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Conserved domains on  [gi|1958645419|ref|XP_038967479|]
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mitogen-activated protein kinase kinase kinase 10 isoform X1 [Rattus norvegicus]

Protein Classification

COG4372 family protein( domain architecture ID 11468211)

COG4372 family protein

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 ...
3-26 1.81e-09

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 cd14148:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 258  Bit Score: 58.84  E-value: 1.81e-09
                          10        20
                  ....*....|....*....|....
gi 1958645419   3 GECWDPDPHGRPDFGSILKQLEVI 26
Cdd:cd14148   235 EECWDPDPHGRPDFGSILKRLEDI 258
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
13-121 2.65e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  13 RPDFGSILKQLEVIEQSALFQMplesfHSLQEdwklEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQEL 92
Cdd:COG4372    19 RPKTGILIAALSEQLRKALFEL-----DKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
                          90       100
                  ....*....|....*....|....*....
gi 1958645419  93 AEREMDIVERELHLlmSQLSQEKPRVRKR 121
Cdd:COG4372    90 QAAQAELAQAQEEL--ESLQEEAEELQEE 116
 
Name Accession Description Interval E-value
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
3-26 1.81e-09

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 58.84  E-value: 1.81e-09
                          10        20
                  ....*....|....*....|....
gi 1958645419   3 GECWDPDPHGRPDFGSILKQLEVI 26
Cdd:cd14148   235 EECWDPDPHGRPDFGSILKRLEDI 258
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
13-121 2.65e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  13 RPDFGSILKQLEVIEQSALFQMplesfHSLQEdwklEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQEL 92
Cdd:COG4372    19 RPKTGILIAALSEQLRKALFEL-----DKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
                          90       100
                  ....*....|....*....|....*....
gi 1958645419  93 AEREMDIVERELHLlmSQLSQEKPRVRKR 121
Cdd:COG4372    90 QAAQAELAQAQEEL--ESLQEEAEELQEE 116
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
24-102 3.08e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 44.10  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  24 EVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKEL-----------RSREEELlrAAQEQRFQEEQlRRREQEL 92
Cdd:pfam03938   9 KILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELqkdgalleeerEEKEQEL--QKKEQELQQLQ-QKAQQEL 85
                          90
                  ....*....|
gi 1958645419  93 AEREMDIVER 102
Cdd:pfam03938  86 QKKQQELLQP 95
PRK12704 PRK12704
phosphodiesterase; Provisional
21-106 7.28e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  21 KQLEVIEQSALFQMPlESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRaaqeqrfQEEQLRRREQELAEREMDIV 100
Cdd:PRK12704   49 KEAEAIKKEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR-------KLELLEKREEELEKKEKELE 120

                  ....*.
gi 1958645419 101 ERELHL 106
Cdd:PRK12704  121 QKQQEL 126
BAR_MUG137_fungi cd07593
The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated ...
23-111 4.35e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This subfamily is composed predominantly of uncharacterized fungal proteins with similarity to Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein (MUG137), which may play a role in meiosis and sporulation in fission yeast. MUG137 contains an N-terminal BAR domain and a C-terminal SH3 domain, similar to endophilins. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153277  Cd Length: 215  Bit Score: 38.87  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  23 LEVIEQSaLFQMplESFHSLQEdwKLEIQHM-FDDLRTK---EKELRSREEELLRAAQeQRFQE--EQLRRREQELAERE 96
Cdd:cd07593   103 LANIERS-LAEM--KEYHSARK--KLESRRLaYDAALTKsqkAKKEDSRLEEELRRAK-AKYEEssEDVEARMVAIKESE 176
                          90
                  ....*....|....*
gi 1958645419  97 MDIVERELHLLMSQL 111
Cdd:cd07593   177 ADQYRDLTDLLDAEL 191
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
24-102 6.86e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.18  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419   24 EVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKEL------------RSREEELlrAAQEQRFQEEQlRRREQE 91
Cdd:smart00935   8 KILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLqkdaatlseaarEKKEKEL--QKKVQEFQRKQ-QKLQQD 84
                           90
                   ....*....|.
gi 1958645419   92 LAEREMDIVER 102
Cdd:smart00935  85 LQKRQQEELQK 95
 
Name Accession Description Interval E-value
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
3-26 1.81e-09

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 58.84  E-value: 1.81e-09
                          10        20
                  ....*....|....*....|....
gi 1958645419   3 GECWDPDPHGRPDFGSILKQLEVI 26
Cdd:cd14148   235 EECWDPDPHGRPDFGSILKRLEDI 258
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
4-26 2.10e-06

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK 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: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 49.31  E-value: 2.10e-06
                          10        20
                  ....*....|....*....|...
gi 1958645419   4 ECWDPDPHGRPDFGSILKQLEVI 26
Cdd:cd14061   236 DCWQPDPHDRPSFADILKQLENI 258
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
13-121 2.65e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.82  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  13 RPDFGSILKQLEVIEQSALFQMplesfHSLQEdwklEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQEL 92
Cdd:COG4372    19 RPKTGILIAALSEQLRKALFEL-----DKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
                          90       100
                  ....*....|....*....|....*....
gi 1958645419  93 AEREMDIVERELHLlmSQLSQEKPRVRKR 121
Cdd:COG4372    90 QAAQAELAQAQEEL--ESLQEEAEELQEE 116
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
24-102 3.08e-05

