C4ZI12

PR
Gene name
aspS
Protein name
Aspartate--tRNA ligase
Names
Aspartyl-tRNA synthetase, AspRS
Species
Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / VPI 0990) (Eubacterium rectale)
KEGG Pathway
ere:EUBREC_2920
EC number
6.1.1.12: 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)

542-598 (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 C4ZI12

Entry ID Method Resolution Chain Position Source
AF-C4ZI12-F1 Predicted AlphaFoldDB

No variants for C4ZI12

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C4ZI12

No associated diseases with C4ZI12

6 regional properties for C4ZI12

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (D/K/N) 128 - 565 IPR004364
domain OB-fold nucleic acid binding domain, AA-tRNA synthetase-type 26 - 111 IPR004365
domain Aminoacyl-tRNA synthetase, class II 149 - 563 IPR006195
domain GAD domain 319 - 412 IPR029351
domain Aspartate-tRNA ligase, type 1, anticodon recognition domain 10 - 144 IPR047089
domain Aspartate-tRNA ligase, type 1, core domain 149 - 564 IPR047090

Functions

Description
EC Number 6.1.1.12 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.

3 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).
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
MAESMQGLHR SHRCTEVSNA NIGEKVTVMG WVQKRRNLGS LIFVDLRDRS GILQIVFGEE
70 80 90 100 110 120
NVGAEGFEKA GTLRSEFVIA VEGTVQKRTA AVNESLKTGD IEVIATSIRV LSEAQTPPFH
130 140 150 160 170 180
IEENSKTSED IRLKYRYLDL RRPDIQRNLM LRSNVLRVMR DFMANEGFLE IETPILCKST
190 200 210 220 230 240
PEGARDYLVP SRIHHGHFYA LPQSPQLFKQ LLMASGYDRY FQIARCFRDE DLRADRQPEF
250 260 270 280 290 300
TQADMELSFV DIDDVIEVNE RLLKHLFKEV INVDVEIPFK RMPWQEAMDR FGSDKPDTRF
310 320 330 340 350 360
GMELCDVSEV VKDCGFGVFT GALENGGSVR GINVEGQAKM PRKKIDKLVE HAKGCGAKGL
370 380 390 400 410 420
AYLCINEDGT YKSSFAKFMT EAELDALVAK MNGKPGDLLL FAADKNKIVW NVLGALRLML
430 440 450 460 470 480
GAELGLIDEN KYNFLWVTEF PLLEWSDEEN RFMAMHHPFT MPMEEDWDKI DSDPGAVRAK
490 500 510 520 530 540
AYDIVLNGTE LGGGSVRIHQ DDIQEKMFEV LGFTKERAHE QFGFLLDAFS YGVPPHAGLA
550 560 570 580 590
FGVDRICMHM LHTDNIKEVI AFPKVKDASD LMSEAPGTVD PKQLEELGIA VAAEEDEE