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 Q2GFL5

Entry ID Method Resolution Chain Position Source
AF-Q2GFL5-F1 Predicted AlphaFoldDB

No variants for Q2GFL5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2GFL5

No associated diseases with Q2GFL5

3 regional properties for Q2GFL5

Type Name Position InterPro Accession
domain Threonyl/alanyl tRNA synthetase, SAD 671 - 713 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 10 - 572 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 5 - 726 IPR018165

Functions

Description
EC Number 6.1.1.7 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.

4 GO annotations of molecular function

Name Definition
alanine-tRNA ligase activity Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
tRNA binding Binding to a transfer RNA.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
alanyl-tRNA aminoacylation The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine accetping tRNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MMKNNLVSNL RKSFIDFFAK NGHQVFPSSP LILKDDPSLL FTNAGMVQFK QMFTNPNNAN
70 80 90 100 110 120
VNTATSSQKC LRVGGKHNDL ENVGYTNRHH TFFEMLGNFS FGSYFKEGAI EFAWNFVIKE
130 140 150 160 170 180
LSLSKDRLYF TVYHDDQEAF DLWKKISGVS DSRIIKITTS DNFWSMGNTG PCGPCSEIFY
190 200 210 220 230 240
DYGDNVKGGL PGTPEEDGAR FTEIWNLVFM QYDRKLDGEL CVLPKKCIDT GMGLERIAAV
250 260 270 280 290 300
MQGVHDNYDI SLFKALIAAS KEQSGNSTNE LAHRVIADHV RSAAFLIAEG LTPGNEGRNY
310 320 330 340 350 360
ILRRIIRRAA RYVYMLKYDD ALMYKVFPTL IDEESCGYMA DYYPELIHAK DLIMSILKIE
370 380 390 400 410 420
EENFKDTLVR ALPLLEKELM NLSSGDILSG DIVFKLYDTY GFPVDITLDI IKEKGVKFDE
430 440 450 460 470 480
QGFYDNMNKQ KERSKLNHSI KSDQQLKEEF WVDIKERCGS TKFVGYERYD TKATVLSIVC
490 500 510 520 530 540
GGDKNVEIAN VGDKVSILLD ITPFYAESGG QKGDVGIFNV IVRQEKELFA NDNIAEVIDT
550 560 570 580 590 600
KKVLDTLYIH ECIIKQGSLM VGDVIFAKID CERRRNLCAN HSATHLLHYV LKSEIDSSIM
610 620 630 640 650 660
QKGSLVSDEK LRFDFSYGVA LTKEQLTLIE DKMYSLISGN NPVISHVCDL KDAVAGGAVA
670 680 690 700 710 720
LFTEKYEEHG VRVVSIKDSK ELCCGTHVKY TSEIGCFKIV SEASIACGIR RIEAVTGRYA
730 740 750 760 770 780
IDYFRQQEKM LNSIAESVKV PVDNVLVQID KLDKKNQELE QKLSDVYFDM INLQGVNTEK
790 800 810 820 830 840
IGNVDFLYSN LSNIPVNVMR KFINKHLTAD RIILFANVVG QNVVCVVGVG NSLHCKVKAV
850 860 870 880
DFVKMIGTMV KSKGGGNAQL AQINGEYVKE IDIMSNVKSK LVDILSN