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Conserved domains on  [gi|73920064|sp|Q6P1Y8|]
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RecName: Full=Type II inositol 3,4-bisphosphate 4-phosphatase; AltName: Full=Inositol polyphosphate 4-phosphatase type II

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 ...
 39-158 4.85e-28

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: 109.20  E-value: 4.85e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920064  39 PQLEFILACRDLVAPVSDRKLNTVVQISVIHPVEQTLTRYSSTEIVEGTKDPLFLTGVTFppDYPIYEETRIKLTVYDVK 118
Cdd:cd04048   1 PKVELSISCRNLLDKDVLSKSDPFVVVYVKTGGSGQWVEIGRTEVIKNNLNPDFVTTFTV--DYYFEEVQKLRFEVYDVD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 73920064 119 DKSHD--TRSFLGCASFKVGELLKSKEQLLSLSLRTSDGGKV 158
Cdd:cd04048  79 SKSKDlsDHDFLGEAECTLGEIVSSPGQKLTLPLKGGKGKGT 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 ...
 39-158 4.85e-28

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: 109.20  E-value: 4.85e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920064  39 PQLEFILACRDLVAPVSDRKLNTVVQISVIHPVEQTLTRYSSTEIVEGTKDPLFLTGVTFppDYPIYEETRIKLTVYDVK 118
Cdd:cd04048   1 PKVELSISCRNLLDKDVLSKSDPFVVVYVKTGGSGQWVEIGRTEVIKNNLNPDFVTTFTV--DYYFEEVQKLRFEVYDVD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 73920064 119 DKSHD--TRSFLGCASFKVGELLKSKEQLLSLSLRTSDGGKV 158
Cdd:cd04048  79 SKSKDlsDHDFLGEAECTLGEIVSSPGQKLTLPLKGGKGKGT 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 ...
 39-158 4.85e-28

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: 109.20  E-value: 4.85e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920064  39 PQLEFILACRDLVAPVSDRKLNTVVQISVIHPVEQTLTRYSSTEIVEGTKDPLFLTGVTFppDYPIYEETRIKLTVYDVK 118
Cdd:cd04048   1 PKVELSISCRNLLDKDVLSKSDPFVVVYVKTGGSGQWVEIGRTEVIKNNLNPDFVTTFTV--DYYFEEVQKLRFEVYDVD 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 73920064 119 DKSHD--TRSFLGCASFKVGELLKSKEQLLSLSLRTSDGGKV 158
Cdd:cd04048  79 SKSKDlsDHDFLGEAECTLGEIVSSPGQKLTLPLKGGKGKGT 120
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
 44-143 3.53e-05

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: 43.59  E-value: 3.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920064  44 ILACRDLVAPVSDRKLNTVVQISVIHPVEQTltryssTEIVEGTKDPLFltGVTFPPDYPIYEETRIKLTVYDVKDKSHD 123
Cdd:cd00030   5 VIEARNLPAKDLNGKSDPYVKVSLGGKQKFK------TKVVKNTLNPVW--NETFEFPVLDPESDTLTVEVWDKDRFSKD 76

                        90       100
                ....*....|....*....|
gi 73920064 124 TrsFLGCASFKVGELLKSKE 143
Cdd:cd00030  77 D--FLGEVEIPLSELLDSGK 94
C2_RGS-like cd08685
C2 domain of the Regulator Of G-Protein Signaling (RGS) family; This CD contains members of ...
 60-143 1.11e-03

C2 domain of the Regulator Of G-Protein Signaling (RGS) family; This CD contains members of the regulator of G-protein signaling (RGS) family. RGS is a GTPase activating protein which inhibits G-protein mediated signal transduction. The protein is largely cytosolic, but G-protein activation leads to translocation of this protein to the plasma membrane. A nuclear form of this protein has also been described, but its sequence has not been identified. There are multiple alternatively spliced transcript variants in this family with some members having additional domains (ex. PDZ and RGS) downstream of the 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: 176067 [Multi-domain]  Cd Length: 119  Bit Score: 39.74  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920064  60 NTVVQISVIhPvEQTLTRYSSTEIVEGTKDPLFLTGVTFPpdypIYEE---TRIKLTVYDVKDKSHDTrSFLGCASFKVG 136
Cdd:cd08685  33 NSYVKISLS-P-DKEVRFRQKTSTVPDSANPLFHETFSFD----VNERdyqKRLLVTVWNKLSKSRDS-GLLGCMSFGVK 105


                ....*..
gi 73920064 137 ELLKSKE 143
Cdd:cd08685 106 SIVNQKE 112
C2_Smurf-like cd08382
C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 ...
 72-166 3.66e-03

C2 domain present in Smad ubiquitination-related factor (Smurf)-like proteins; A single C2 domain is found in Smurf proteins, C2-WW-HECT-domain E3s, which play an important role in the downregulation of the TGF-beta signaling pathway. Smurf proteins also regulate cell shape, motility, and polarity by degrading small guanosine triphosphatases (GTPases). 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. Members here have type-II topology.


Pssm-ID: 176028 [Multi-domain]  Cd Length: 123  Bit Score: 38.44  E-value: 3.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920064  72 EQTltrySSTEIVEGTKDPLFLTgvTFppDYPIYEETRIKLTVYDVKDKSHDTRSFLGCASFKVGELLKSK----EQLLS 147
Cdd:cd08382  32 GQT----HSTDVAKKTLDPKWNE--HF--DLTVGPSSIITIQVFDQKKFKKKDQGFLGCVRIRANAVLPLKdtgyQRLDL 103

                        90
                ....*....|....*....
gi 73920064 148 LSLRTSDGGKVVGTIEVSL 166
Cdd:cd08382 104 RKLKKSDNLSVRGKIVVSL 122
 
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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