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Conserved domains on  [gi|922581648|ref|NP_001300333|]
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CHK kinase-like domain-containing protein [Caenorhabditis elegans]

Protein Classification

aminoglycoside/choline kinase family protein( domain architecture ID 10651865)

aminoglycoside/choline kinase family protein may catalyze the phosphorylation of small molecule substrates such as aminoglycoside antibiotics, N-acetylhexosamine, or ecdysteroids (insect growth and moulting hormones)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
 53-232 9.25e-39

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


:

Pssm-ID: 214734  Cd Length: 196  Bit Score: 135.15  E-value: 9.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648    53 VIVMEMFEDC-KVYDIITGFNEEQLYKIVDEIVKLHIFSLT-TEEWKTIVPDAFVLEMAGYFQTMVAGIGEK-------- 122
Cdd:smart00587   1 IIFEDLSPKGyVNADRLKGLDLEHTSLVLKKLAKLHAASAVlIEEEKGSYLEEFDEGLFERFKRMFSEEFIGglenflre 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648   123 LAQQPGLELVSTYIK--NTFATDPKFLQNINDEYLEERRiSVLTHGDLWAPQILWDKNDD----IAGIIDWQITHRGSPM 196
Cdd:smart00587  81 LLSQPELLKVEEYIEklDKLLDNLEDLKKEDKEPDEGEF-NVLNHGDLWANNIMFKYDDEgkpeDVALIDFQLSHYGSPA 159

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 922581648   197 EDFHHIMSTCTSVENRKNLTKPLLDYYFDKLSSGLE 232
Cdd:smart00587 160 EDLHYFLLTSLSVEIRREHFDELLKFYYETLVETLK 195
 
Name Accession Description Interval E-value
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
 53-232 9.25e-39

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


Pssm-ID: 214734  Cd Length: 196  Bit Score: 135.15  E-value: 9.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648    53 VIVMEMFEDC-KVYDIITGFNEEQLYKIVDEIVKLHIFSLT-TEEWKTIVPDAFVLEMAGYFQTMVAGIGEK-------- 122
Cdd:smart00587   1 IIFEDLSPKGyVNADRLKGLDLEHTSLVLKKLAKLHAASAVlIEEEKGSYLEEFDEGLFERFKRMFSEEFIGglenflre 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648   123 LAQQPGLELVSTYIK--NTFATDPKFLQNINDEYLEERRiSVLTHGDLWAPQILWDKNDD----IAGIIDWQITHRGSPM 196
Cdd:smart00587  81 LLSQPELLKVEEYIEklDKLLDNLEDLKKEDKEPDEGEF-NVLNHGDLWANNIMFKYDDEgkpeDVALIDFQLSHYGSPA 159

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 922581648   197 EDFHHIMSTCTSVENRKNLTKPLLDYYFDKLSSGLE 232
Cdd:smart00587 160 EDLHYFLLTSLSVEIRREHFDELLKFYYETLVETLK 195
DUF1679 pfam07914
Uncharacterized oxidoreductase dhs-27; The region featured in this family is found in a number ...
 14-259 1.70e-22

Uncharacterized oxidoreductase dhs-27; The region featured in this family is found in a number of C. elegans proteins, in one case as a repeat. In many of the family members, this region is associated with the CHK region described by SMART as being found in ZnF_C4 and HLH domain-containing kinases. In fact, one member of this family is annotated as being a member of the nuclear hormone receptor family, and contains regions typical of such proteins (Interpro:IPR000536, Interpro:IPR008946, and Interpro:IPR001628).


Pssm-ID: 369592  Cd Length: 413  Bit Score: 96.58  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648   14 MHNTECNYYKIFAKLTEKPLHLPVIYAAIKAEDKEAPVPVIVME---------MFEDCKVYDIITgfneeqlykIVDEIV 84
Cdd:pfam07914 112 LHNREVNFYKILEKFNHPDIPFTKVYFLKKFDDENDLKGYIIMEyvpnihtrhMYENIPADELIP---------VLRAIA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648   85 KL--HIFSLTTEEWKTIVPDAFVLEMAGYFQTMvAGIGEKLAQqpglelvsTYIKNTFATDPKF--LQNINDEYLEER-- 158
Cdd:pfam07914 183 TFqaLGESLSEEEKKSANGADFLEEMFETFMSE-EGLKGIFEQ--------LRNIFGAAYPEKVeeLVDIFEHYGPEIli 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648  159 -----RIS-------VLTHGDLWAPQILWDKNDD----IAGIIDWQITHRGSPMEDFHHIMSTCTSVENRKNLTKPLLDY 222
Cdd:pfam07914 254 fkkytNLNkvlgikpVLVHGDLWQSNILWTLENDgklkLKAIIDYQTVHMGNPAEDLVRLLLSCLSGADRRAHWEELLEQ 333

