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Conserved domains on  [gi|71984274|ref|NP_510235|]
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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
 142-321 2.41e-38

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


:

Pssm-ID: 214734  Cd Length: 196  Bit Score: 136.69  E-value: 2.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    142 VIVMEMFEDC-KVYDIITGFNEEQLYKIVDEIVKLHIFSLT-TEEWKTIVPDAFVLEMAGYFQTMVAGIGEK-------- 211
Cdd:smart00587   1 IIFEDLSPKGyVNADRLKGLDLEHTSLVLKKLAKLHAASAVlIEEEKGSYLEEFDEGLFERFKRMFSEEFIGglenflre 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    212 LAQQPGLELVSTYIK--NTFATDPKFLQNINDEYLEERRiSVLTHGDLWAPQILWDKNDD----IAGIIDWQITHRGSPM 285
Cdd:smart00587  81 LLSQPELLKVEEYIEklDKLLDNLEDLKKEDKEPDEGEF-NVLNHGDLWANNIMFKYDDEgkpeDVALIDFQLSHYGSPA 159

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 71984274    286 EDFHHIMSTCTSVENRKNLTKPLLDYYFDKLSSGLE 321
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
 142-321 2.41e-38

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 136.69  E-value: 2.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    142 VIVMEMFEDC-KVYDIITGFNEEQLYKIVDEIVKLHIFSLT-TEEWKTIVPDAFVLEMAGYFQTMVAGIGEK-------- 211
Cdd:smart00587   1 IIFEDLSPKGyVNADRLKGLDLEHTSLVLKKLAKLHAASAVlIEEEKGSYLEEFDEGLFERFKRMFSEEFIGglenflre 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    212 LAQQPGLELVSTYIK--NTFATDPKFLQNINDEYLEERRiSVLTHGDLWAPQILWDKNDD----IAGIIDWQITHRGSPM 285
Cdd:smart00587  81 LLSQPELLKVEEYIEklDKLLDNLEDLKKEDKEPDEGEF-NVLNHGDLWANNIMFKYDDEgkpeDVALIDFQLSHYGSPA 159

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 71984274    286 EDFHHIMSTCTSVENRKNLTKPLLDYYFDKLSSGLE 321
Cdd:smart00587 160 EDLHYFLLTSLSVEIRREHFDELLKFYYETLVETLK 195
DUF1679 pfam07914
Uncharacterized oxidoreductase dhs-27; The region featured in this family is found in a number ...
 18-348 3.70e-25

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: 105.82  E-value: 3.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    18 EIIEKKIGVKPKIGTSGILDN-SEL-GYMSMIRKVQLHFdaEHEESHPNLPKHVVLKIACSSKGTGVLD----SAGADMT 91
Cdd:pfam07914  20 KAIQEQLGTEAKFGENKKATNiGDGkGFMSRIALIEPDW--TNVEPSKNLPKKFALKISSQLHLIALSKkmkfEGGNGFT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    92 ETDHSANVELF---MHNTECNYYKIFAKLTEKPLHLPVIYAAIKAEDKEAPVPVIVME---------MFEDCKVYDIITg 159
Cdd:pfam07914  98 EEKELKHFEKStreLHNREVNFYKILEKFNHPDIPFTKVYFLKKFDDENDLKGYIIMEyvpnihtrhMYENIPADELIP- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274   160 fneeqlykIVDEIVKL--HIFSLTTEEWKTIVPDAFVLEMAGYFQTMvAGIGEKLAQqpglelvsTYIKNTFATDPKF-- 235
Cdd:pfam07914 177 --------VLRAIATFqaLGESLSEEEKKSANGADFLEEMFETFMSE-EGLKGIFEQ--------LRNIFGAAYPEKVee 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274   236 LQNINDEYLEER-------RIS-------VLTHGDLWAPQILWDKNDD----IAGIIDWQITHRGSPMEDFHHIMSTCTS 297
Cdd:pfam07914 240 LVDIFEHYGPEIlifkkytNLNkvlgikpVLVHGDLWQSNILWTLENDgklkLKAIIDYQTVHMGNPAEDLVRLLLSCLS 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 71984274   298 VENRKNLTKPLLDYYFDKLSSGLEakGVKMPWTREEIEEEYKYSFINGAAL 348
Cdd:pfam07914 320 GADRRAHWEELLEQYYETFTKALG--DNEEPYTLEQLKDSYNLYFPMMSLL 368
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 251-315 1.87e-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: 1.87e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71984274 251 VLTHGDLWAPQILWDKNDD-IAGIIDWQITHRGSPMEDFHHIMSTCTSVENRKNLTKPLLDYYFDK 315
Cdd:COG3173 193 VLVHGDLRPGNLLVDPDDGrLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPRAAFLAAYEEA 258
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 250-312 5.46e-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: 5.46e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71984274 250 SVLTHGDLWAPQILWDKNDDIAGIIDWQITHRGSPMEDF--HHIMSTCTSVENrknltkpLLDYY 312
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
 142-321 2.41e-38

