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 B1HUK4

Entry ID Method Resolution Chain Position Source
AF-B1HUK4-F1 Predicted AlphaFoldDB

No variants for B1HUK4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1HUK4

No associated diseases with B1HUK4

3 regional properties for B1HUK4

Type Name Position InterPro Accession
domain Threonyl/alanyl tRNA synthetase, SAD 685 - 728 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 26 - 585 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 22 - 741 IPR018165

Functions

Description
EC Number 6.1.1.7 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
alanine-tRNA ligase activity Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
tRNA binding Binding to a transfer RNA.
zinc ion binding Binding to a zinc ion (Zn).

1 GO annotations of biological process

Name Definition
alanyl-tRNA aminoacylation The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine 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
MGRQGLIHIV ILQYKLGGIY PMKAVDIRQM YLEFFKEKGH HHEPSAPLVP INDPSLLWIN
70 80 90 100 110 120
SGVATLKPYF DGRVIPDNPR ITNAQKSIRT NDIENVGKTA RHHTFFEMLG NFSIGDYFKK
130 140 150 160 170 180
EAIHYAWEFL TDKKWMGFDP ELLSITIHPE DQEAYDVWHQ EIGIPEERLI RLEGNFWDIG
190 200 210 220 230 240
EGPSGPNSEI FYDRGVEYGS DENDPEMYPG GENERYLEIW NLVFSQFNHN PDGTYTPLPK
250 260 270 280 290 300
QNIDTGMGLE RIVSVVQNVP TNFDTDLFMP IIEKIEEFAN RKYKRPSEVD LNEIFGSEED
310 320 330 340 350 360
INTPFKVIAD HIRTVAFAIG DGALPSNEGR GYVLRRLLRR AVRYAKQIGI EKPFMFELVP
370 380 390 400 410 420
TVGKIMEDFY PEVTEKCEFI QRVIKNEEIR FHETLDGGLA IFNEVAESQK AAGHDFIPGA
430 440 450 460 470 480
DAFRLYDTYG FPIELTEEYA EEVGMKVDHE GFETAMEEQR ERARAARQDV DSMQVQNEVL
490 500 510 520 530 540
ANLTVASEFV GFDTLVANTE IAAMIVNGQV EKVASEGQEA LVILAKTPFY AEMGGQIADS
550 560 570 580 590 600
GIISNDSFTA VVKDVQKAPN GQPLHTVIVE SGEMHVEDAV QAIVHRDDRN LIIKNHTATH
610 620 630 640 650 660
IMQRALKDVL GDHVNQAGSY VGPDRLRFDF SHFGQVTKEE LQQIERIVNE KVWDDIEVVI
670 680 690 700 710 720
EEMAIDQAKA KGAMALFGEK YGDVVRVVSI GDYSIELCGG IHVKRSSEIG FFKIVSEGGI
730 740 750 760 770 780
GAGTRRIEAV TGKVAYEVVK EEEALLNDAA ALLKANPKDI VTKVQALQGD YKELQRDNEA
790 800 810 820 830 840
LSQKIANAHS WGNCRCSTNN WRCHSSFYKS RSKDNNLLRQ MMDDLKALMP KAVIVLGAVD
850 860 870 880 890 900
GDLSDAMCRG ITIINRWQLP CWKYREIWCQ KLVVVIGGVR PDMAMAGAKD ASKLDEALLS
VYDYVKSI