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 P18185

Entry ID Method Resolution Chain Position Source
AF-P18185-F1 Predicted AlphaFoldDB

No variants for P18185

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P18185

No associated diseases with P18185

13 regional properties for P18185

Type Name Position InterPro Accession
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 128 - 333 IPR005479-1
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 670 - 868 IPR005479-2
domain Carbamoyl-phosphate synthetase, large subunit oligomerisation domain 420 - 542 IPR005480
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 19 - 33 IPR005483-1
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 48 - 58 IPR005483-2
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 168 - 180 IPR005483-3
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 204 - 223 IPR005483-4
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 239 - 256 IPR005483-5
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 296 - 325 IPR005483-6
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 378 - 396 IPR005483-7
domain Methylglyoxal synthase-like domain 925 - 1027 IPR011607
domain ATP-grasp fold 133 - 327 IPR011761-1
domain ATP-grasp fold 675 - 863 IPR011761-2

Functions

Description
EC Number 6.3.4.16 Other carbon--nitrogen ligases
Subcellular Localization
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.
carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: 2 ATP + L-glutamine + CO2 + H2O = 2 ADP + phosphate + glutamate + carbamoyl phosphate.
metal ion binding Binding to a metal ion.

4 GO annotations of biological process

Name Definition
arginine biosynthetic process The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
glutamine metabolic process The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.
nitrogen compound metabolic process The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.
pyrimidine nucleotide biosynthetic process The chemical reactions and pathways resulting in the formation of a pyrimidine nucleotide, a compound consisting of nucleoside (a pyrimidine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPKDTSISSI LVIGSGPIII GQAAEFDYSG TQGCIALKEE GYRVILVNSN PATIMTDEAF
70 80 90 100 110 120
ADEIYFEPLT AESLTAIIKK ERPDGLLANL GGQTALNLAV ELEETGVLKE HGVKLLGTSV
130 140 150 160 170 180
ETIQKGEDRE KFRSLMNELK QPVPESEIVD NEADALHFAE SIGFPVIIRP AYTLGGKGGG
190 200 210 220 230 240
IAPDKEAFTA MIKQALLASP INQCLVEKSI AGFKEIEYEV MRDSNNTCIT VCNMENIDPV
250 260 270 280 290 300
GVHTGDSIVV APSQTLTDED YQMLRTASLT IISALDVVGG CNIQFALDPF SKQYYVIEVN
310 320 330 340 350 360
PRVSRSSALA SKATGYPIAK MAAKLAVGYT LDELKNPLTG STYASFEPAL DYVIVKFPRW
370 380 390 400 410 420
PFDKFKNADR KLGTKMKATG EVMAIERNLE AAIQKAAASL ELKNIGTHLP ELSGLSIDTL
430 440 450 460 470 480
WDLAITPDDR RFFVVMELLS RSVSIDDIHE KTKIDPFFLH TFDNIIKLEN RLMEAGSDLS
490 500 510 520 530 540
FELLKKAKEK GFSDATIASL ISKTEEEVRA LRKEMGITPS FKIVDTCAAE FDAKTNYFYS
550 560 570 580 590 600
TYFGETDGDI SRKEKKRALI IGSGPIRIGQ GVEFDYSAVH GVLTLQELGF ETIMINNNPE
610 620 630 640 650 660
TVSTDYEIAD RLYFEPMTTE HIVNVAEQEN IDFAIVQFGG QTAINAAEAL EKAGITLLGT
670 680 690 700 710 720
SFQTLDVLED RDQFYQLLDE LGLKHAKGEI AYTKEEAASK ASEIGYPVLI RPSYVIGGMG
730 740 750 760 770 780
MIIVDSQAQL SQLLNDEDSM PYPILIDQYV SGKEVEIDLI SDGEEVFIPT YTEHIERAGV
790 800 810 820 830 840
HSGDSFAILP GPSITSGLQQ GMKDAAQKIA RKLSFKGIMN IQFVIDNGNI LVLEVNPRAS
850 860 870 880 890 900
RTVPVVSKVM GVPMIPLATR LLAGASLKDL NPAVQNHHGV AVKFPVFSSH AIQDVDVKLG
910 920 930 940 950 960
PEMKSTGEGM CVAYDSNSAL KKIYTRVWSQ KGSIYLQNVP EDVKELAENA GFTIHEGTFA
970 980 990 1000 1010 1020
SWMEQEGNSL HINLSGSEEA RKERLEAMTH GIPVFTEEET VRAFLQSGSG HPQPVSLKDL
YKKEVASCTQ