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 Q4A891

Entry ID Method Resolution Chain Position Source
AF-Q4A891-F1 Predicted AlphaFoldDB

No variants for Q4A891

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4A891

No associated diseases with Q4A891

3 regional properties for Q4A891

Type Name Position InterPro Accession
domain tRNA-binding domain 39 - 153 IPR002547
domain tRNA synthetase, B5-domain 386 - 460 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 45 - 145 IPR033714

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
MLFSLRRLKK LANLEAFSDQ KVIDSLINLG FEVDQITKLN EISGIKFGQI LEIRKNPEAD
70 80 90 100 110 120
NLWICKVQFA DKIREIQTTA KNVIENKQVL AFIPGSKSGN TTFLAKKLRG HISEGMLISA
130 140 150 160 170 180
AELGFNKHLL NSELDQGVLV FDPIFDLESN PLKVLELDDL ILDIKLLWNR PDGNSYLVLA
190 200 210 220 230 240
NELAAFFKTD FSLINKEITG KFYSELKIIN KTDSKIFALE IQKLPKLALV DIFLLLKSEV
250 260 270 280 290 300
KIDNLAQNFA NFILIYTGQP CYCLQLEKNQ QKVELIEQKV KIKYEPDAIS SYHFLDQEKK
310 320 330 340 350 360
PLLIPEFSDQ IIMENNSFFL IMPKFNLLKV KQIKQFLKKN SLKLTQLGKN YNYGTTFIAL
370 380 390 400 410 420
SFLNFFLEDQ KIDFSWPINF DKSLISKKTF LDLNYNELKE ILGLELSQED ISKTNLILEK
430 440 450 460 470 480
IGYNFDNTSF SPPFYRVDIE FFADYAADFL RFYGLEKLKD CKLEQVKAKI PNPDFEPVKL
490 500 510 520 530 540
KTLGYYETNS FLLISKKEDF NPLELKSQDL LTFPSQEHTK IRYSLAWQLA KITKYNQKRK
550 560 570 580 590 600
ITEINLYEKG SIAGWNHSLA LASTIYTSED LKKHLKILYN YDFDFLPADS EFLNPEKSQF
610 620 630 640 650 660
IYLDNVLVGW LGQVVEKYNY ENVTFLEILL SKVEKIPKKE GGKIKFRPYD NSQLKYRDIT
670 680 690 700 710
LSLPMKDIPD PYLKVIQKIP EIFSVKLINY VIINNQQKIT YRITGPDQVC AEIDKFYK