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 Q2NVL2

Entry ID Method Resolution Chain Position Source
AF-Q2NVL2-F1 Predicted AlphaFoldDB

No variants for Q2NVL2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2NVL2

No associated diseases with Q2NVL2

4 regional properties for Q2NVL2

Type Name Position InterPro Accession
domain DHHA1 domain 732 - 870 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 653 - 696 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 7 - 555 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 3 - 709 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
MSKSTAEIRQ AFLDFFHSKG HQVVASSSLV PDNDPTLLFT NAGMNQFKDV FLGLDNRFYR
70 80 90 100 110 120
RATTSQRCVR AGGKHNDLEN VGYTARHHTF FEMLGNFSFG DYFKHDAIRF AWELLTGEHW
130 140 150 160 170 180
FNLPKEKLWV TVYATDDEAY NIWASEVGIP AERIIRIGDN KGSAYASDNF WQMGDTGPCG
190 200 210 220 230 240
PCSEIFYDHG EHIWGGPPGS PEEDGDRYIE IWNLVFMQFN RQADGTLLPL PKPSVDTGMG
250 260 270 280 290 300
LERIAAVLQH VNSNYDIDLF KTLIAAAAEA TGASDPDSKS LRVIADHIRS CVFLVSDGVV
310 320 330 340 350 360
PSNEGRGYVL RRIIRRAIRH GNMLGASDTF FYKLVAPLID VMGSAASQLQ PQQAMVEQVL
370 380 390 400 410 420
RAEEEQFART LERGLTLLDD ELAKLTGDTL DGETAFRLYD TYGFSLDLTA DVCRERNLRV
430 440 450 460 470 480
DEAGFERAME AQRKRARESS GFGADYNSLL RVDETTRFFG YEHLEHQGRV TALFRDGQLV
490 500 510 520 530 540
GVIRQGEEAV VVLDETPFYG ESGGQVGDRG VLKAASGVFE VADTQKYGKA FGHQGKLSYG
550 560 570 580 590 600
ELKLGAQVTA QVDSARRERI RLNHSATHLL HAALRQVLGD HVGQKGSLVN DHYLRFDFSH
610 620 630 640 650 660
NEAMKPEQIR RVEEIVNEQI RCNLPIQTDI MALEDARNKG AMALFGEKYE AQVRVLSMGD
670 680 690 700 710 720
FSTELCGGTH ASRTGDIGLF RIIAESGTAA GIRRIEAVTG EEALASLHQQ SDLVQHIAQL
730 740 750 760 770 780
VKGDSQTLVD KVRALQERSR QLEKDLQQLK NQQAAQESAS LGRNVRDING VKVLVRQLDS
790 800 810 820 830 840
AEPKMLRTMV DDLKNQLGSA VIILATVAEG KVSLIAGVTK DLTDRVKAGD IVGHLAQQVG
850 860 870
GKGGGRPDLA QAGGSDIAAL PAALASVDAM LAAKL