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Conserved domains on  [gi|118444592|ref|YP_878682|]
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serine/threonine kinase related protein [Clostridium novyi NT]

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List of domain hits

Name Accession Description Interval E-value
APH_ChoK_like super family cl17270
Aminoglycoside 3'-phosphotransferase (APH) and Choline Kinase (ChoK) family. The APH/ChoK ...
13-80 6.98e-06

Aminoglycoside 3'-phosphotransferase (APH) and Choline Kinase (ChoK) family. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K). The family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine.


The actual alignment was detected with superfamily member COG2112:

Pssm-ID: 266599  Cd Length: 201  Bit Score: 43.55  E-value: 6.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118444592  13 LSGCKFLGEGHHGKVFLMEDGKVIKIC------TTVRSCKSEYLILKKVNGSKYFPKVYKYEYLYMIRDYVGGE 80
Cdd:COG2112   24 LRVEKELAKGTTSVVYLGEWRGGEVALkvrrrdSPRRNLEKEAKILEILAGEGVTPEVYFYGEDFIRMEYIDGR 97
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
17-178 2.75e-05

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


:

Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 42.42  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592  17 KFLGEGHHGKVFLMED-----GKVIKICTTVRSC-----KSEYLILKKVNGSKYFPKVYKY----EYLYMIRDYVGGECM 82
Cdd:COG0515    6 RKLGEGSFGEVYLARDrklvaLKVLAKKLESKSKeverfLREIQILASLNHPPNIVKLYDFfqdeGSLYLVMEYVDGGSL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592  83 RDYIKTHG--------LSKVLALNVINLLEEFKRLKFTKIDIRCKDIFVQEKEN-VMVID-------PKGCYSRHKKYPS 146
Cdd:COG0515   86 EDLLKKIGrkgplsesEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDfglakllPDPGSTSSIPALP 165
                        170       180       190
                 ....*....|....*....|....*....|..
gi 118444592 147 HLIKGLKKSMYLEKFLKILKNERPDLYDEWIL 178
Cdd:COG0515  166 STSVGTPGYMAPEVLLGLSLAYASSSSDIWSL 197
 
Name Accession Description Interval E-value
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]
13-80 6.98e-06

Predicted Ser/Thr protein kinase [Signal transduction mechanisms]


Pssm-ID: 225023  Cd Length: 201  Bit Score: 43.55  E-value: 6.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118444592  13 LSGCKFLGEGHHGKVFLMEDGKVIKIC------TTVRSCKSEYLILKKVNGSKYFPKVYKYEYLYMIRDYVGGE 80
Cdd:COG2112   24 LRVEKELAKGTTSVVYLGEWRGGEVALkvrrrdSPRRNLEKEAKILEILAGEGVTPEVYFYGEDFIRMEYIDGR 97
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
17-133 1.77e-04

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, MSK2, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK 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. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis.


Pssm-ID: 173705 [Multi-domain]  Cd Length: 332  Bit Score: 39.94  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592  17 KFLGEGHHGKVFLMEDG-----------KVIKICT------TVRSCKSEYLILKKVNGSKYFPKV-YKYEY---LYMIRD 75
Cdd:cd05614    6 KVLGTGAYGKVFLVRKVtghdtgklyamKVLQKAAlvqkakTVEHTRTERNVLEHVRQSPFLVTLhYAFQTeakLHLILD 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118444592  76 YV-GGECM-----RDYIKTHGLsKVLALNVINLLEEFKRLKFTKIDIRCKDIFVQEKENVMVID 133
Cdd:cd05614   86 YVsGGEMFthlyqRDNFSEDEV-RFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTD 148
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
17-178 2.75e-05

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 42.42  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592  17 KFLGEGHHGKVFLMED-----GKVIKICTTVRSC-----KSEYLILKKVNGSKYFPKVYKY----EYLYMIRDYVGGECM 82
Cdd:COG0515    6 RKLGEGSFGEVYLARDrklvaLKVLAKKLESKSKeverfLREIQILASLNHPPNIVKLYDFfqdeGSLYLVMEYVDGGSL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592  83 RDYIKTHG--------LSKVLALNVINLLEEFKRLKFTKIDIRCKDIFVQEKEN-VMVID-------PKGCYSRHKKYPS 146
Cdd:COG0515   86 EDLLKKIGrkgplsesEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDfglakllPDPGSTSSIPALP 165
                        170       180       190
                 ....*....|....*....|....*....|..
gi 118444592 147 HLIKGLKKSMYLEKFLKILKNERPDLYDEWIL 178
Cdd:COG0515  166 STSVGTPGYMAPEVLLGLSLAYASSSSDIWSL 197
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
17-90 2.83e-03

