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 Q971C1

Entry ID Method Resolution Chain Position Source
AF-Q971C1-F1 Predicted AlphaFoldDB

No variants for Q971C1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q971C1

No associated diseases with Q971C1

4 regional properties for Q971C1

Type Name Position InterPro Accession
domain Anticodon-binding 333 - 426 IPR004154
domain Aminoacyl-tRNA synthetase, class II 25 - 328 IPR006195
domain Histidyl-anticodon-binding 330 - 425 IPR033656
domain Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain 13 - 318 IPR041715

Functions

Description
EC Number 6.1.1.10 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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
methionine-tRNA ligase activity Catalysis of the reaction: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).

1 GO annotations of biological process

Name Definition
methionyl-tRNA aminoacylation The process of coupling methionine to methionyl-tRNA, catalyzed by methionyl-tRNA synthetase. The methionyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a methionine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKIFVASAWP YVNAVPHLGN LIGSVLSADV FARYARLKYG QENVVFVSGS DEHGTPIEVE
70 80 90 100 110 120
AKKRNVNPKE LTDQAHEYDK KLFLDVWEIS YNNYTRTESE IHKTFVRDFM LKLEKYIKIE
130 140 150 160 170 180
EDEIPYCEYD KIYLPDRFVK GTCPYCGFED ARGDQCDNCG RLLTPRLLVN PKCVLCGRTP
190 200 210 220 230 240
VFKKTKHWFF DLSAFNDKIE EWIKNSQTLP ENVKSVALSW VKEGLKPRSI TRDNAWGIPA
250 260 270 280 290 300
PFEGAEGKTI YVWFEALLGY ISATIEYFKK IGKEEEWKKF WFGNDVKSYY FIGKDNIPFH
310 320 330 340 350 360
AVILPAMLMA SGENYVLPTV IAATEYLLYE GQKFSKSRKI GVWIDEAPQL LDIEYWRFIL
370 380 390 400 410 420
IRLRPEERDT NFTWREALRI VNTELNDDIG NYANRVLSMV RRYFNGEVPQ IKYEKLKDED
430 440 450 460 470 480
TKFISEIKEA PKKMSELFEL GKLKAGSEEI LKLARNGNSY LNIRAPWNLI KNDKEEAGNV
490 500 510 520 530 540
LNIAVNSLRT LSIMLYPLMP KSAEKLYNML GFKDIEREKW DLAGELVIKS NHKINEVSVL
550 560 570
FKKVELNEND INKKLDEIRK NLEKIRPTLL R