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 Q2NT27

Entry ID Method Resolution Chain Position Source
AF-Q2NT27-F1 Predicted AlphaFoldDB

No variants for Q2NT27

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2NT27

No associated diseases with Q2NT27

6 regional properties for Q2NT27

Type Name Position InterPro Accession
domain tRNA-binding domain 39 - 148 IPR002547
domain Ferrodoxin-fold anticodon-binding domain 701 - 794 IPR005121
domain B3/B4 tRNA-binding domain 212 - 385 IPR005146
domain tRNA synthetase, B5-domain 401 - 476 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 45 - 147 IPR033714
domain Phenylalanyl tRNA synthetase beta chain, core domain 474 - 689 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
MKFSELWLRE WVNPAIDSEA LVDQITMSGL EVDGVEPVAG RFTGVVVGRV VECRQHSNAD
70 80 90 100 110 120
KLRVTKVDVG GERLLDIVCG APNCRAGLRV AVAMLGAVLP GDFKIKVAKL RGEPSEGMLC
130 140 150 160 170 180
SFSELGITGD HDGIIELPAE APIGQDIRDY LQLDDNTIDI SVTPNRADCL GLLGIARDVA
190 200 210 220 230 240
VRNRLPLHMP AIETVTPEIS DTLPIRVDAV EACPRYLGRV VKNINVSAAT PLWMKEKLRR
250 260 270 280 290 300
CGLRSVDAVV DITNYVLLEL GQPMHAFDRA RIEGGIVVRH ARQDETLTLL DGSDVTLSLD
310 320 330 340 350 360
TLVIADHGQA LAMAGIFGGG AYCISPTTRD VVLECAFFNP LAITGRARRY GLHTDASHRY
370 380 390 400 410 420
ERGVDPALQP RAMERATALL VAICGGQPGP VIDVTSASAQ PQPATITLRR KTLDRLIGHV
430 440 450 460 470 480
IPDEDVSDIL TRLGCQVSRT AEGWQAVAPS WRFDMAIEED LIEEVARVYG YDAIPNVPVR
490 500 510 520 530 540
ANLVMPHHRE AALPLARVKT LLVDRGYQEA ITYSFVDPKT QVLLHPQQAP LVLPSPISQD
550 560 570 580 590 600
MSAMRLSLWT GLLGAVVYNQ NRQQQRVRLF ESGLRFVPDN AADLGIRQDL MLAGVIAGPR
610 620 630 640 650 660
SDEHWDQLRQ PVDFYDAKGD LEAILELTGK LDDIEFRAQR HPALHPGQSA AIYLNNEAIG
670 680 690 700 710 720
FIGVIHPELE AKLNLNGCTL VFELLWEKVA ERKVPEANDI SRFPANRRDI AVVVADDVAV
730 740 750 760 770 780
ADIIAECKKV GANQLVGVNL FDVYRGRGVA EGFKSLAISL ILQDTARTLE EEEIAATVAK
790
CVAALKQRFQ ASLRD