN WTQDSDVLDT WFSSALWPFS TMGWPNTEAP DFKRYFPTNT
490 500 510 520 530 540
LVTGYDIIFF WVSRMIFQSL EFTEQRPFEH VLIHGLIRDE QGRKMSKSLG NGIDPMEVIE
550 560 570 580 590 600
KYGADALRWF LTSGSTPGQD VRFSYTKMDA AWNFINKIWN ASRFVIMNLE DTPAPTKVPE
610 620 630 640 650 660
AANLDLTDKW ILSQLNQTVA DVTRLYEGFE FGEAGRTLYN FIWNDFCDWY IEMAKEVLYG
670 680 690 700 710 720
DDQEAIANKR YNLAYVLDQT LRLLHPVMPF VTEEIWQSMP HTGESIMTAS YPEVHAELDD
730 740 750 760 770 780
QEATTQMNAL IDLIRSVRNI RSEANAPLSK PIDILINIQD TPLMAIFKQN QDFIERFVHP
790 800 810 820 830 840
KSLEIAEGLT APALAKTAII SGAEVYVPLA ELLDLDEEIT RLEGELKRLN GEIKRAQGKL
850 860 870 880
ANKGFTDRAP EKVVQEERDK QADYEQQYQS VEKRLAELKA AR