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 Q3ZXB5

Entry ID Method Resolution Chain Position Source
AF-Q3ZXB5-F1 Predicted AlphaFoldDB

No variants for Q3ZXB5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3ZXB5

No associated diseases with Q3ZXB5

6 regional properties for Q3ZXB5

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 267 - 473 IPR002314
domain Anticodon-binding 485 - 572 IPR004154
domain Aminoacyl-tRNA synthetase, class II 185 - 478 IPR006195
domain Threonyl/alanyl tRNA synthetase, SAD 112 - 161 IPR012947
domain Threonine-tRNA ligase catalytic core domain 185 - 483 IPR033728
domain Threonine-tRNA ligase, class IIa, anticodon-binding domain 483 - 572 IPR047246

Functions

Description
EC Number 6.1.1.3 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.
metal ion binding Binding to a metal ion.
threonine-tRNA ligase activity Catalysis of the reaction: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr).
tRNA binding Binding to a transfer RNA.

1 GO annotations of biological process

Name Definition
threonyl-tRNA aminoacylation The process of coupling threonine to threonyl-tRNA, catalyzed by threonyl-tRNA synthetase. The threonyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a threonine-accetping tRNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MANQIDESKP ISDLEIMRHS AAHIMAEAVL SMFPEAKLGI GPAIDTGFYY DFDLPRTLTP
70 80 90 100 110 120
EDLPEIETRM NQLVKSNLPF RREEMSKDEA RKLFANQPYK LELLNDITDE TVSIYRQGNF
130 140 150 160 170 180
CDLCRGPHVN YTSKVKAFKL LSIAGAYWRG DEKRPMLQRI YGAAFLDKAS LAEYLNMLEE
190 200 210 220 230 240
AAKRDHRKLG KELELFSLHQ EIGGGLVNWL PNGAIVRHLI EEFWKKEHLK RGYDLVYTPH
250 260 270 280 290 300
IAKVDLWKTS GHWGFYRENM YSPMDIDGEE YVLKPMNCVY HILMFKNRTR SYKELPIRMA
310 320 330 340 350 360
ELGTVYRYER SGVLHGLSRV RGFTQDDAHI FCLYDQLEKE VVKVLDLAKF MIDTFGFTKY
370 380 390 400 410 420
KVMLSTRPEK YVGELDKWEY ATDILAKALE ANQIPYQVDP GEGVFYGPKI DIKFEDALGR
430 440 450 460 470 480
TWQGPTIQVD FQLPERFDVS VVGEDGKDQP VAMVHRTVLG SMERFMSCLT EQYGGAFPAW
490 500 510 520 530 540
LSPKQVMVIP IADRHTEFAE KLACELREEE VRVEVDSRSE TMNQKIRQAQ LAKIPYMLVV
550 560 570 580
GDKEIETQSV AVRTRTGSQQ VMPFAEFKSM LLAKIKTKST EI