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Conserved domains on  [gi|1958676003|ref|XP_038947868|]
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phosphatidylinositol 4-kinase type 2-beta isoform X2 [Rattus norvegicus]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
125-299 1.49e-32

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member pfam00454:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 241  Bit Score: 120.51  E-value: 1.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676003 125 GSSGSYFVKDSKR---TIIGVFKPKSEEPYGQLNPKWTkyvHKVCCPCCFGRGCLLPNQGYLSEAGAYLVDTKLQLGIVP 201
Cdd:pfam00454   1 GYGGIYKVGDDLRqdeLILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGENGVPP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676003 202 KTKVVWLvsetfnysaidRAKSRGKKYALEKvpkvgrkFHRIGLPPKIGSFQLFVKDYKEAEYWLRRfeaeplpeniRKQ 281
Cdd:pfam00454  78 TAMVKIL-----------HSALNYPKLKLEF-------ESRISLPPKVGLLQWFVKKSPDAEEWGEA----------RKN 129
                         170
                  ....*....|....*...
gi 1958676003 282 FQSQFERLVILDYIIRNT 299
Cdd:pfam00454 130 FVRSCAGYSVLDYILGNG 147
 
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 ...
125-299 1.49e-32

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: 120.51  E-value: 1.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676003 125 GSSGSYFVKDSKR---TIIGVFKPKSEEPYGQLNPKWTkyvHKVCCPCCFGRGCLLPNQGYLSEAGAYLVDTKLQLGIVP 201
Cdd:pfam00454   1 GYGGIYKVGDDLRqdeLILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGENGVPP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676003 202 KTKVVWLvsetfnysaidRAKSRGKKYALEKvpkvgrkFHRIGLPPKIGSFQLFVKDYKEAEYWLRRfeaeplpeniRKQ 281
Cdd:pfam00454  78 TAMVKIL-----------HSALNYPKLKLEF-------ESRISLPPKVGLLQWFVKKSPDAEEWGEA----------RKN 129
                         170
                  ....*....|....*...
gi 1958676003 282 FQSQFERLVILDYIIRNT 299
Cdd:pfam00454 130 FVRSCAGYSVLDYILGNG 147
globin_sensor cd01068
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ...
214-293 2.20e-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: 37.94  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676003 214 NYSAIDRAKSRGKKYAL------------EKVPKVGRKFHRIGLPPK--IGSFQLFVkdykeaEYWLRRFEAE--PLPEN 277
Cdd:cd01068    50 DHSTIERLKQTQRAHWLelfsgdfdeayvERRRRIGRVHVRIGLEPRwyIGAYALLL------EELIEIIAEElrKDPEE 123
                          90
                  ....*....|....*.
gi 1958676003 278 IRKQFQSqFERLVILD 293
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 ...
125-299 1.49e-32

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: 120.51  E-value: 1.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676003 125 GSSGSYFVKDSKR---TIIGVFKPKSEEPYGQLNPKWTkyvHKVCCPCCFGRGCLLPNQGYLSEAGAYLVDTKLQLGIVP 201
Cdd:pfam00454   1 GYGGIYKVGDDLRqdeLILQVFKLMDEELSKDNLDLRR---LKPYSVIPLGPKCGIIEWVPNSETLAYILDEYGENGVPP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676003 202 KTKVVWLvsetfnysaidRAKSRGKKYALEKvpkvgrkFHRIGLPPKIGSFQLFVKDYKEAEYWLRRfeaeplpeniRKQ 281
Cdd:pfam00454  78 TAMVKIL-----------HSALNYPKLKLEF-------ESRISLPPKVGLLQWFVKKSPDAEEWGEA----------RKN 129
                         170
                  ....*....|....*...
gi 1958676003 282 FQSQFERLVILDYIIRNT 299
Cdd:pfam00454 130 FVRSCAGYSVLDYILGNG 147
globin_sensor cd01068
Globin sensor domain of globin-coupled-sensors (GCSs), protoglobins (Pgbs), and sensor ...
214-293 2.20e-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: 37.94  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958676003 214 NYSAIDRAKSRGKKYAL------------EKVPKVGRKFHRIGLPPK--IGSFQLFVkdykeaEYWLRRFEAE--PLPEN 277
Cdd:cd01068    50 DHSTIERLKQTQRAHWLelfsgdfdeayvERRRRIGRVHVRIGLEPRwyIGAYALLL------EELIEIIAEElrKDPEE 123
                          90
                  ....*....|....*.
gi 1958676003 278 IRKQFQSqFERLVILD 293
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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