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 Q2LRK2

Entry ID Method Resolution Chain Position Source
AF-Q2LRK2-F1 Predicted AlphaFoldDB

No variants for Q2LRK2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2LRK2

No associated diseases with Q2LRK2

3 regional properties for Q2LRK2

Type Name Position InterPro Accession
domain CTP synthase, N-terminal 4 - 266 IPR017456
domain Glutamine amidotransferase 301 - 526 IPR017926
domain CTP synthase GATase domain 290 - 524 IPR033828

Functions

Description
EC Number 6.3.4.2 Other carbon--nitrogen ligases
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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
CTP synthase activity Catalysis of the reaction: ATP + UTP + glutamine + H20= ADP + phosphate + CTP + glutamate.
glutaminase activity Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH3.
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
'de novo' CTP biosynthetic process The chemical reactions and pathways resulting in the formation of cytidine 5'-triphosphate (CTP) from simpler components.
glutamine metabolic process The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRTKYIFITG GVLSSLGKGL AAASIAAVLE CRGLRVTNQK LDPYINVDPG TMSPFQHGEV
70 80 90 100 110 120
FVTDDGAETD LDLGHYERFT STRMGKSNNL TTGQVYFSVI TKERRGDYLG KTVQVIPHIT
130 140 150 160 170 180
NEIKDYIRQS SEGFDVALIE IGGTVGDIES LPFLEAIRQF RNEVGKQNAI FIHLTWVPFI
190 200 210 220 230 240
KTAGEVKTKP TQHSVKALRE IGIQPDILLC RTEEFLSEDI KAKIALFCNV EEAAVFTAKD
250 260 270 280 290 300
VSCIYEVPLI YHREGLDQKI VDLLNIWTGQ PHLEAWENVV QKITSPSYEV NIAIVGKYVN
310 320 330 340 350 360
LTDSYKSLNE ALVHGGIGND CQVNLRFVDS EKIEKDGLNH QLENVDGILV PGGFGNRGIE
370 380 390 400 410 420
GMIQVIRYAR ENKVPFFGIC LGMQMAVVEF ARHVCGLEKA NSSEFDENTP HPVIDLLPEQ
430 440 450 460 470 480
KAVQEMGASM RLGSYPCRLS DASLACEAYG EVEIGERHRH RYEFNRDYQE RLEACGLRIT
490 500 510 520 530
GRSPDGRLVE IVEIKDHPWF LGCQFHPEFK SRPTEPHPLF QRFIEAALRY RKKRAEDQ