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 35.97  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592    17 KFLGEGHHGKVFLMEDG--------KVIK---ICTTVRSCKSEYLILKKVNgSKYFPKVYKY----EYLYMIRDYVGGEC 81
Cdd:smart00220   5 EKLGEGSFGKVYLARDKktgklvaiKVIKkkkIKKDRERILREIKILKKLK-HPNIVRLYDVfedeDKLYLVMEYCEGGD 83

                   ....*....
gi 118444592    82 MRDYIKTHG 90
Cdd:smart00220  84 LFDLLKKRG 92
 
Name Accession Description Interval E-value
COG2112 COG2112
Predicted Ser/Thr protein kinase [Signal transduction mechanisms]
13-80 6.98e-06

Predicted Ser/Thr protein kinase [Signal transduction mechanisms]


Pssm-ID: 225023  Cd Length: 201  Bit Score: 43.55  E-value: 6.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118444592  13 LSGCKFLGEGHHGKVFLMEDGKVIKIC------TTVRSCKSEYLILKKVNGSKYFPKVYKYEYLYMIRDYVGGE 80
Cdd:COG2112   24 LRVEKELAKGTTSVVYLGEWRGGEVALkvrrrdSPRRNLEKEAKILEILAGEGVTPEVYFYGEDFIRMEYIDGR 97
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and ...
17-133 1.77e-04

N-terminal catalytic domain of the Protein Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; Serine/Threonine Kinases (STKs), Mitogen and stress-activated kinase (MSK) subfamily, MSK2, N-terminal catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MSK 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. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis.


Pssm-ID: 173705 [Multi-domain]  Cd Length: 332  Bit Score: 39.94  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592  17 KFLGEGHHGKVFLMEDG-----------KVIKICT------TVRSCKSEYLILKKVNGSKYFPKV-YKYEY---LYMIRD 75
Cdd:cd05614    6 KVLGTGAYGKVFLVRKVtghdtgklyamKVLQKAAlvqkakTVEHTRTERNVLEHVRQSPFLVTLhYAFQTeakLHLILD 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118444592  76 YV-GGECM-----RDYIKTHGLsKVLALNVINLLEEFKRLKFTKIDIRCKDIFVQEKENVMVID 133
Cdd:cd05614   86 YVsGGEMFthlyqRDNFSEDEV-RFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTD 148
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
19-132 4.43e-03

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 35.29  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592  19 LGEGHHGKVFLMEDGK-----VIKI------CTTVRSCKSEYLILKKVNgSKYFPKVYKY----EYLYMIRDYVGGECMR 83
Cdd:cd00180    1 LGEGGFGTVYLARDKKtgkkvAIKIikkedsSSLLEELLREIEILKKLN-HPNIVKLYGVfedeNHLYLVMEYCEGGSLK 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 118444592  84 DYIKTH--GLSKVLALNVI-NLLEEFKRLKFTKI---DIRCKDIFVQEKENVMVI 132
Cdd:cd00180   80 DLLKENegKLSEDEILRILlQILEGLEYLHSNGIihrDLKPENILLDSDNGKVKL 134
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
17-178 2.75e-05

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 42.42  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592  17 KFLGEGHHGKVFLMED-----GKVIKICTTVRSC-----KSEYLILKKVNGSKYFPKVYKY----EYLYMIRDYVGGECM 82
Cdd:COG0515    6 RKLGEGSFGEVYLARDrklvaLKVLAKKLESKSKeverfLREIQILASLNHPPNIVKLYDFfqdeGSLYLVMEYVDGGSL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592  83 RDYIKTHG--------LSKVLALNVINLLEEFKRLKFTKIDIRCKDIFVQEKEN-VMVID-------PKGCYSRHKKYPS 146
Cdd:COG0515   86 EDLLKKIGrkgplsesEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRvVKLIDfglakllPDPGSTSSIPALP 165
                        170       180       190
                 ....*....|....*....|....*....|..
gi 118444592 147 HLIKGLKKSMYLEKFLKILKNERPDLYDEWIL 178
Cdd:COG0515  166 STSVGTPGYMAPEVLLGLSLAYASSSSDIWSL 197
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
17-90 2.83e-03

Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or threonine-specific kinase subfamily.


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 35.97  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118444592    17 KFLGEGHHGKVFLMEDG--------KVIK---ICTTVRSCKSEYLILKKVNgSKYFPKVYKY----EYLYMIRDYVGGEC 81
Cdd:smart00220   5 EKLGEGSFGKVYLARDKktgklvaiKVIKkkkIKKDRERILREIKILKKLK-HPNIVRLYDVfedeDKLYLVMEYCEGGD 83

                   ....*....
gi 118444592    82 MRDYIKTHG 90
Cdd:smart00220  84 LFDLLKKRG 92
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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