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 Q8TNY4

Entry ID Method Resolution Chain Position Source
AF-Q8TNY4-F1 Predicted AlphaFoldDB

No variants for Q8TNY4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8TNY4

No associated diseases with Q8TNY4

14 regional properties for Q8TNY4

Type Name Position InterPro Accession
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 128 - 331 IPR005479-1
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 667 - 869 IPR005479-2
domain Carbamoyl-phosphate synthetase, large subunit oligomerisation domain 414 - 534 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 294 - 323 IPR005483-6
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 376 - 394 IPR005483-7
domain Methylglyoxal synthase-like domain 930 - 1070 IPR011607
domain ATP-grasp fold 133 - 325 IPR011761-1
domain ATP-grasp fold 672 - 863 IPR011761-2
domain Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain 936 - 1038 IPR033937

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
'de novo' UMP biosynthetic process The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD(+) or oxygen.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPKREDIKKV LLIGSGPITI GQAAEFDFSG SQACRSLKEE GVQVVLVNSN PATIMTDPEM
70 80 90 100 110 120
ADSVYIEPLD ARIVEKIIEK ERPDGIIAGI GGQTGLNITS ELAEMGVFEK YGVQILGTPV
130 140 150 160 170 180
EAIKNTEDRE LFKETMLRIG EKVPQSRAVH TLKEAEEVVE ELGLPLIVRP AYTLGGAGGG
190 200 210 220 230 240
IARTKEELLE ITERGLRRSR ISQVLIEESV LGWAEVEYEV MRDANDTCIV ICNMENIDPM
250 260 270 280 290 300
GVHTGESAVV APSQTLTDAE HQMLRSASIK IIRALKIEGG CNIQYALKEG DYRIVEVNPR
310 320 330 340 350 360
VSRSSALASK ATGYPIARVT AKIAIGMALD EIINSVTKNT PASFEPALDY VITKIPRWPF
370 380 390 400 410 420
DKFVTADKTL TTAMKSTGEI MAIGRTMEES LLKAFKSLDI DSQLGNKRWD EHEVKTLLKT
430 440 450 460 470 480
PTSERLFVIF HALERGMSVK EIAELTSINP FFISKIKKIV EMEKRIRTEE LTSELLREVK
490 500 510 520 530 540
KLGFPDTRLA ELTGKTREQI SDLRHDAGIL ATFKMVDTCA AEFQAATPYY YSTYEDTCET
550 560 570 580 590 600
NPTDRKKILI LGAGPIRIGQ GIEFDYCTVH AVTALREEGI ETHIINNNPE TVSTDFDTSD
610 620 630 640 650 660
KLFFEPLTME YVMNVIERER PDGVLVQFGG QTSVNLALPL KKELKRRTDL DTMIMGTDPE
670 680 690 700 710 720
DMDLAEDREK FYVLMQKFGI LQPEGGYATS QHEAIEVAQR IGFPVLVRPS YVLGGRAMEI
730 740 750 760 770 780
VYDEIDLERY MKEAVRVSPE HPILIDDFLE GACEIDVDAV CDRKDVLIGA IMEHIEEAGV
790 800 810 820 830 840
HSGDSACVIP PQSLSEDVLA QVRDYTRKIA LGLRVKGLIN IQMAEKGGKV FVLEANPRSS
850 860 870 880 890 900
RTIPFVSKAV GLPLAKIAAR VIAGHSLKEM GYTDEPKPKH VSIKEVLLPF DKLPGADPVL
910 920 930 940 950 960
GPEMKSTGEV MGIDYDFGRA YYKAELAADN LLPLTGKVFL SIRNADKPEL VEVARKLQAA
970 980 990 1000 1010 1020
GLELMGTRGT VNYLAQHGVF MDTVKKVHDG SPNVIDMMRR DEVDLIINTP TSKQSRRDGS
1030 1040 1050 1060
RIRRAAVDFK VPYITTIQAA SAAAAAIETM KKGEDLTIKS INEYHKEMGL