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Conserved domains on  [gi|1907188658|ref|XP_036009845|]
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type II inositol 3,4-bisphosphate 4-phosphatase isoform X4 [Mus musculus]

Protein Classification

inositol 3,4-bisphosphate 4-phosphatase family protein( domain architecture ID 10134303)

inositol 3,4-bisphosphate 4-phosphatase family protein similar to Homo sapiens type I/II inositol 3,4-bisphosphate 4-phosphatase that catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate and inositol 3,4-trisphosphate

EC:  3.1.3.66
Gene Ontology:  GO:0008289|GO:0016316
PubMed:  8976547|9632630

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 39-175 4.76e-26

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


:

Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 103.42  E-value: 4.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188658  39 PQLEFILACRDLVAPVSDRKLNTVVQISVIHPVEQTLTRYSSTEIVEGTKDPLFLTGVTFppDYPIYEETRIKLTVYDVK 118
Cdd:cd04048     1 PKVELSISCRNLLDKDVLSKSDPFVVVYVKTGGSGQWVEIGRTEVIKNNLNPDFVTTFTV--DYYFEEVQKLRFEVYDVD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907188658 119 DKSHDtirtsvlPEHKDplpevarsFLGCASFKVGELLKSKEQLLSLSLRTSDGGKV 175
Cdd:cd04048    79 SKSKD-------LSDHD--------FLGEAECTLGEIVSSPGQKLTLPLKGGKGKGT 120
 
Name Accession Description Interval E-value
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 39-175 4.76e-26

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 103.42  E-value: 4.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188658  39 PQLEFILACRDLVAPVSDRKLNTVVQISVIHPVEQTLTRYSSTEIVEGTKDPLFLTGVTFppDYPIYEETRIKLTVYDVK 118
Cdd:cd04048     1 PKVELSISCRNLLDKDVLSKSDPFVVVYVKTGGSGQWVEIGRTEVIKNNLNPDFVTTFTV--DYYFEEVQKLRFEVYDVD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907188658 119 DKSHDtirtsvlPEHKDplpevarsFLGCASFKVGELLKSKEQLLSLSLRTSDGGKV 175
Cdd:cd04048    79 SKSKD-------LSDHD--------FLGEAECTLGEIVSSPGQKLTLPLKGGKGKGT 120
 
Name Accession Description Interval E-value
C2A_Copine cd04048
C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a ...
 39-175 4.76e-26

C2 domain first repeat in Copine; There are 2 copies of the C2 domain present in copine, a protein involved in membrane trafficking, protein-protein interactions, and perhaps even cell division and growth. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176013 [Multi-domain]  Cd Length: 120  Bit Score: 103.42  E-value: 4.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188658  39 PQLEFILACRDLVAPVSDRKLNTVVQISVIHPVEQTLTRYSSTEIVEGTKDPLFLTGVTFppDYPIYEETRIKLTVYDVK 118
Cdd:cd04048     1 PKVELSISCRNLLDKDVLSKSDPFVVVYVKTGGSGQWVEIGRTEVIKNNLNPDFVTTFTV--DYYFEEVQKLRFEVYDVD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907188658 119 DKSHDtirtsvlPEHKDplpevarsFLGCASFKVGELLKSKEQLLSLSLRTSDGGKV 175
Cdd:cd04048    79 SKSKD-------LSDHD--------FLGEAECTLGEIVSSPGQKLTLPLKGGKGKGT 120
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 44-160 7.59e-03

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 37.05  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188658  44 ILACRDLVAPVSDRKLNTVVQISVIHPVEQTltryssTEIVEGTKDPLFltGVTFPPDYPIYEETRIKLTVYDVKDKSHD 123
Cdd:cd00030     5 VIEARNLPAKDLNGKSDPYVKVSLGGKQKFK------TKVVKNTLNPVW--NETFEFPVLDPESDTLTVEVWDKDRFSKD 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1907188658 124 TirtsvlpehkdplpevarsFLGCASFKVGELLKSKE 160
Cdd:cd00030    77 D-------------------FLGEVEIPLSELLDSGK 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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