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Conserved domains on  [gi|1405457274|ref|NP_001351421|]
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dual specificity mitogen-activated protein kinase kinase 5 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PB1_Map2k5 cd06395
PB1 domain is essential part of the mitogen-activated protein kinase kinase 5 (Map2k5, alias ...
 17-107 9.44e-61

PB1 domain is essential part of the mitogen-activated protein kinase kinase 5 (Map2k5, alias MEK5) one of the key member of the signaling kinases cascade which involved in angiogenesis and early cardiovascular development. The PB1 domain of Map2k5 interacts with the PB1 domain of another members of kinase cascade MEKK2 (or MEKK3). A canonical PB1-PB1 interaction, involving heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. The Map2k5 protein contains a type I PB1 domain.


:

Pssm-ID: 99717  Cd Length: 91  Bit Score: 183.53  E-value: 9.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457274  17 LVIRIKIPNSGAVDWTVHSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYYSTVMEQQVNG 96
Cdd:cd06395     1 LVIRIKIPNGGAVDWTVQSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYCSTVMEQQVNG 80

                          90
                  ....*....|.
gi 1405457274  97 QLIEPLQIFPR 107
Cdd:cd06395    81 QLIEPLQIFPR 91
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 164-186 1.60e-06

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 cd06619:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 279  Bit Score: 46.80  E-value: 1.60e-06
                          10        20
                  ....*....|....*....|...
gi 1405457274 164 QDIRYRDTLGHGNGGTVYKLLHI 186
Cdd:cd06619     1 QDIQYQEILGHGNGGTVYKAYHL 23
 
Name Accession Description Interval E-value
PB1_Map2k5 cd06395
PB1 domain is essential part of the mitogen-activated protein kinase kinase 5 (Map2k5, alias ...
 17-107 9.44e-61

PB1 domain is essential part of the mitogen-activated protein kinase kinase 5 (Map2k5, alias MEK5) one of the key member of the signaling kinases cascade which involved in angiogenesis and early cardiovascular development. The PB1 domain of Map2k5 interacts with the PB1 domain of another members of kinase cascade MEKK2 (or MEKK3). A canonical PB1-PB1 interaction, involving heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. The Map2k5 protein contains a type I PB1 domain.


Pssm-ID: 99717  Cd Length: 91  Bit Score: 183.53  E-value: 9.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457274  17 LVIRIKIPNSGAVDWTVHSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYYSTVMEQQVNG 96
Cdd:cd06395     1 LVIRIKIPNGGAVDWTVQSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYCSTVMEQQVNG 80

                          90
                  ....*....|.
gi 1405457274  97 QLIEPLQIFPR 107
Cdd:cd06395    81 QLIEPLQIFPR 91
PB1 pfam00564
PB1 domain;
19-92 5.48e-15

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 66.55  E-value: 5.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405457274  19 IRIKIPNSGAVDWTVHSGPQLLFRDVLDVIGQVLPEAT-TTAFEYEDEDGDRITVRSDEEMKAMLSYYYSTVMEQ 92
Cdd:pfam00564   2 VRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLDDvDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKS 76
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 27-88 2.76e-10

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 54.13  E-value: 2.76e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405457274   27 GAVDWTVHSGPQLLFRDVLDVIGQVLP-EATTTAFEYEDEDGDRITVRSDEEMKAMLSYYYST 88
Cdd:smart00666   9 GGETRRLSVPRDISFEDLRSKVAKRFGlDNQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSL 71
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 164-186 1.60e-06

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 46.80  E-value: 1.60e-06
                          10        20
                  ....*....|....*....|...
gi 1405457274 164 QDIRYRDTLGHGNGGTVYKLLHI 186
Cdd:cd06619     1 QDIQYQEILGHGNGGTVYKAYHL 23
 
Name Accession Description Interval E-value
PB1_Map2k5 cd06395
PB1 domain is essential part of the mitogen-activated protein kinase kinase 5 (Map2k5, alias ...
 17-107 9.44e-61

PB1 domain is essential part of the mitogen-activated protein kinase kinase 5 (Map2k5, alias MEK5) one of the key member of the signaling kinases cascade which involved in angiogenesis and early cardiovascular development. The PB1 domain of Map2k5 interacts with the PB1 domain of another members of kinase cascade MEKK2 (or MEKK3). A canonical PB1-PB1 interaction, involving heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. The Map2k5 protein contains a type I PB1 domain.


Pssm-ID: 99717  Cd Length: 91  Bit Score: 183.53  E-value: 9.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1405457274  17 LVIRIKIPNSGAVDWTVHSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYYSTVMEQQVNG 96
Cdd:cd06395     1 LVIRIKIPNGGAVDWTVQSGPQLLFRDVLDVIGQVLPEATTTAFEYEDEDGDRITVRSDEEMKAMLSYYCSTVMEQQVNG 80

                          90
                  ....*....|.
gi 1405457274  97 QLIEPLQIFPR 107
Cdd:cd06395    81 QLIEPLQIFPR 91
PB1 pfam00564
PB1 domain;
19-92 5.48e-15

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 66.55  E-value: 5.48e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1405457274  19 IRIKIPNSGAVDWTVHSGPQLLFRDVLDVIGQVLPEAT-TTAFEYEDEDGDRITVRSDEEMKAMLSYYYSTVMEQ 92
Cdd:pfam00564   2 VRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLDDvDFKLKYPDEDGDLVSLTSDEDLEEALEEARSLGSKS 76
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
 27-88 2.76e-10

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 54.13  E-value: 2.76e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1405457274   27 GAVDWTVHSGPQLLFRDVLDVIGQVLP-EATTTAFEYEDEDGDRITVRSDEEMKAMLSYYYST 88
Cdd:smart00666   9 GGETRRLSVPRDISFEDLRSKVAKRFGlDNQSFTLKYQDEDGDLVSLTSDEDLEEAIEEYDSL 71
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
 19-85 1.97e-09

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99716 [Multi-domain]  Cd Length: 81  Bit Score: 51.89  E-value: 1.97e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1405457274  19 IRIKIP-NSGAVDWTVHSgPQLLFRDVLDVIGQVLP-EATTTAFEYEDEDGDRITVRSDEEMKAMLSYY 85
Cdd:cd05992     1 VRVKVKyGGEIRRFVVVS-RSISFEDLRSKIAEKFGlDAVSFKLKYPDEDGDLVTISSDEDLEEAIEEA 68
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
 164-186 1.60e-06

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 46.80  E-value: 1.60e-06
                          10        20
                  ....*....|....*....|...
gi 1405457274 164 QDIRYRDTLGHGNGGTVYKLLHI 186
Cdd:cd06619     1 QDIQYQEILGHGNGGTVYKAYHL 23
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
 164-185 1.18e-03

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 38.48  E-value: 1.18e-03
                          10        20
                  ....*....|....*....|..
gi 1405457274 164 QDIRYRDTLGHGNGGTVYKLLH 185
Cdd:cd06605     1 DDLEYLGELGEGNGGVVSKVRH 22
 
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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