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 Q5QY18

Entry ID Method Resolution Chain Position Source
AF-Q5QY18-F1 Predicted AlphaFoldDB

No variants for Q5QY18

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5QY18

No associated diseases with Q5QY18

4 regional properties for Q5QY18

Type Name Position InterPro Accession
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 36 - 284 IPR005190-1
domain Glutamate-ammonia ligase adenylyltransferase, repeated domain 557 - 802 IPR005190-2
domain PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase 304 - 442 IPR013546-1
domain PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase 829 - 933 IPR013546-2

Functions

Description
EC Number 2.7.7.42 Nucleotidyltransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
[glutamate-ammonia-ligase] adenylyltransferase activity Catalysis of the reaction: ATP + [L-glutamate:ammonia ligase (ADP-forming)] = diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)].
[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase Catalysis of the reaction: adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O = AMP + [L-glutamate:ammonia ligase (ADP-forming)].
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
magnesium ion binding Binding to a magnesium (Mg) ion.

2 GO annotations of biological process

Name Definition
metabolic process The chemical reactions and pathways, including anabolism and catabolism, by which living organisms transform chemical substances. Metabolic processes typically transform small molecules, but also include macromolecular processes such as DNA repair and replication, and protein synthesis and degradation.
regulation of glutamine family amino acid metabolic process Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving amino acids of the glutamine family, comprising arginine, glutamate, glutamine and proline.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLTPDNKLMS ETETAWERYK EVVESITLTA EQEQILRALF AVSPFIGRVA ESYPEHLVTD
70 80 90 100 110 120
FFDGSGSSVR LIDADSYGDR IAESLSQVTN EDEAKKCLRR LRHCWMAKLA AADILQQVSL
130 140 150 160 170 180
KESLHHYSTF ADAAINKSLE WLFERFVQRH GKPLDANDQL MPMLVIGMGK LGGKELNFSS
190 200 210 220 230 240
DIDLIFAFPE QGETQGPGRN LEHGVFYKRL AQSLIGLLDE TTADGQVFRV DMRLRPFGQS
250 260 270 280 290 300
GPLVTSLNAL EHYYQEQGRD WERYAMVKAR MIGADEQYEQ AFQQLIRPFV YRRYIDFGAI
310 320 330 340 350 360
EALRKMKLLI TQETRRQGVK NNIKLGAGGI REVEFIVQAH QLIRGGQEKS LQTRSVYIAM
370 380 390 400 410 420
NGLVELDLID PEHARQLLKD YEYLRVIEHR LQQIDDQQTQ QLPTDETGRM RLCAMLNEPE
430 440 450 460 470 480
WETLQRKIDE CMERIHAEFQ QVVGAESEDD EDEQGLQVLW QDMLDDDAAL EIIESEGVDE
490 500 510 520 530 540
PQALWTLIKN FRQESRRRSS GPRGRSALAR LMPIMLRHAI QHQHPERLLE RLLSIIKAVM
550 560 570 580 590 600
SRTAYIELLA ENPGAREQLC KLCMASPWIS EQLALHPILL DELIDPQQLY SLPESKDYAA
610 620 630 640 650 660
VLREYLMRIP EQDLETQMDA LRQAKQALQL KIAAADISGV LELMNVSDHL SALAEAIISE
670 680 690 700 710 720
VVGLAWQHLT QKHGKPAGTC LDNTGFAVLG YGKLGGQELG YGSDLDLVFV TDANYQGQTD
730 740 750 760 770 780
GQRPIEVQQF YLRLAQRILH LFTTRTVAGI LYDVDLRLRP SGQAGLLVTQ VNSFARYLRD
790 800 810 820 830 840
DAWTWELQAL VRARPVYGVP ALRDTVMDIR RSVLSQKRDE QELRQSIVKM REKMREHLTQ
850 860 870 880 890 900
RNSRKFDLKQ DPGGIADIEF ITQYLVLRYA HKYPELCKYS DNVRLLTEAQ QLHLLTEVDA
910 920 930 940
QNLINAFQIF RCESHSLALQ GEQLLEEHNL DNERQAVLNC WNHLLEDD