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 922581648  223 YFDKLSSGLEakGVKMPWTREEIEEEYKYSFINGAAL 259
Cdd:pfam07914 334 YYETFTKALG--DNEEPYTLEQLKDSYNLYFPMMSLL 368
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 162-226 1.11e-08

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 55.12  E-value: 1.11e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581648 162 VLTHGDLWAPQILWDKNDD-IAGIIDWQITHRGSPMEDFHHIMSTCTSVENRKNLTKPLLDYYFDK 226
Cdd:COG3173  193 VLVHGDLRPGNLLVDPDDGrLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPRAAFLAAYEEA 258
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 161-223 3.47e-06

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' 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).


Pssm-ID: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 47.62  E-value: 3.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581648 161 SVLTHGDLWAPQILWDKNDDIAGIIDWQITHRGSPMEDF--HHIMSTCTSVENrknltkpLLDYY 223
Cdd:cd05152  185 TVLVHGDLHPGHILVDEDGRVTGLIDWTEAKVGDPADDFawHYAAFGEEALER-------LLDAY 242
 
Name Accession Description Interval E-value
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
 53-232 9.25e-39

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


Pssm-ID: 214734  Cd Length: 196  Bit Score: 135.15  E-value: 9.25e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648    53 VIVMEMFEDC-KVYDIITGFNEEQLYKIVDEIVKLHIFSLT-TEEWKTIVPDAFVLEMAGYFQTMVAGIGEK-------- 122
Cdd:smart00587   1 IIFEDLSPKGyVNADRLKGLDLEHTSLVLKKLAKLHAASAVlIEEEKGSYLEEFDEGLFERFKRMFSEEFIGglenflre 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648   123 LAQQPGLELVSTYIK--NTFATDPKFLQNINDEYLEERRiSVLTHGDLWAPQILWDKNDD----IAGIIDWQITHRGSPM 196
Cdd:smart00587  81 LLSQPELLKVEEYIEklDKLLDNLEDLKKEDKEPDEGEF-NVLNHGDLWANNIMFKYDDEgkpeDVALIDFQLSHYGSPA 159

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 922581648   197 EDFHHIMSTCTSVENRKNLTKPLLDYYFDKLSSGLE 232
Cdd:smart00587 160 EDLHYFLLTSLSVEIRREHFDELLKFYYETLVETLK 195
DUF1679 pfam07914
Uncharacterized oxidoreductase dhs-27; The region featured in this family is found in a number ...
 14-259 1.70e-22

Uncharacterized oxidoreductase dhs-27; The region featured in this family is found in a number of C. elegans proteins, in one case as a repeat. In many of the family members, this region is associated with the CHK region described by SMART as being found in ZnF_C4 and HLH domain-containing kinases. In fact, one member of this family is annotated as being a member of the nuclear hormone receptor family, and contains regions typical of such proteins (Interpro:IPR000536, Interpro:IPR008946, and Interpro:IPR001628).


Pssm-ID: 369592  Cd Length: 413  Bit Score: 96.58  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648   14 MHNTECNYYKIFAKLTEKPLHLPVIYAAIKAEDKEAPVPVIVME---------MFEDCKVYDIITgfneeqlykIVDEIV 84
Cdd:pfam07914 112 LHNREVNFYKILEKFNHPDIPFTKVYFLKKFDDENDLKGYIIMEyvpnihtrhMYENIPADELIP---------VLRAIA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648   85 KL--HIFSLTTEEWKTIVPDAFVLEMAGYFQTMvAGIGEKLAQqpglelvsTYIKNTFATDPKF--LQNINDEYLEER-- 158
Cdd:pfam07914 183 TFqaLGESLSEEEKKSANGADFLEEMFETFMSE-EGLKGIFEQ--------LRNIFGAAYPEKVeeLVDIFEHYGPEIli 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648  159 -----RIS-------VLTHGDLWAPQILWDKNDD----IAGIIDWQITHRGSPMEDFHHIMSTCTSVENRKNLTKPLLDY 222
Cdd:pfam07914 254 fkkytNLNkvlgikpVLVHGDLWQSNILWTLENDgklkLKAIIDYQTVHMGNPAEDLVRLLLSCLSGADRRAHWEELLEQ 333

