Q3MGL3

PR
Gene name
aspS
Protein name
Aspartate--tRNA(Asp/Asn) ligase
Names
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS
Species
Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis)
KEGG Pathway
ava:Ava_0247
EC number
6.1.1.23: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-46 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q3MGL3

Entry ID Method Resolution Chain Position Source
AF-Q3MGL3-F1 Predicted AlphaFoldDB

No variants for Q3MGL3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3MGL3

No associated diseases with Q3MGL3

6 regional properties for Q3MGL3

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 143 - 583 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 37 - 122 IPR004365
domain Aminoacyl-tRNA synthetase, class II 165 - 580 IPR006195
domain GAD domain 334 - 434 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 21 - 159 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 163 - 584 IPR047090

Functions

Description
EC Number 6.1.1.23 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
aspartate-tRNA ligase activity Catalysis of the reaction: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).
aspartate-tRNA(Asn) ligase activity Catalysis of the reaction: tRNA(Asx) + L-aspartate + ATP = aspartyl-tRNA(Asx) + diphosphate + AMP.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
nucleic acid binding Binding to a nucleic acid.

1 GO annotations of biological process

Name Definition
aspartyl-tRNA aminoacylation The process of coupling aspartate to aspartyl-tRNA, catalyzed by aspartyl-tRNA synthetase. The aspartyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an aspartic acid 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
MGRLWHSLAN LARKNKLTTM RTHYCGELRQ KDIGETVTLY GWVDRRRDHG GVIFLDLRDR
70 80 90 100 110 120
SGIVQVVSDP QRTPDSYELA NSLRNEYVVE ITGRVTQRPE ESLNSRIPTG EVEIYADKIE
130 140 150 160 170 180
LLNGVRKQLP FQVSTADTET VREDLRLKYR YLDLRRDRMA RNIQLRHQVV KAMRRYLEDV
190 200 210 220 230 240
EGFIEVETPI LTRSTPEGAR DYVLPSRVNP GEWFALPQSP QLFKQILMVS GMDRYYQIAR
250 260 270 280 290 300
CFRDEDLRAD RQPEFTQLDM EMSFMSEEEI IQLNEKLVSY IFKTVKGVEL PLPFPRLTYA
310 320 330 340 350 360
EAMERYGCDK PDTRYDLQLV NVSDVMKDSG FKVFRDAVAN GGIVKILPIP NGNEQISNVR
370 380 390 400 410 420
IKPGGDLFRE ASEAGAKGLA YIRVREDGEI DTIGAIKDNL SEEQKQEILQ RTGAKPGHLL
430 440 450 460 470 480
LFGAGDAATV NKTLDRLRQA IAKEFGLIDP DKINLLWVVD FPMFEWNADE KRLEALHHPF
490 500 510 520 530 540
TAPHPDDLHD LKTARAQAYD LVFNGFEVGG GSRRIYQREV QEQVFETIGL SPEEAQNKFG
550 560 570 580 590 600
FLLEAFEYGT PPHGGIAYGL DRLVMLFAGE ESIRDVIAFP KTQQARCLLT DAPSGVDVKQ
610
LKELHVASTY KPKS