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 B2S0L6

Entry ID Method Resolution Chain Position Source
AF-B2S0L6-F1 Predicted AlphaFoldDB

No variants for B2S0L6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B2S0L6

No associated diseases with B2S0L6

3 regional properties for B2S0L6

Type Name Position InterPro Accession
domain Phenylalanyl-tRNA synthetase 92 - 328 IPR002319
domain Phenylalanine-tRNA ligase, class II, N-terminal 20 - 87 IPR004188
domain Aminoacyl-tRNA synthetase, class II 116 - 319 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).
RNA binding Binding to an RNA molecule or a portion thereof.

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
MPKVEVYRSI LLGKIGKDLT DCELVSILEM AKAEICEFYT GNDKIKIEFN DTNRPDLWSY
70 80 90 100 110 120
TGLARQIKTY LFGQLPSFEF FSTADNLQKF YGEILVSPEA FSIRPFIFGF LAKGMICNEQ
130 140 150 160 170 180
MLETLIQLQE KLCHNYGQKR KRVAMGMYSS ASIEFPVSYV TCNSDYRFIP LGMDIEMSIK
190 200 210 220 230 240
EINKRHPKGI EYASILEHFT EYPLLLDYND KVLSYPPVIN SHDIGALKVG DTDLFIEVTG
250 260 270 280 290 300
TNLEATLLSL SVVACDLHDM GFEILPVKTV FPKETPFGKE IICPYYFQNT LEVSVESVNR
310 320 330 340 350 360
MFGSNFTVND MCLDLKKLGI SAYFKELDKF YIIPPVYRND FLHEVDVIEE IMIGRGLDSF
370 380 390 400 410 420
KPELPKDFTL GKLSQIEEFS RKIKNLMIGM GFQEMIYNYL GSRTDFIEKM NIKSDEFLSV
430 440 450 460 470 480
ANPMTEGYEY VRGSIVPDLL KSESISSNFP YPHKIFEIGK VALKDLSSVD GTMTYDNLAF
490 500 510 520 530 540
LMADKEFSFN EINSLVSSLF YYLNIEFKLR ESSQTLYING RGADILINDI ILGSFGEVSP
550 560
YILSNFGIMV PCCVLEINLN KILH