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 B0JI84

Entry ID Method Resolution Chain Position Source
AF-B0JI84-F1 Predicted AlphaFoldDB

No variants for B0JI84

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0JI84

No associated diseases with B0JI84

4 regional properties for B0JI84

Type Name Position InterPro Accession
domain DHHA1 domain 729 - 868 IPR003156
domain Threonyl/alanyl tRNA synthetase, SAD 648 - 691 IPR012947
domain Alanyl-tRNA synthetase, class IIc, N-terminal 9 - 549 IPR018164
domain Alanyl-tRNA synthetase, class IIc, core domain 5 - 704 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
MSNHLSGSEI RQRFLDFFAA RNHKILPSAS LVPEDPTVLL TIAGMLPFKP IFLGQKTPEF
70 80 90 100 110 120
PRATTSQKCI RTNDIENVGR TARHHTFFEM LGNFSFGDYF KEQAIAWAWE LSTEVFNLPP
130 140 150 160 170 180
ERLVVSVFKE DEEAFAIWRD KIGIPAHRIQ KMGEEDNFWV SGPTGPCGPC SEIYYDFHPE
190 200 210 220 230 240
LGDKTIDLED DSRFIEFYNL VFMQYNRDAD GNLTPLANKN IDTGMGLERM AQILQKVANN
250 260 270 280 290 300
YETDLIFPIV AEAARLAAID YQKADEKTKV SLKVIGDHVR SVVHMIADGI SASNTDRGYV
310 320 330 340 350 360
LRRLIRRVVR HGRLIGIEGQ FITKVAEVAI ALSESVYGNV RERETVIKAE LEREEARFLE
370 380 390 400 410 420
TLERGEKLLE SILEKEKSQI SGVDAFTLYD TYGFPLELTQ EIAEEQGLSV DTAGFEQEMK
430 440 450 460 470 480
KQQQRSKAAH ETIDLTVQGS LDKLAEHIHP TEFLGYTDLQ ATATVTAVLV AGKTVESAAA
490 500 510 520 530 540
GTEVQVVLDR TPFYAESGGQ IGDKGYLTGD NLLIRIEDVQ KESGIFIHFG RIERGIVTTG
550 560 570 580 590 600
DTINAQIDRS CRRRAQANHT ATHLLQSALK KLVDGGISQA GSLVSFDRLR FDFNCPRPLT
610 620 630 640 650 660
SSELQQVEEQ INTWIAEAHD TQIAVMGLEE AKQKGAIAMF GEKYGSEVRV IDIPSVSMEL
670 680 690 700 710 720
CGGTHVKNTA EIGLFKIISE TGIAAGIRRI EAVAGPAVLA YLNERDQVVR ALCDRFKVKP
730 740 750 760 770 780
LEIPDRITAL QSELKGTQKQ LEAVKQELAL NKSDALLSQA ESIGEFKLLV ASLGDIDANA
790 800 810 820 830 840
LMAAAERLQQ KLGEGAVILA STPAADKVSL VAAFSPRVIK DKGLQAGKFI GAIAKICAGG
850 860 870
GGGRPNLAQA GGRDASKLSE ALAKAKSQLT SSLQ