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Conserved domains on  [gi|1397887290|gb|PXW88185|]
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thiamine kinase-like enzyme [Streptohalobacillus salinus]

Protein Classification

phosphotransferase family protein( domain architecture ID 10001645)

phosphotransferase family protein similar to Streptococcus pneumoniae LicA, a choline kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to choline, producing phosphorylcholine, a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine and sphingomyelin

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
92-237 1.86e-24

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


:

Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 95.62  E-value: 1.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  92 RIHHSAELLdmltrigkkPLQPAALVKDLRRDYQTLANEklsllvIERALEYMETHLHIvEGIKPVVCHCDLNHNNWMIT 171
Cdd:COG0510     1 RLHASPALL---------RFDLFARLERYLALGPRDLPE------LLRRLEELERALAA-RPLPLVLCHGDLHPGNFLVT 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397887290 172 DRGELYLIDWDNAEIADPAIDLSLLFKRY-IPREDWDKWLAFYG-EVNDEELTVRMYWYMFYELLTSL 237
Cdd:COG0510    65 DDGRLYLIDWEYAGLGDPAFDLAALLVEYgLSPEQAEELLEAYGfGRPTEELLRRLRAYRALADLLWA 132
 
Name Accession Description Interval E-value
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
92-237 1.86e-24

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 95.62  E-value: 1.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  92 RIHHSAELLdmltrigkkPLQPAALVKDLRRDYQTLANEklsllvIERALEYMETHLHIvEGIKPVVCHCDLNHNNWMIT 171
Cdd:COG0510     1 RLHASPALL---------RFDLFARLERYLALGPRDLPE------LLRRLEELERALAA-RPLPLVLCHGDLHPGNFLVT 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397887290 172 DRGELYLIDWDNAEIADPAIDLSLLFKRY-IPREDWDKWLAFYG-EVNDEELTVRMYWYMFYELLTSL 237
Cdd:COG0510    65 DDGRLYLIDWEYAGLGDPAFDLAALLVEYgLSPEQAEELLEAYGfGRPTEELLRRLRAYRALADLLWA 132
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 14-228 1.17e-21

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: 90.64  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  14 AGGSTGEAYYAQSKHKRLFLKRNSSP-----------FLAVLSAQGI--VPKLVWTK--RMENGDVITAQEWLDGNELNP 78
Cdd:pfam01636   6 SSGASNRTYLVTTGDGRYVLRLPPPGraaeelrrelaLLRHLAAAGVppVPRVLAGCtdAELLGLPFLLMEYLPGEVLAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  79 EVLQHP------KVAELLGRIHHSAELLDMLTRIGKKPLQPAALVKDLRRDYQTLANEKLSLLVIERALEYMEthLHIVE 152
Cdd:pfam01636  86 PLLPEErgalleALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLLAALL--ALLPA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1397887290 153 GIKPVVCHCDLNHNNWMITDRGEL-YLIDWDNAEIADPAIDLSLLFkRYIPREDWDKWLAFYGEVNDEELTVRMYWY 228
Cdd:pfam01636 164 ELPPVLVHGDLHPGNLLVDPGGRVsGVIDFEDAGLGDPAYDLAILL-NSWGRELGAELLAAYLAAYGAFGYARLREL 239
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 123-197 5.48e-09

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK 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: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 53.71  E-value: 5.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1397887290 123 DYQTLANEKLSLLVIERALEYMEThLHIVEGIKPVVCHCDLNHNNWMITDrGELYLIDWDNAEIADPAIDLSLLF 197
Cdd:cd05151    75 GATLLTNDFSDPENLERIAALLRK-LHSSPLEDLVLCHNDLVPGNFLLDD-DRLYLIDWEYAGMNDPLFDLAALF 147
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
 158-186 4.92e-04

