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 A1SJJ3

Entry ID Method Resolution Chain Position Source
AF-A1SJJ3-F1 Predicted AlphaFoldDB

No variants for A1SJJ3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1SJJ3

No associated diseases with A1SJJ3

3 regional properties for A1SJJ3

Type Name Position InterPro Accession
conserved_site Fumarate lyase, conserved site 282 - 291 IPR020557
domain Fumarate lyase, N-terminal 13 - 307 IPR022761
domain Argininosuccinate lyase, C-terminal 370 - 438 IPR029419

Functions

Description
EC Number 6.3.4.5 Other carbon--nitrogen ligases
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
argininosuccinate synthase activity Catalysis of the reaction: ATP + L-citrulline + L-aspartate = AMP + diphosphate + (N(omega)-L-arginino)succinate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
protein homodimerization activity Binding to an identical protein to form a homodimer.

1 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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSKVLTSLPV GQRVGIAFSG GLDTSVAVAW MRDKGAIPCT YTADIGQYDE PDVSGVPARA
70 80 90 100 110 120
REYGAEIARV VDCRAQLVEE GLAALACGAF HIRSGGRIYF NTTPLGRAVT GTILVRAMHE
130 140 150 160 170 180
DGVDIWGDGS TFKGNDIERF YRYGLLANPQ LRIYKPWLDP DFVHELGGRT EMSQWLTSHG
190 200 210 220 230 240
LPYRDSQEKA YSTDANIWGA THEAKTLEHL DTSLEVVTPI MGVRFWDPAV DIATEDVTVA
250 260 270 280 290 300
FEQGRPVALN GRRFDDPVEL VEEANAIGGR HGLGMSDQIE NRIIEAKSRG VYEAPGMALL
310 320 330 340 350 360
WLTYERLMNA IHNEDTLANY QISGRRLGRL LYEGRWLDPQ ALMLRESIQR WVASVVTGEV
370 380 390 400 410 420
TVRLRRGEDY TIVRTEGPAL SYHPEKLSME RTSNSAFGPT DRIGQLTMRN LDIADSRAML
430 440 450 460 470
EMYAGQPLDQ GQVLVENGTL FGELPSGGFD QITENPEVQA EPEEEALDAA AMEAGTD