Descriptions

Signal transduction ATPase with numerous domains (STANDs), initially in monomeric resting forms, multimerize into large hubs that activate target macromolecules. Autoinhibitory interactions maintain the STAND conserved core (the NOD) closed in the absence of an inducer. The NOD module comprises three domains including nucleotide-binding domain, the helical domain, and the winged-helix domain. In resting STAND proteins with a TPR sensor domain, the sensor domain establishes interactions with the NOD that strengthens the arm-based autoinhibition of STAND proteins. The interactions are disrupted in the multimerization-competent forms upon addition of its inducer. Similar interactions exist in a well-characterized STAND homolog of PH0952, MalT from Escherichia coli, contributing to its autoinhibition.

Autoinhibitory domains (AIDs)

Target domain

6-232 (Nucleotide-binding domain, NBD)

Relief mechanism

Ligand binding

Assay

Mutagenesis experiment

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

2 structures for P06993

Entry ID Method Resolution Chain Position Source
1HZ4 X-ray 145 A A 437-806 PDB
AF-P06993-F1 Predicted AlphaFoldDB

No variants for P06993

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P06993

No associated diseases with P06993

9 regional properties for P06993

Type Name Position InterPro Accession
domain Protein kinase domain 513 - 784 IPR000719
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 515 - 784 IPR001245
repeat Leucine-rich repeat 92 - 150 IPR001611
conserved_site Tyrosine-protein kinase, receptor class II, conserved site 677 - 685 IPR002011
domain Immunoglobulin-like domain 196 - 285 IPR007110
active_site Tyrosine-protein kinase, active site 649 - 661 IPR008266
binding_site Protein kinase, ATP binding site 519 - 547 IPR017441
domain Tyrosine-protein kinase, catalytic domain 513 - 784 IPR020635
domain Growth factor receptor NTRK, leucine rich repeat C-terminal 151 - 194 IPR031635

Functions

Description
EC Number
Subcellular Localization
PANTHER Family PTHR44688 FAMILY NOT NAMED
PANTHER Subfamily PTHR44688:SF7 HTH-TYPE TRANSCRIPTIONAL REGULATOR MALT
PANTHER Protein Class helix-turn-helix transcription factor
winged helix/forkhead transcription factor
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
DNA-binding transcription factor activity A transcription regulator activity that modulates transcription of gene sets via selective and non-covalent binding to a specific double-stranded genomic DNA sequence (sometimes referred to as a motif) within a cis-regulatory region. Regulatory regions include promoters (proximal and distal) and enhancers. Genes are transcriptional units, and include bacterial operons.
identical protein binding Binding to an identical protein or proteins.
trisaccharide binding Binding to a trisaccharide. Trisaccharides are sugars composed of three monosaccharide units.

3 GO annotations of biological process

Name Definition
carbohydrate metabolic process The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
positive regulation of carbohydrate metabolic process Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways involving carbohydrate.
positive regulation of DNA-templated transcription Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLIPSKLSRP VRLDHTVVRE RLLAKLSGAN NFRLALITSP AGYGKTTLIS QWAAGKNDIG
70 80 90 100 110 120
WYSLDEGDNQ QERFASYLIA AVQQATNGHC AICETMAQKR QYASLTSLFA QLFIELAEWH
130 140 150 160 170 180
SPLYLVIDDY HLITNPVIHE SMRFFIRHQP ENLTLVVLSR NLPQLGIANL RVRDQLLEIG
190 200 210 220 230 240
SQQLAFTHQE AKQFFDCRLS SPIEAAESSR ICDDVSGWAT ALQLIALSAR QNTHSAHKSA
250 260 270 280 290 300
RRLAGINASH LSDYLVDEVL DNVDLATRHF LLKSAILRSM NDALITRVTG EENGQMRLEE
310 320 330 340 350 360
IERQGLFLQR MDDTGEWFCY HPLFGNFLRQ RCQWELAAEL PEIHRAAAES WMAQGFPSEA
370 380 390 400 410 420
IHHALAAGDA LMLRDILLNH AWSLFNHSEL SLLEESLKAL PWDSLLENPQ LVLLQAWLMQ
430 440 450 460 470 480
SQHRYGEVNT LLARAEHEIK DIREDTMHAE FNALRAQVAI NDGNPDEAER LAKLALEELP
490 500 510 520 530 540
PGWFYSRIVA TSVLGEVLHC KGELTRSLAL MQQTEQMARQ HDVWHYALWS LIQQSEILFA
550 560 570 580 590 600
QGFLQTAWET QEKAFQLINE QHLEQLPMHE FLVRIRAQLL WAWARLDEAE ASARSGIEVL
610 620 630 640 650 660
SSYQPQQQLQ CLAMLIQCSL ARGDLDNARS QLNRLENLLG NGKYHSDWIS NANKVRVIYW
670 680 690 700 710 720
QMTGDKAAAA NWLRHTAKPE FANNHFLQGQ WRNIARAQIL LGEFEPAEIV LEELNENARS
730 740 750 760 770 780
LRLMSDLNRN LLLLNQLYWQ AGRKSDAQRV LLDALKLANR TGFISHFVIE GEAMAQQLRQ
790 800 810 820 830 840
LIQLNTLPEL EQHRAQRILR EINQHHRHKF AHFDENFVER LLNHPEVPEL IRTSPLTQRE
850 860 870 880 890 900
WQVLGLIYSG YSNEQIAGEL EVAATTIKTH IRNLYQKLGV AHRQDAVQHA QQLLKMMGYG
V