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Conserved domains on  [gi|145966899|ref|NP_080227|]
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phosphatidylinositol 4-kinase type 2-beta isoform 1 [Mus musculus]

Protein Classification

phosphatidylinositol 4-kinase( domain architecture ID 10452261)

phosphatidylinositol 4-kinase catalyzes the ATP-dependent phosphorylation of 1-phosphatidyl-1D-myo-inositol to orm 1-phosphatidyl-1D-myo-inositol 4-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 117-415 1.92e-56

Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid kinase activity and are protein kinases,.


:

Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 187.15  E-value: 1.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899  117 GSSGSYFVKDSKRN---IIGVFKPKSEEPYGQLNPKWTkyvHKVCCPCCFGRGCLLPNQGYLSEAGAYLVDVKLNLGIVP 193
Cdd:pfam00454   1 GYGGIYKVGDDLRQdelILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGENGVPP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899  194 KTKVVWLvsetfnysaidRAKSRGKKYALEKvpkvgrkFHRIGLPPKVGSFQLFVKDYKEAEYWLRRfeaeplpeniRKQ 273
Cdd:pfam00454  78 TAMVKIL-----------HSALNYPKLKLEF-------ESRISLPPKVGLLQWFVKKSPDAEEWGEA----------RKN 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899  274 FQSQFEKLVILDYIIRNTDRGNDNWLVKydemkyakkiesEESNwidnkqlliKIAAIDNGLAFpfkhPDEWRAYPFhwa 353
Cdd:pfam00454 130 FVRSCAGYSVLDYILGNGDRHLDNILVD------------KTTG---------KLFHIDFGLCL----PDAGKDLPF--- 181

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145966899  354 wlPqAKVPFsEETRNLILPY--ISDMNFVQDLCEDLYELFKTDKGFDRAAFEnqMSVMRGQILN 415
Cdd:pfam00454 182 --P-EKVPF-RLTREMVYAMgpSGDEGLFRELCETAYEALRRNLNLLTNLLK--LMVADGLPDW 239
 
Name Accession Description Interval E-value
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 117-415 1.92e-56

Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid kinase activity and are protein kinases,.


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 187.15  E-value: 1.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899  117 GSSGSYFVKDSKRN---IIGVFKPKSEEPYGQLNPKWTkyvHKVCCPCCFGRGCLLPNQGYLSEAGAYLVDVKLNLGIVP 193
Cdd:pfam00454   1 GYGGIYKVGDDLRQdelILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGENGVPP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899  194 KTKVVWLvsetfnysaidRAKSRGKKYALEKvpkvgrkFHRIGLPPKVGSFQLFVKDYKEAEYWLRRfeaeplpeniRKQ 273
Cdd:pfam00454  78 TAMVKIL-----------HSALNYPKLKLEF-------ESRISLPPKVGLLQWFVKKSPDAEEWGEA----------RKN 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899  274 FQSQFEKLVILDYIIRNTDRGNDNWLVKydemkyakkiesEESNwidnkqlliKIAAIDNGLAFpfkhPDEWRAYPFhwa 353
Cdd:pfam00454 130 FVRSCAGYSVLDYILGNGDRHLDNILVD------------KTTG---------KLFHIDFGLCL----PDAGKDLPF--- 181

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145966899  354 wlPqAKVPFsEETRNLILPY--ISDMNFVQDLCEDLYELFKTDKGFDRAAFEnqMSVMRGQILN 415
Cdd:pfam00454 182 --P-EKVPF-RLTREMVYAMgpSGDEGLFRELCETAYEALRRNLNLLTNLLK--LMVADGLPDW 239
globin_sensor cd01068
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ...
 206-285 6.49e-03

Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor single-domain globins (SSDgbs); S family; This family includes sensor domains which binds porphyrins, and other non-heme cofactors. GCSs have an N-terminal sensor domain coupled to a functional domain. For heme-bound oxygen sensing/binding globin domains, O2 binds to/dissociates from the heme iron complex inducing a structural change in the sensor domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Functional domains include DGC/GGDEF, EAL, histidine kinase, MCP, PAS, and GAF domains. Characterized members include Bacillus subtilis heme-based aerotaxis transducer (HemAT-Bs) which has a sensor domain coupled to an MCP domain. HemAT-Bs mediates an aerophilic response, and may control the movement direction of bacteria and archaea. Its MCP domain interacts with the CheA histidine kinase, a component of the CheA/CheY signal transduction system that regulates the rotational direction of flagellar motors. Another GCS having the sensor domain coupled to an MCP domain is Caulobacter crescentus McpB. McpB is encoded by a gene which lies adjacent to the major chemotaxis operon. Like McpA (encoded on this operon), McpB has three potential methylation sites, a C-terminal CheBR docking motif, and a motif needed for proteolysis via a ClpX-dependent pathway during the swarmer-to-stalked cell transition. Also included is Geobacter sulfurreducens GCS, a GCS of unknown function, in which the sensor domain is coupled to a transmembrane signal-transduction domain. Pgbs are single-domain globins of unknown function. Methanosarcina acetivorans Pgbs is dimeric and has an N-terminal extension, which together with other Pgb-specific loops, buries the heme within the protein; small ligand molecules gain access to the heme via two orthogonal apolar tunnels. Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain.