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 136.69  E-value: 2.41e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    142 VIVMEMFEDC-KVYDIITGFNEEQLYKIVDEIVKLHIFSLT-TEEWKTIVPDAFVLEMAGYFQTMVAGIGEK-------- 211
Cdd:smart00587   1 IIFEDLSPKGyVNADRLKGLDLEHTSLVLKKLAKLHAASAVlIEEEKGSYLEEFDEGLFERFKRMFSEEFIGglenflre 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    212 LAQQPGLELVSTYIK--NTFATDPKFLQNINDEYLEERRiSVLTHGDLWAPQILWDKNDD----IAGIIDWQITHRGSPM 285
Cdd:smart00587  81 LLSQPELLKVEEYIEklDKLLDNLEDLKKEDKEPDEGEF-NVLNHGDLWANNIMFKYDDEgkpeDVALIDFQLSHYGSPA 159

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 71984274    286 EDFHHIMSTCTSVENRKNLTKPLLDYYFDKLSSGLE 321
Cdd:smart00587 160 EDLHYFLLTSLSVEIRREHFDELLKFYYETLVETLK 195
DUF1679 pfam07914
Uncharacterized oxidoreductase dhs-27; The region featured in this family is found in a number ...
 18-348 3.70e-25

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: 105.82  E-value: 3.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    18 EIIEKKIGVKPKIGTSGILDN-SEL-GYMSMIRKVQLHFdaEHEESHPNLPKHVVLKIACSSKGTGVLD----SAGADMT 91
Cdd:pfam07914  20 KAIQEQLGTEAKFGENKKATNiGDGkGFMSRIALIEPDW--TNVEPSKNLPKKFALKISSQLHLIALSKkmkfEGGNGFT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    92 ETDHSANVELF---MHNTECNYYKIFAKLTEKPLHLPVIYAAIKAEDKEAPVPVIVME---------MFEDCKVYDIITg 159
Cdd:pfam07914  98 EEKELKHFEKStreLHNREVNFYKILEKFNHPDIPFTKVYFLKKFDDENDLKGYIIMEyvpnihtrhMYENIPADELIP- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274   160 fneeqlykIVDEIVKL--HIFSLTTEEWKTIVPDAFVLEMAGYFQTMvAGIGEKLAQqpglelvsTYIKNTFATDPKF-- 235
Cdd:pfam07914 177 --------VLRAIATFqaLGESLSEEEKKSANGADFLEEMFETFMSE-EGLKGIFEQ--------LRNIFGAAYPEKVee 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274   236 LQNINDEYLEER-------RIS-------VLTHGDLWAPQILWDKNDD----IAGIIDWQITHRGSPMEDFHHIMSTCTS 297
Cdd:pfam07914 240 LVDIFEHYGPEIlifkkytNLNkvlgikpVLVHGDLWQSNILWTLENDgklkLKAIIDYQTVHMGNPAEDLVRLLLSCLS 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 71984274   298 VENRKNLTKPLLDYYFDKLSSGLEakGVKMPWTREEIEEEYKYSFINGAAL 348
Cdd:pfam07914 320 GADRRAHWEELLEQYYETFTKALG--DNEEPYTLEQLKDSYNLYFPMMSLL 368
EcKL pfam02958
Ecdysteroid kinase-like family; This family includes ecdysteroid 22-kinase, an enzyme ...
 42-316 1.79e-13