3-deoxy-D-manno-octulosonic-acid kinase; Reviewed


Pssm-ID: 234975  Cd Length: 239  Bit Score: 40.64  E-value: 4.92e-04
                          10        20
                  ....*....|....*....|....*....
gi 1397887290 158 VCHCDLNHNNWMITDRGELYLIDWDNAEI 186
Cdd:PRK01723  163 VYHADLNAHNILLDPDGKFWLIDFDRGEL 191
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
 137-213 5.99e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 36.92  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  137 IERALEYMETHLHIVEGIKPVVCHCDLNHNN--WMITDRGEL---YLIDWDNAEIADPAIDLSLLF----KRYIPREDWD 207
Cdd:smart00587 101 LDNLEDLKKEDKEPDEGEFNVLNHGDLWANNimFKYDDEGKPedvALIDFQLSHYGSPAEDLHYFLltslSVEIRREHFD 180


                   ....*.
gi 1397887290  208 KWLAFY 213
Cdd:smart00587 181 ELLKFY 186
 
Name Accession Description Interval E-value
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
92-237 1.86e-24

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 95.62  E-value: 1.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  92 RIHHSAELLdmltrigkkPLQPAALVKDLRRDYQTLANEklsllvIERALEYMETHLHIvEGIKPVVCHCDLNHNNWMIT 171
Cdd:COG0510     1 RLHASPALL---------RFDLFARLERYLALGPRDLPE------LLRRLEELERALAA-RPLPLVLCHGDLHPGNFLVT 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397887290 172 DRGELYLIDWDNAEIADPAIDLSLLFKRY-IPREDWDKWLAFYG-EVNDEELTVRMYWYMFYELLTSL 237
Cdd:COG0510    65 DDGRLYLIDWEYAGLGDPAFDLAALLVEYgLSPEQAEELLEAYGfGRPTEELLRRLRAYRALADLLWA 132
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 14-228 1.17e-21

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: 90.64  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  14 AGGSTGEAYYAQSKHKRLFLKRNSSP-----------FLAVLSAQGI--VPKLVWTK--RMENGDVITAQEWLDGNELNP 78
Cdd:pfam01636   6 SSGASNRTYLVTTGDGRYVLRLPPPGraaeelrrelaLLRHLAAAGVppVPRVLAGCtdAELLGLPFLLMEYLPGEVLAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  79 EVLQHP------KVAELLGRIHHSAELLDMLTRIGKKPLQPAALVKDLRRDYQTLANEKLSLLVIERALEYMEthLHIVE 152
Cdd:pfam01636  86 PLLPEErgalleALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRLEELEERLLAALL--ALLPA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1397887290 153 GIKPVVCHCDLNHNNWMITDRGEL-YLIDWDNAEIADPAIDLSLLFkRYIPREDWDKWLAFYGEVNDEELTVRMYWY 228
Cdd:pfam01636 164 ELPPVLVHGDLHPGNLLVDPGGRVsGVIDFEDAGLGDPAYDLAILL-NSWGRELGAELLAAYLAAYGAFGYARLREL 239
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
 61-257 2.97e-10

Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444583 [Multi-domain]  Cd Length: 331  Bit Score: 59.52  E-value: 2.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  61 NGDVITAQEWLDGNELNPEVLQHPK-VAELLGRIHHSA------ELLDMLTRIGKKPLQPAALVKDLRRdYQTLANEK-- 131
Cdd:COG5881    81 GGKLYYLTEWIEGRECDYKNPEDLKkAAETLAEFHKASkgfeppPGSKGRSHLGKWPERFEKRLEELEK-FKKIAEKKkn 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 132 ---LSLLVIERALEYMETHLHIVEGIK--------------PVVCHCDLNHNNWMITDRGELYLIDWDNAEIADPAIDLS 194
Cdd:COG5881   160 kneFDRLFLKNIDYFLEQAEKALELLEksayyklvkeakkeGGFCHHDYAYHNILIDEDGKIYIIDFDYCIYDLPVHDLA 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 195 LLFKRYIPREDWDK-----WLAFYGEVN---DEELTVrMYWYM-----FYELLTS-------------LNHIQTVTEQTE 248
Cdd:COG5881   240 KLLRRVMKRGNWDIekakeILEAYNKINplsKEEIEV-LLAFLlfpqkFWRLVNKyyyekknwseekfIKKLQKLIEEEE 318

                         250
                  ....*....|...
gi 1397887290 249 K----LEELQEIL 257
Cdd:COG5881   319 EkeefLEEFEKIL 331
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 40-221 7.76e-10