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 922581648  223 YFDKLSSGLEakGVKMPWTREEIEEEYKYSFINGAAL 259
Cdd:pfam07914 334 YYETFTKALG--DNEEPYTLEQLKDSYNLYFPMMSLL 368
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
 4-227 5.41e-12

Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme responsible for the phosphorylation of ecdysteroids (insect growth and moulting hormones) at C-22, to form physiologically inactive ecdysteroid 22-phosphates. Most insects contain 12 to 105 genes encoding this family and yet so far only one enzyme (ecdysteroid 22-kinase from Bombyx mori) has characterized substrates (2-deoxyecdysone, ecdysone, 20-hydroxyecdysone). There are good reasons to believe that this family includes kinases that act on other small molecule substrates and that they may function in detoxification processes.


Pssm-ID: 397213 [Multi-domain]  Cd Length: 293  Bit Score: 64.98  E-value: 5.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648    4 TDHSANVELFmhNTECN-YYKI---FAKLTEKPLHLPVIYAAIKAEDKEAPVPVIVME--------MFEDCKvydiitGF 71
Cdd:pfam02958  40 REMFSSLNLF--TREINmYEKVlpeLEALYREAGDPFKLAPKCYYADLEPEDQVIILEdlslkgykNADRLK------GL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648   72 NEEQLYKIVDEIVKLHIFSLTTEEWKTIVPDAFV---LEMaGYFQTMVAGIGEKLAQ---QPGLELVSTYIKNTFATDPK 145
Cdd:pfam02958 112 DLEHTKLVLEKLAKFHAASAALKELQPEVFKQLKkglFEE-DYVNGAIKEFFEPLMEtglDAAAEALREQLPEYEKYAEK 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922581648  146 FlQNINDEYLE---------ERRISVLTHGDLWAPQIL--WDKNDDIAGI--IDWQITHRGSPMEDFHHIMSTCTSVENR 212
Cdd:pfam02958 191 L-EKLKDNYFDrllrlveptPGEFNVLNHGDLWVNNIMfkYDDEGEPEDVilVDFQLSRYGSPAIDLNYFLYTSTELELR 269

                         250
                  ....*....|....*
gi 922581648  213 KNLTKPLLDYYFDKL 227
Cdd:pfam02958 270 LEHFDELLRYYHSSL 284
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 162-226 1.11e-08

Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 55.12  E-value: 1.11e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922581648 162 VLTHGDLWAPQILWDKNDD-IAGIIDWQITHRGSPMEDFHHIMSTCTSVENRKNLTKPLLDYYFDK 226
Cdd:COG3173  193 VLVHGDLRPGNLLVDPDDGrLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPRAAFLAAYEEA 258
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 140-199 5.94e-07

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 49.42  E-value: 5.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922581648  140 FATDPKFLQNINDEYLEERRIS---VLTHGDLWAPQILWDKNDDIAGIIDWQITHRGSPMEDF 199
Cdd:pfam01636 143 LDRLEELEERLLAALLALLPAElppVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDL 205
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 161-223 3.47e-06

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' 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).


Pssm-ID: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 47.62  E-value: 3.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 922581648 161 SVLTHGDLWAPQILWDKNDDIAGIIDWQITHRGSPMEDF--HHIMSTCTSVENrknltkpLLDYY 223
Cdd:cd05152  185 TVLVHGDLHPGHILVDEDGRVTGLIDWTEAKVGDPADDFawHYAAFGEEALER-------LLDAY 242
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 155-188 2.74e-04

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This 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 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).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 40.75  E-value: 2.74e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 922581648 155 LEERRISVLTHGDLWAPQILWDKNDDIAGIIDWQ 188
Cdd:cd05120  105 LHRIDSSVLTHGDLHPGNILVKPDGKLSGIIDWE 138
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 153-198 2.15e-03

N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily 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).


Pssm-ID: 270703 [Multi-domain]  Cd Length: 254  Bit Score: 38.75  E-value: 2.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 922581648 153 EYLEERR----ISVLTHGDLWAPQILWDKNDDIAGIIDWQITHRGSPMED 198
Cdd:cd05154  165 RWLRANLpadgRPVLVHGDFRLGNLLFDPDGRVTAVLDWELATLGDPLED 214
 
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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