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 44.10  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  24 EVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKEL-----------RSREEELlrAAQEQRFQEEQlRRREQEL 92
Cdd:pfam03938   9 KILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELqkdgalleeerEEKEQEL--QKKEQELQQLQ-QKAQQEL 85
                          90
                  ....*....|
gi 1958645419  93 AEREMDIVER 102
Cdd:pfam03938  86 QKKQQELLQP 95
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
1-26 5.38e-05

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 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: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 45.41  E-value: 5.38e-05
                          10        20
                  ....*....|....*....|....*.
gi 1958645419   1 MSGECWDPDPHGRPDFGSILKQLEVI 26
Cdd:cd14147   242 LMADCWAQDPHRRPDFASILQQLEAL 267
RNase_Y_N pfam12072
RNase Y N-terminal region;
57-122 5.72e-05

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 44.49  E-value: 5.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958645419  57 LRTK-EKELRSREEELlrAAQEQRFQ--EEQLRRREQELAEREMDIVERElhllmSQLSQEKPRVRKRK 122
Cdd:pfam12072  65 LRAEaERELKERRNEL--QRQERRLLqkEETLDRKDESLEKKEESLEKKE-----KELEAQQQQLEEKE 126
PRK12704 PRK12704
phosphodiesterase; Provisional
21-106 7.28e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.54  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  21 KQLEVIEQSALFQMPlESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRaaqeqrfQEEQLRRREQELAEREMDIV 100
Cdd:PRK12704   49 KEAEAIKKEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR-------KLELLEKREEELEKKEKELE 120

                  ....*.
gi 1958645419 101 ERELHL 106
Cdd:PRK12704  121 QKQQEL 126
PRK12704 PRK12704
phosphodiesterase; Provisional
41-127 1.42e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  41 SLQEDWKLEIQHMFDDLRTK-EKELRSREEELlrAAQEQRFQ--EEQLrRREQELAEREmdivERELHLLMSQLSQEKPR 117
Cdd:PRK12704   53 AIKKEALLEAKEEIHKLRNEfEKELRERRNEL--QKLEKRLLqkEENL-DRKLELLEKR----EEELEKKEKELEQKQQE 125
                          90
                  ....*....|
gi 1958645419 118 VRKRKGNFKR 127
Cdd:PRK12704  126 LEKKEEELEE 135
RNase_Y_N pfam12072
RNase Y N-terminal region;
40-103 1.45e-04

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 43.34  E-value: 1.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958645419  40 HSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRAAQ--EQRfqEEQLRRREQELAEREMDIVERE 103
Cdd:pfam12072  63 HKLRAEAERELKERRNELQRQERRLLQKEETLDRKDEslEKK--EESLEKKEKELEAQQQQLEEKE 126
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
4-26 7.22e-04

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 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: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 41.95  E-value: 7.22e-04
                          10        20
                  ....*....|....*....|...
gi 1958645419   4 ECWDPDPHGRPDFGSILKQLEVI 26
Cdd:cd14145   248 DCWNPDPHSRPPFTNILDQLTAI 270
ZapB COG3074
Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...
34-94 2.21e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442308 [Multi-domain]  Cd Length: 79  Bit Score: 37.26  E-value: 2.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958645419  34 MPLESFHSLQEdwklEIQHMFDD---LRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAE 94
Cdd:COG3074     1 MSLELLEELEA----KVQQAVDTielLQMEVEELKEKNEELEQENEELQSENEELQSENEQLKT 60
CCDC50_N pfam15295
Coiled-coil domain-containing protein 50 N-terminus;
26-102 2.61e-03

Coiled-coil domain-containing protein 50 N-terminus;


Pssm-ID: 464621 [Multi-domain]  Cd Length: 126  Bit Score: 38.17  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  26 IEQSALFQMPLESFHSLQED----WKLEIQHMFDDLRTKEKEL-RSREEELLRAAQEQRFQEEQLRRREQELAEREMDIV 100
Cdd:pfam15295  43 IQRNQLVQNDIRVAKQLQEEeelqAQTLFQRRLAQLEEQDEEIaKEIQEELQREAEERRRREEEDEEIARQLQERERERE 122

                  ..
gi 1958645419 101 ER 102
Cdd:pfam15295 123 RR 124
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
4-26 2.96e-03

