The domain within your query sequence starts at position 1070 and ends at position 1149; the E-value for the IPT domain shown below is 6.13e-14.
NPVITAISPGRSPVSGGRTITVAGERFHMVQNVSMAVHHIGREPTFCKVLNSTLITCPSP GALSNASAPVDFFINGRAYA
IPTig-like, plexins, transcription factors |
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SMART accession number: | SM00429 |
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Description: | - |
Interpro abstract (IPR002909): | The IPT (Ig-like, plexins, transcription factors) domain has an immunoglobulin like fold [ (PUBMED:10390613) ]. These domains are found in cell surface receptors such as Met and Ron as well as in intracellular transcription factors where it is involved in DNA binding. The Ron tyrosine kinase receptor shares with the members of its subfamily (Met and Sea) a unique functional feature: the control of cell dissociation, motility, and invasion of extracellular matrices (scattering) [ (PUBMED:8816464) ]. |
Family alignment: |
There are 37987 IPT domains in 14790 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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Taxonomic distribution of proteins containing IPT domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with IPT domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing IPT domain in the selected taxonomic class.
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Aravind L, Koonin EV
- Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches.
- J Mol Biol. 1999; 287: 1023-40
- Display abstract
Using a number of diverse protein families as test cases, we investigate the ability of the recently developed iterative sequence database search method, PSI-BLAST, to identify subtle relationships between proteins that originally have been deemed detectable only at the level of structure-structure comparison. We show that PSI-BLAST can detect many, though not all, of such relationships, but the success critically depends on the optimal choice of the query sequence used to initiate the search. Generally, there is a correlation between the diversity of the sequences detected in the first pass of database screening and the ability of a given query to detect subtle relationships in subsequent iterations. Accordingly, a thorough analysis of protein superfamilies at the sequence level is necessary in order to maximize the chances of gleaning non-trivial structural and functional inferences, as opposed to a single search, initiated, for example, with the sequence of a protein whose structure is available. This strategy is illustrated by several findings, each of which involves an unexpected structural prediction: (i) a number of previously undetected proteins with the HSP70-actin fold are identified, including a highly conserved and nearly ubiquitous family of metal-dependent proteases (typified by bacterial O-sialoglycoprotease) that represent an adaptation of this fold to a new type of enzymatic activity; (ii) we show that, contrary to the previous conclusions, ATP-dependent and NAD-dependent DNA ligases are confidently predicted to possess the same fold; (iii) the C-terminal domain of 3-phosphoglycerate dehydrogenase, which binds serine and is involved in allosteric regulation of the enzyme activity, is shown to typify a new superfamily of ligand-binding, regulatory domains found primarily in enzymes and regulators of amino acid and purine metabolism; (iv) the immunoglobulin-like DNA-binding domain previously identified in the structures of transcription factors NFkappaB and NFAT is shown to be a member of a distinct superfamily of intracellular and extracellular domains with the immunoglobulin fold; and (v) the Rag-2 subunit of the V-D-J recombinase is shown to contain a kelch-type beta-propeller domain which rules out its evolutionary relationship with bacterial transposases.
- Metabolism (metabolic pathways involving proteins which contain this domain)
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% proteins involved KEGG pathway ID Description 14.26 map04360 Axon guidance 8.56 map04662 B cell receptor signaling pathway 8.56 map04660 T cell receptor signaling pathway 5.87 map04370 VEGF signaling pathway 5.87 map04310 Wnt signaling pathway 5.87 map04650 Natural killer cell mediated cytotoxicity 5.70 map05120 Epithelial cell signaling in Helicobacter pylori infection 4.19 map05222 Small cell lung cancer 4.19 map04620 Toll-like receptor signaling pathway 4.19 map05212 Pancreatic cancer 4.19 map04210 Apoptosis 4.19 map05220 Chronic myeloid leukemia 4.19 map04920 Adipocytokine signaling pathway 4.19 map05215 Prostate cancer 4.19 map05221 Acute myeloid leukemia 2.68 map04010 MAPK signaling pathway 1.51 map04520 Adherens junction 1.51 map04060 Cytokine-cytokine receptor interaction 1.51 map05210 Colorectal cancer 1.51 map04510 Focal adhesion 1.51 map05211 Renal cell carcinoma 1.51 map05218 Melanoma This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with IPT domain which could be assigned to a KEGG orthologous group, and not all proteins containing IPT domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.