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 58.01  E-value: 7.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  40 FLAVLSAQGI-VPKLVWTK-----RMENGDVITAQEWLDG---NELNPEVLQHpkVAELLGRIHHSAELLDMltrigkkp 110
Cdd:COG2334    60 LLAHLAAAGLpVPAPVPTRdgetlLELEGRPAALFPFLPGrspEEPSPEQLEE--LGRLLARLHRALADFPR-------- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 111 lqPAAL-VKDLRRDYQTLANEKLS----LLVIERALEYMETHLHIVEGIKPV-VCHCDLNHNNWMITDRGELYLIDWDNA 184
Cdd:COG2334   130 --PNARdLAWWDELLERLLGPLLPdpedRALLEELLDRLEARLAPLLGALPRgVIHGDLHPDNVLFDGDGVSGLIDFDDA 207

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1397887290 185 E----IADPAIDLSLLFKRYIPREDWDKWLAFYGEVN---DEEL 221
Cdd:COG2334   208 GygprLYDLAIALNGWADGPLDPARLAALLEGYRAVRpltEAEL 251
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 123-197 5.48e-09

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK 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: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 53.71  E-value: 5.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1397887290 123 DYQTLANEKLSLLVIERALEYMEThLHIVEGIKPVVCHCDLNHNNWMITDrGELYLIDWDNAEIADPAIDLSLLF 197
Cdd:cd05151    75 GATLLTNDFSDPENLERIAALLRK-LHSSPLEDLVLCHNDLVPGNFLLDD-DRLYLIDWEYAGMNDPLFDLAALF 147
Choline_kinase pfam01633
Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of ...
 41-197 3.31e-08

Choline/ethanolamine kinase; Choline kinase catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway. This alignment covers the protein kinase portion of the protein. The divergence of this family makes it very difficult to create a model that specifically predicts choline/ethanolamine kinases only. However if [add Pfam ID here for Choline_kinase_C] is also present then it is definitely a member of this family.


Pssm-ID: 396278 [Multi-domain]  Cd Length: 211  Bit Score: 52.66  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  41 LAVLSAQGIVPKLVwtKRMENGDVitaQEWLDGNELNPEVLQHPK----VAELLGRIHHSAelldmltRIGKKPlqpAAL 116
Cdd:pfam01633  27 FALLSERGLGPKLY--GFFPNGRI---EEFIPSRTLSTEDLRDPEisklIAKRLAELHSLE-------MPGKKS---PSL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 117 VKDLRR---DYQTLAN----------EKLSLLVIERALEYMETHLhiVEGIKPVV-CHCDLNHNNWMITD-RGELYLIDW 181
Cdd:pfam01633  92 WKTMRKwlsLLKNLGApesvnkseqlKSINLEDLEKEINKLEKWL--ELLDSPIVfCHNDLQSGNILLLNeTKRLVLIDF 169

                         170
                  ....*....|....*.
gi 1397887290 182 DNAEIADPAIDLSLLF 197
Cdd:pfam01633 170 EYASYNYRGFDIANHF 185
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 50-196 6.55e-08

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 52.42  E-value: 6.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  50 VPKLVWTKrmENGDVI----TAQEWLDGNELNPEVLQHP---------KVAELLGRIH----HSAELLDMltrigkKPLQ 112
Cdd:COG3173    78 VPRPLALG--EDGEVIgapfYVMEWVEGETLEDALPDLSpaerralarALGEFLAALHavdpAAAGLADG------RPEG 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 113 PAALVKDLRRDYQTLANEKLSLLVI-ERALEYMETHLHivEGIKPVVCHCDLNHNNWMIT-DRGELY-LIDWDNAEIADP 189
Cdd:COG3173   150 LERQLARWRAQLRRALARTDDLPALrERLAAWLAANLP--EWGPPVLVHGDLRPGNLLVDpDDGRLTaVIDWELATLGDP 227


                  ....*..
gi 1397887290 190 AIDLSLL 196
Cdd:COG3173   228 AADLAYL 234
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 138-213 1.96e-05

Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group from ATP to aminoglycoside antibiotics such as kanamycin, streptomycin, neomycin, and gentamicin, among others. The aminoglycoside antibiotics target the 30S ribosome and promote miscoding, leading to the production of defective proteins which insert into the bacterial membrane, resulting in membrane damage and the ultimate demise of the bacterium. Phosphorylation of the aminoglycoside antibiotics results in their inactivation, leading to bacterial antibiotic resistance. The APH gene is found on transposons and plasmids and is thought to have originated as a self-defense mechanism used by microorganisms that produce the antibiotics. The APH 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: 270699 [Multi-domain]  Cd Length: 244  Bit Score: 44.88  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 138 ERALEYMETHLHIVEgiKPVVCHCDLNHNNWMITDRGELYLIDWDNAEIADPAIDLSL-----------------LFKRY 200
Cdd:cd05150   147 EELLAELEATRPAEE--DLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLALavrslrenlggeeyaerFLDAY 224

                          90
                  ....*....|....
gi 1397887290 201 -IPREDWDKwLAFY 213
Cdd:cd05150   225 gIDAPDPER-LAYY 237
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 41-205 2.00e-05

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: 44.91  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  41 LAVLSAQGI-VPKLVWTKrmENGDVITAQ----EWLDGNELNPEVLQHPKVAELLGRIHHSaeLLDMLTRIGKKPLQPAA 115
Cdd:cd05154    52 LRALAGTGVpVPRVLALC--EDPSVLGAPfyvmERVDGRVLPDPLPRPDLSPEERRALARS--LVDALAALHSVDPAALG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 116 L-------------VKDLRRDYQTLANEKLSLLviERALEYMETHlhIVEGIKPVVCHCDLNHNNWMITDRGELY-LIDW 181
Cdd:cd05154   128 LadlgrpegylerqVDRWRRQLEAAATDPPPAL--EEALRWLRAN--LPADGRPVLVHGDFRLGNLLFDPDGRVTaVLDW 203

                         170       180
                  ....*....|....*....|....*
gi 1397887290 182 DNAEIADPAIDL-SLLFKRYIPRED 205
Cdd:cd05154   204 ELATLGDPLEDLaWLLARWWRPGDP 228
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 40-212 4.43e-05

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase 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: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 43.79  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  40 FLAVLSAQGI-VPKLVWTK-----RMENGDVITAQEWLDGNEL---NPEVLQHpkVAELLGRIHHSAElldmltriGKKP 110
Cdd:cd05153    60 LLDHLAQAGLpVPRPLADKdgellGELNGKPAALFPFLPGESLttpTPEQCRA--IGAALARLHLALA--------GFPP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 111 LQPAALVKDLRRDYQTLANEKLSLLVI-ERAL---EYMETHLHIVEGIKPVVCHCDLNHNNwMITDRGELY-LIDWDNAE 185
Cdd:cd05153   130 PRPNPRGLAWWKPLAERLKARLDLLAAdDRALledELARLQALAPSDLPRGVIHADLFRDN-VLFDGDRLSgIIDFYDAC 208

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1397887290 186 IADPAIDLSLLFKRYI----PREDWDKWLAF 212
Cdd:cd05153   209 YDPLLYDLAIALNDWCfdddGKLDPERAKAL 239
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
4-239 4.72e-05

Fructosamine-3-kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 43.65  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290   4 ILGDDWIIESA----GGSTGEAYYAQSKHKRLFLKRNSSPFLAVLSA-----------QGI-VPKLVWTKRMENGDVItA 67
Cdd:COG3001    10 ALGPPFEITSVrpvsGGDINQAYRVTTDGRRVFVKLNPASPLGMFEAeaaglralaatGTIrVPEVIGVGTTGDHAFL-V 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  68 QEWLDGNELNPEvlqhpkVAELLGR----IH-HSAEL--LDMLTRIGKKPlQPAALVKD-------LRRDYQ-TLANEK- 131
Cdd:COG3001    89 LEYLELGPPTAG------AWERLGRqlaaLHqATAPRfgWDRDNFIGSTP-QPNTWTDDwaeffaeQRLGPQlQLAAEKg 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 132 ----LSLLVIERALEYMETHLHIVEgIKPVVCHCDLNHNNWMITDRGELYLID----WdnaeiADPAIDLSLL------- 196
Cdd:COG3001   162 llfaADRERIERLVERLPELLAPHE-PQPSLLHGDLWSGNVLFTADGEPVLIDpavyY-----GDREVDLAMTelfggfp 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1397887290 197 ---FKRYipREDWDKwlafygevnDEELTVRMYWYMFYELLTSLNH 239
Cdd:COG3001   236 dafYDAY--QEVWPL---------DPGYEERKPLYQLYHLLNHLNL 270
ETNK_euk cd05157
Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group ...
 41-180 1.13e-04

