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 Q7W7C6

Entry ID Method Resolution Chain Position Source
AF-Q7W7C6-F1 Predicted AlphaFoldDB

No variants for Q7W7C6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q7W7C6

No associated diseases with Q7W7C6

3 regional properties for Q7W7C6

Type Name Position InterPro Accession
domain Phenylalanyl-tRNA synthetase 91 - 326 IPR002319
domain Phenylalanine-tRNA ligase, class II, N-terminal 19 - 87 IPR004188
domain Aminoacyl-tRNA synthetase, class II 119 - 317 IPR006195

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
MQFPESWLRS LVNPSIGTDE LAHRLTMAGL EVEETEPAAP PFTGVVVARI VDIAPHPDAD
70 80 90 100 110 120
KLRVCQVDDG SGALLQIVCG APNAAAGLTV PLARVGAELP GGMKIGVAKM RGVQSSGMLC
130 140 150 160 170 180
SARELGLSQD HAGLLELPAA LRPGTDIRAA LDLDDTLFTL KLTPNRADCL SIFGVAREVA
190 200 210 220 230 240
ALTGTPLTAP AAEPVPVTID HRLPVAIQAP DLCGRFAGRV IQGVNARAAT PEWMKTRLER
250 260 270 280 290 300
AGQRSVSALV DISNYVMLEV GRPSHVFDLD KIGGDLSVRW AREGETLELL NGQAVALDPK
310 320 330 340 350 360
VGVVVAGEQV ESLAGIMGGE ATSVTLDTRN IYLEAAFWWP GAIAGRARRY KFSSEASHRF
370 380 390 400 410 420
ERGVDYASIP EHIELITRLI LDICGGQAGP VDDQCVNLPV REPVRMRLAR CHRVLGVAVE
430 440 450 460 470 480
RAEVAQIFTR LGLPFQEQGD DFVVTPPSYR FDIEIEEDLI EEVARVYGFE RIPDVPPVAR
490 500 510 520 530 540
AKMHAQPEAR RGAHAVRRLV AARDYQEVVN YSFVEAAWER DYAGNDNLVR LVNPIASHLS
550 560 570 580 590 600
VMRSSLIAGL VAIVRHNANR KQSRVRLFEL GRVFHRDPQL ADGPLEVAGV RQPLMLAGVA
610 620 630 640 650 660
WGGAVEEQWG VPHRQVDFYD VKQDVEALFG ARADALRFVA DRYPALHPGR SARIELDGQP
670 680 690 700 710 720
IGWLGELHPQ WTQQADLHHA PVVFELDFEA LAERRLPAVR ELSRQPAVVR DLALWVDAKL
730 740 750 760 770 780
PAQAMLDTVA AAIARDPQLS VVQDAQVFDV WREKPVAGQT VTEKSLAFRF WLQDTEVTLD
790 800
EARVADCIAR IKDALVAAHN ARQRA