- Structure (3D structures containing this domain)
3D Structures of IPT domains in PDB
PDB code Main view Title 1a02 STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA 1a3q HUMAN NF-KAPPA-B P52 BOUND TO DNA 1bfs STRUCTURE OF NF-KB P50 HOMODIMER BOUND TO A KB SITE 1bft STRUCTURE OF NF-KB P50 HOMODIMER BOUND TO A KB SITE 1gji Crystal structure of c-Rel bound to DNA 1ikn IKAPPABALPHA/NF-KAPPAB COMPLEX 1imh TonEBP/DNA COMPLEX 1k3z X-ray crystal structure of the IkBb/NF-kB p65 homodimer complex 1le5 Crystal structure of a NF-kB heterodimer bound to an IFNb-kB 1le9 Crystal structure of a NF-kB heterodimer bound to the Ig/HIV-kB siti 1lei The kB DNA sequence from the HLV-LTR functions as an allosteric regulator of HIV transcription 1my5 NF-kappaB p65 subunit dimerization domain homodimer 1my7 NF-kappaB p65 subunit dimerization domain homodimer N202R mutation 1nfi I-KAPPA-B-ALPHA/NF-KAPPA-B COMPLEX 1nfk STRUCTURE OF THE NUCLEAR FACTOR KAPPA-B (NF-KB) P50 HOMODIMER 1ooa CRYSTAL STRUCTURE OF NF-kB(p50)2 COMPLEXED TO A HIGH-AFFINITY RNA APTAMER 1owr CRYSTAL STRUCTURE OF HUMAN NFAT1 BOUND MONOMERICALLY TO DNA 1oy3 CRYSTAL STRUCTURE OF AN IKBBETA/NF-KB P65 HOMODIMER COMPLEX 1p7h Structure of NFAT1 bound as a dimer to the HIV-1 LTR kB element 1pzu An asymmetric NFAT1-RHR homodimer on a pseudo-palindromic, Kappa-B site 1qho FIVE-DOMAIN ALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX 1qhp FIVE-DOMAIN ALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE COMPLEX 1ram A NOVEL DNA RECOGNITION MODE BY NF-KB P65 HOMODIMER 1s9k Crystal Structure of Human NFAT1 and Fos-Jun on the IL-2 ARRE1 Site 1svc NFKB P50 HOMODIMER BOUND TO DNA 1u36 Crystal stucture of WLAC mutant of dimerisation domain of NF-kB p50 transcription factor 1u3j Crystal stucture of MLAV mutant of dimerisation domain of NF-kB p50 transcription factor 1u3y Crystal stucture of ILAC mutant of dimerisation domain of NF-kB p50 transcription factor 1u3z Crystal stucture of MLAC mutant of dimerisation domain of NF-kB p50 transcription factor 1u41 Crystal stucture of YLGV mutant of dimerisation domain of NF-kB p50 transcription factor 1u42 Crystal stucture of MLAM mutant of dimerisation domain of NF-kB p50 transcription factor 1vkx CRYSTAL STRUCTURE OF THE NFKB P50/P65 HETERODIMER COMPLEXED TO THE IMMUNOGLOBULIN KB DNA 1zk9 NF-kB RelB forms an intertwined homodimer 1zka NF-kB RelB forms an intertwined homodimer, Y300S mutant 2as5 Structure of the DNA binding domains of NFAT and FOXP2 bound specifically to DNA. 2i9t Structure of NF-kB p65-p50 heterodimer bound to PRDII element of B-interferon promoter 2o61 Crystal Structure of NFkB, IRF7, IRF3 bound to the interferon-b enhancer 2o93 Crystal structure of NFAT bound to the HIV-1 LTR tandem kappaB enhancer element 2ram A NOVEL DNA RECOGNITION MODE BY NF-KB P65 HOMODIMER 2uzx Structure of the human receptor tyrosine kinase Met in complex with the Listeria monocytogenes invasion protein InlB: Crystal form I 2uzy Structure of the human receptor tyrosine kinase Met in complex with the Listeria monocytogenes invasion protein inlb: low resolution, Crystal form II 2v2t X-ray structure of a NF-kB p50-RelB-DNA complex 2yrp Solution structure of the TIG domain from Human Nuclear factor of activated T-cells, cytoplasmic 4 3do7 X-ray structure of a NF-kB p52/RelB/DNA complex 3gut Crystal structure of a higher-order complex of p50:RelA bound to the HIV-1 LTR 3jss Crystal structure of a mutant RelB dimerization domain 3juz Crystal structure of a mutant of RelB dimerization domain(M5) 3jv0 Crystal structure of a mutant of RelB dimerization domain(M6) 3jv4 Crystal structure of the dimerization domains p50 and RelB 3jv5 Crystal structure of the dimerization domains p52 homodimer 3jv6 Crystal structure of the dimerization domains p52 and RelB 3kya Crystal structure of Putative phosphatase (NP_812416.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.77 A resolution 3mlp Early B-cell Factor 1 (Ebf1) bound to DNA 3mqi Human early B-cell factor 1 (EBF1) IPT/TIG domain 3muj Early B-cell factor 3 (EBF3) IPT/TIG and dimerization helices 3n50 Human Early B-cell factor 3 (EBF3) IPT/TIG and HLHLH domains 3qrf Structure of a domain-swapped FOXP3 dimer 3tc9 Crystal structure of a Hypothetical hydrolase (BT_3476) from Bacteroides thetaiotaomicron VPI-5482 at 2.23 A resolution 4hw6 Crystal structure of a hypothetical protein (BACOVA_00264) from Bacteroides ovatus ATCC 8483 at 1.70 A resolution 4jgm Crystal structure of RelB double mutants: Y300F/I335V 4jhb Crystal structure of RelB double mutants: Y300F/I335F 4qt8 4QT8 5l56 5L56 5l59 5L59 5l5c 5L5C 5l5g 5L5G 5l5k 5L5K 5l5l 5L5L 5l5m 5L5M 5l5n 5L5N - Links (links to other resources describing this domain)
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INTERPRO IPR002909