Pssm-ID: 381256 [Multi-domain]  Cd Length: 146  Bit Score: 37.17  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899 206 NYSAIDRAKSRGKKYAL------------EKVPKVGRKFHRIGLPPK--VGSFQLFVkdykeaEYWLRRFEAE--PLPEN 269
Cdd:cd01068   50 DHSTIERLKQTQRAHWLelfsgdfdeayvERRRRIGRVHVRIGLEPRwyIGAYALLL------EELIEIIAEElrKDPEE 123

                         90
                 ....*....|....*.
gi 145966899 270 IRKQFQSqFEKLVILD 285
Cdd:cd01068  124 LAELLLA-LVKALNLD 138
 
Name Accession Description Interval E-value
PI3_PI4_kinase pfam00454
Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid ...
 117-415 1.92e-56

Phosphatidylinositol 3- and 4-kinase; Some members of this family probably do not have lipid kinase activity and are protein kinases,.


Pssm-ID: 395364 [Multi-domain]  Cd Length: 241  Bit Score: 187.15  E-value: 1.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899  117 GSSGSYFVKDSKRN---IIGVFKPKSEEPYGQLNPKWTkyvHKVCCPCCFGRGCLLPNQGYLSEAGAYLVDVKLNLGIVP 193
Cdd:pfam00454   1 GYGGIYKVGDDLRQdelILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGENGVPP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899  194 KTKVVWLvsetfnysaidRAKSRGKKYALEKvpkvgrkFHRIGLPPKVGSFQLFVKDYKEAEYWLRRfeaeplpeniRKQ 273
Cdd:pfam00454  78 TAMVKIL-----------HSALNYPKLKLEF-------ESRISLPPKVGLLQWFVKKSPDAEEWGEA----------RKN 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899  274 FQSQFEKLVILDYIIRNTDRGNDNWLVKydemkyakkiesEESNwidnkqlliKIAAIDNGLAFpfkhPDEWRAYPFhwa 353
Cdd:pfam00454 130 FVRSCAGYSVLDYILGNGDRHLDNILVD------------KTTG---------KLFHIDFGLCL----PDAGKDLPF--- 181

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145966899  354 wlPqAKVPFsEETRNLILPY--ISDMNFVQDLCEDLYELFKTDKGFDRAAFEnqMSVMRGQILN 415
Cdd:pfam00454 182 --P-EKVPF-RLTREMVYAMgpSGDEGLFRELCETAYEALRRNLNLLTNLLK--LMVADGLPDW 239
globin_sensor cd01068
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ...
 206-285 6.49e-03

Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor single-domain globins (SSDgbs); S family; This family includes sensor domains which binds porphyrins, and other non-heme cofactors. GCSs have an N-terminal sensor domain coupled to a functional domain. For heme-bound oxygen sensing/binding globin domains, O2 binds to/dissociates from the heme iron complex inducing a structural change in the sensor domain, which is then transduced to the functional domain, switching on (or off) the function of the latter. Functional domains include DGC/GGDEF, EAL, histidine kinase, MCP, PAS, and GAF domains. Characterized members include Bacillus subtilis heme-based aerotaxis transducer (HemAT-Bs) which has a sensor domain coupled to an MCP domain. HemAT-Bs mediates an aerophilic response, and may control the movement direction of bacteria and archaea. Its MCP domain interacts with the CheA histidine kinase, a component of the CheA/CheY signal transduction system that regulates the rotational direction of flagellar motors. Another GCS having the sensor domain coupled to an MCP domain is Caulobacter crescentus McpB. McpB is encoded by a gene which lies adjacent to the major chemotaxis operon. Like McpA (encoded on this operon), McpB has three potential methylation sites, a C-terminal CheBR docking motif, and a motif needed for proteolysis via a ClpX-dependent pathway during the swarmer-to-stalked cell transition. Also included is Geobacter sulfurreducens GCS, a GCS of unknown function, in which the sensor domain is coupled to a transmembrane signal-transduction domain. Pgbs are single-domain globins of unknown function. Methanosarcina acetivorans Pgbs is dimeric and has an N-terminal extension, which together with other Pgb-specific loops, buries the heme within the protein; small ligand molecules gain access to the heme via two orthogonal apolar tunnels. Pgbs and other single-domain globins can function as sensors, when coupled to an appropriate regulator domain.


Pssm-ID: 381256 [Multi-domain]  Cd Length: 146  Bit Score: 37.17  E-value: 6.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145966899 206 NYSAIDRAKSRGKKYAL------------EKVPKVGRKFHRIGLPPK--VGSFQLFVkdykeaEYWLRRFEAE--PLPEN 269
Cdd:cd01068   50 DHSTIERLKQTQRAHWLelfsgdfdeayvERRRRIGRVHVRIGLEPRwyIGAYALLL------EELIEIIAEElrKDPEE 123

                         90
                 ....*....|....*.
gi 145966899 270 IRKQFQSqFEKLVILD 285
Cdd:cd01068  124 LAELLLA-LVKALNLD 138
 
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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