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: 70.38  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274    42 GYMSMIRKVQLHFdaeHEESHPNLPKHVVLKIacsskgtgVLDSAGAdmteTDHSANVELFmhNTECN-YYKI---FAKL 117
Cdd:pfam02958   4 NYASVMLRVTIEY---EKGDGSKRTKSLIVKT--------MPDNEER----REMFSSLNLF--TREINmYEKVlpeLEAL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274   118 TEKPLHLPVIYAAIKAEDKEAPVPVIVME--------MFEDCKvydiitGFNEEQLYKIVDEIVKLHIFSLTTEEWKTIV 189
Cdd:pfam02958  67 YREAGDPFKLAPKCYYADLEPEDQVIILEdlslkgykNADRLK------GLDLEHTKLVLEKLAKFHAASAALKELQPEV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274   190 PDAFV---LEM-----------AGYFQTMVAGIGEKLAQQ-PGLELVSTYIKntfatdpKFLQNINDEYLE-----ERRI 249
Cdd:pfam02958 141 FKQLKkglFEEdyvngaikeffEPLMETGLDAAAEALREQlPEYEKYAEKLE-------KLKDNYFDRLLRlveptPGEF 213

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71984274   250 SVLTHGDLWAPQIL--WDKNDDIAGI--IDWQITHRGSPMEDFHHIMSTCTSVENRKNLTKPLLDYYFDKL 316
Cdd:pfam02958 214 NVLNHGDLWVNNIMfkYDDEGEPEDVilVDFQLSRYGSPAIDLNYFLYTSTELELRLEHFDELLRYYHSSL 284
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 251-315 1.87e-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: 1.87e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71984274 251 VLTHGDLWAPQILWDKNDD-IAGIIDWQITHRGSPMEDFHHIMSTCTSVENRKNLTKPLLDYYFDK 315
Cdd:COG3173 193 VLVHGDLRPGNLLVDPDDGrLTAVIDWELATLGDPAADLAYLLLYWRLPDDLLGPRAAFLAAYEEA 258
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 229-288 9.18e-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: 9.18e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71984274   229 FATDPKFLQNINDEYLEERRIS---VLTHGDLWAPQILWDKNDDIAGIIDWQITHRGSPMEDF 288
Cdd:pfam01636 143 LDRLEELEERLLAALLALLPAElppVLVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDL 205
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 250-312 5.46e-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: 5.46e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71984274 250 SVLTHGDLWAPQILWDKNDDIAGIIDWQITHRGSPMEDF--HHIMSTCTSVENrknltkpLLDYY 312
Cdd:cd05152 185 TVLVHGDLHPGHILVDEDGRVTGLIDWTEAKVGDPADDFawHYAAFGEEALER-------LLDAY 242
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 244-277 3.84e-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: 3.84e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 71984274 244 LEERRISVLTHGDLWAPQILWDKNDDIAGIIDWQ 277
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 ...
 242-287 3.18e-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: 3.18e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 71984274 242 EYLEERR----ISVLTHGDLWAPQILWDKNDDIAGIIDWQITHRGSPMED 287
Cdd:cd05154 165 RWLRANLpadgRPVLVHGDFRLGNLLFDPDGRVTAVLDWELATLGDPLED 214
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
218-313 9.80e-03

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 36.68  E-value: 9.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71984274 218 LELVSTYIKNTFATDPKFLQNIND--EYLEERRIS-VLTHGDLWAPQILWDKNDDIAgIIDWQITHRGSPMEDfhhIMST 294
Cdd:COG0510  14 FARLERYLALGPRDLPELLRRLEEleRALAARPLPlVLCHGDLHPGNFLVTDDGRLY-LIDWEYAGLGDPAFD---LAAL 89

                        90
                ....*....|....*....
gi 71984274 295 CTSVENRKNLTKPLLDYYF 313
Cdd:COG0510  90 LVEYGLSPEQAEELLEAYG 108
 
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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