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 Q82VV6

Entry ID Method Resolution Chain Position Source
AF-Q82VV6-F1 Predicted AlphaFoldDB

No variants for Q82VV6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q82VV6

No associated diseases with Q82VV6

6 regional properties for Q82VV6

Type Name Position InterPro Accession
domain tRNA-binding domain 39 - 149 IPR002547
domain Ferrodoxin-fold anticodon-binding domain 694 - 786 IPR005121
domain B3/B4 tRNA-binding domain 213 - 386 IPR005146
domain tRNA synthetase, B5-domain 400 - 475 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 45 - 148 IPR033714
domain Phenylalanyl tRNA synthetase beta chain, core domain 473 - 682 IPR041616

Functions

Description
EC Number 6.1.1.20 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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
magnesium ion binding Binding to a magnesium (Mg) ion.
phenylalanine-tRNA ligase activity Catalysis of the reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
tRNA binding Binding to a transfer RNA.

1 GO annotations of biological process

Name Definition
phenylalanyl-tRNA aminoacylation The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting 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
MKFSGNWLRK LVDLQYSDEE LAHKLTMAGL EVESVAPVAP FFDKVVVAQV VSVQKHANAD
70 80 90 100 110 120
RLNVCKVDVG TQSDGFLQIV CGAQNVKEGM KTVCALVGAR LPELDIRQGK IRGVESLGML
130 140 150 160 170 180
CSAKELGLAS DADGLLELPG DTPVGVDFRK YYSLDDCIFT LKLTPNRADC LGMFGIAREV
190 200 210 220 230 240
AAITASELDL PEIVFVNPVI EDVLQIRVEE PESCPLYCGR VIKGVATDTA IPLWMSQRLE
250 260 270 280 290 300
RAGLRMINPV VDIINYAMLE TGQPMHAFDL NQINQEICVR FAGENEHLLL LNGERLTLQK
310 320 330 340 350 360
DMLVIADSSK PLALAGIMGG SESGVTNTTI DVFLESAFFS PVVISGKSFK LGFTSDSAHR
370 380 390 400 410 420
FERGVDFSMT RSVLERATAL ILEICGGKAG PVTEIGNDLP RREAVRVRQK RIAKILGVDF
430 440 450 460 470 480
SVELISEYFQ RLQFSYTIAG EMFYVVPPAA RFDLVIEEDF IEEIARVHGY DLIPARLPKA
490 500 510 520 530 540
PVHMLAEPET GVSPVKRLRQ ILTAKDYQEV INYTFVDTQW EADFSGNDIP IRLKNPIASH
550 560 570 580 590 600
MDVMRSSLFG GLIDNLQFNL NRKQSRVRIF ELGSCFSKEG DEEKEVENLA ALCSGSAYPE
610 620 630 640 650 660
QWGVPDRDID FYDVKMDIES LFWPRSVYFE LALHPALHPG KSARILIDKK PVGWIGELHP
670 680 690 700 710 720
RWQSKYHLSQ SAILFELRTE ALAAELLPAM YPLSKFPPVR RDIAVVVESD VSVASLLETM
730 740 750 760 770 780
HLEKDRSISE ISLFDLYSGE KLVQGKKSLA FRILLQDSEK TLTDQEIDRA VSQLVGILER
KFGATLRS