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 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: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 40.02  E-value: 2.96e-03
                          10        20
                  ....*....|....*....|...
gi 1958645419   4 ECWDPDPHGRPDFGSILKQLEVI 26
Cdd:cd14146   246 ECWEQDPHIRPSFALILEQLTAI 268
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
13-121 3.41e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.89  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  13 RPDFGSILKQLEVIEqsalFQMPLESfHSLQEDWKL--EIQHMFDDLRTKEKELRSREE--ELLRAAQEQRFQEEQLRRR 88
Cdd:COG1340   108 GGSIDKLRKEIERLE----WRQQTEV-LSPEEEKELveKIKELEKELEKAKKALEKNEKlkELRAELKELRKEAEEIHKK 182
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958645419  89 EQELAErEMDiverELHLLMSQLSQEKPRVRKR 121
Cdd:COG1340   183 IKELAE-EAQ----ELHEEMIELYKEADELRKE 210
BAR_MUG137_fungi cd07593
The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated ...
23-111 4.35e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. This subfamily is composed predominantly of uncharacterized fungal proteins with similarity to Schizosaccharomyces pombe Meiotically Up-regulated Gene 137 protein (MUG137), which may play a role in meiosis and sporulation in fission yeast. MUG137 contains an N-terminal BAR domain and a C-terminal SH3 domain, similar to endophilins. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153277  Cd Length: 215  Bit Score: 38.87  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  23 LEVIEQSaLFQMplESFHSLQEdwKLEIQHM-FDDLRTK---EKELRSREEELLRAAQeQRFQE--EQLRRREQELAERE 96
Cdd:cd07593   103 LANIERS-LAEM--KEYHSARK--KLESRRLaYDAALTKsqkAKKEDSRLEEELRRAK-AKYEEssEDVEARMVAIKESE 176
                          90
                  ....*....|....*
gi 1958645419  97 MDIVERELHLLMSQL 111
Cdd:cd07593   177 ADQYRDLTDLLDAEL 191
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
57-150 5.69e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.10  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  57 LRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREmDIVERELHLLMSQLSQEKPRVRKRKGNFKRSRLLKLREG 136
Cdd:cd16269   193 LTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQE-RSYEEHLRQLKEKMEEERENLLKEQERALESKLKEQEAL 271
                          90
                  ....*....|....
gi 1958645419 137 SShislpSGFEHKI 150
Cdd:cd16269   272 LE-----EGFKEQA 280
COG5493 COG5493
Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only] ...
42-128 5.83e-03

Uncharacterized protein, contains PD-(D/E)XK nuclease domain [General function prediction only];


Pssm-ID: 444244 [Multi-domain]  Cd Length: 239  Bit Score: 38.81  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  42 LQEDW--------KLEIQHMFDDLRtkeKELRSREEELLRAAQEQRFQEEQLRR-REQELAERE----MDIVERELHLLM 108
Cdd:COG5493    16 LREDPefryavlgLLATKDGLEELL---ERLEKLEEQMRKWEEQLRKLEEEIKKlREQVRKLEEdvkrLEEQERKLEEAM 92
                          90       100
                  ....*....|....*....|
gi 1958645419 109 SQLSQEKPRVRKRKGNFKRS 128
Cdd:COG5493    93 AEHSELREELMKLIKRLERS 112
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
49-113 6.26e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.16  E-value: 6.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958645419  49 EIQHMFDDLRTKEKELRSREEELlrAAQEQRFQE-----EQLRRREQELAEREMDI---VERELHLLMSQLSQ 113
Cdd:pfam13863  21 EIERLEELLKQREEELEKKEQEL--KEDLIKFDKflkenDAKRRRALKKAEEETKLkkeKEKEIKKLTAQIEE 91
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
24-102 6.86e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 37.18  E-value: 6.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419   24 EVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKEL------------RSREEELlrAAQEQRFQEEQlRRREQE 91
Cdd:smart00935   8 KILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLqkdaatlseaarEKKEKEL--QKKVQEFQRKQ-QKLQQD 84
                           90
                   ....*....|.
gi 1958645419   92 LAEREMDIVER 102
Cdd:smart00935  85 LQKRQQEELQK 95
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
21-118 7.32e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.16  E-value: 7.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958645419  21 KQLEVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTK-----EKELRSREEELLRAAQEQ------RFQEEQLRR-- 87
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRkqrleEERQRQEEEERKQRLQLQaaqeraRQQQEEFRRkl 432
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958645419  88 ------REQELAEREMDIVERELHLLMsQLSQEKPRV 118
Cdd:pfam15709 433 qelqrkKQQEEAERAEAEKQRQKELEM-QLAEEQKRL 468
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
28-99 9.03e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 37.51  E-value: 9.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958645419  28 QSALFQMPleSFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELlrAAQEQRFQEEQLRRREQELAEREMDI 99
Cdd:COG2825    32 QRILQESP--EGKAAQKKLEKEFKKRQAELQKLEKELQALQEKL--QKEAATLSEEERQKKERELQKKQQEL 99
MobB_NDR_LATS-like cd21742
Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear ...
47-98 9.83e-03

Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear Dbf2-related (NDR)/large tumor suppressor (LATS) family includes NDR, LATS, CBK1, and Sid2p. They are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. NDR/LATS kinases bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. These kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR/LATS family serine/threonine protein kinases.


Pssm-ID: 439267  Cd Length: 62  Bit Score: 34.87  E-value: 9.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958645419  47 KLEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREMD 98
Cdd:cd21742     2 KQYIENHYTNLLQQLKERRERRKQLEEKLENLNLSEEEKEQLRKELLKKESE 53
 
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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