Euykaryotic Ethanolamine kinase; ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate, and displays negligible activity towards N-methylated derivatives of Etn. The Drosophila ETNK is implicated in development and neuronal function. Mammals contain two ETNK proteins, ETNK1 and ETNK2. ETNK1 selectively increases Etn uptake and phosphorylation, as well as PtdEtn synthesis. ETNK2 is found primarily in the liver and reproductive tissues. It plays a critical role in regulating placental hemostasis to support late embryonic development. It may also have a role in testicular maturation. ETNK 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: 270706 [Multi-domain]  Cd Length: 307  Bit Score: 42.57  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  41 LAVLSAQGIVPKLVwtKRMENGDVitaQEWLDGNELNPEVLQHPKVAEL----LGRIHHsaelLDMLTRIGKKPlqPAAL 116
Cdd:cd05157    50 LQLLSRAGIGPKLY--GRFENGRV---EEFLPGRTLTPEDLRDPKISRLiarrLAELHS----IVPLGEIEGKK--KPIL 118

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1397887290 117 VKDLRRdYQTLANEKLSLLVIERA------LEYMETHLHIVEGI------KPVV-CHCDLNHNNWMITDR-GELYLID 180
Cdd:cd05157   119 WTTIRK-WLDLAPEVFEDEKNKEKklekvdLERLRKELEWLEKWleslekSPIVfCHNDLLYGNILYNEDdDSVTFID 195
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 158-220 2.95e-04

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 40.33  E-value: 2.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1397887290 158 VCHCDLNHNNwMITDRGELYLIDWDNAEIADP----AIDLsLLFKRYI-------PREDWDKWLAFYGEVNDEE 220
Cdd:COG3642    72 IVHGDLTTSN-ILVDDGGVYLIDFGLARYSDPledkAVDL-AVLKRSLesthpdpAEELWEAFLEGYREVGPAE 143
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
 158-186 4.92e-04

3-deoxy-D-manno-octulosonic-acid kinase; Reviewed


Pssm-ID: 234975  Cd Length: 239  Bit Score: 40.64  E-value: 4.92e-04
                          10        20
                  ....*....|....*....|....*....
gi 1397887290 158 VCHCDLNHNNWMITDRGELYLIDWDNAEI 186
Cdd:PRK01723  163 VYHADLNAHNILLDPDGKFWLIDFDRGEL 191
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 156-197 6.15e-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: 39.21  E-value: 6.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1397887290 156 PVVCHCDLNHNNWMITDRGELY-LIDWDNAEIADPAIDLSLLF 197
Cdd:cd05120   111 SVLTHGDLHPGNILVKPDGKLSgIIDWEFAGYGPPAFDYAAAL 153
ChoK-like_euk cd14021
Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline ...
 40-197 1.46e-03

Euykaryotic Choline Kinase and similar proteins; This group is composed of eukaryotic choline kinase, ethanolamine kinase, and similar proteins. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK 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: 270923 [Multi-domain]  Cd Length: 229  Bit Score: 39.17  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  40 FLAVLSAQGIVPKLVwtkrmENGDVITAQEWLDGNEL------NPEVLQhpKVAELLGRIHhsaelldmltRIGKKPLqp 113
Cdd:cd14021    52 VFKILSEQGLGPKLI-----YKFDGGRIEEYIDGRPLttdelrNPSVLT--SIAKLLAKFH----------KIKTPPV-- 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 114 aalvkdlrrdyqtlaneklsllvieraleymethlhivegikpVVCHCDLNHNNWMITDRG-ELYLIDWDNAEIADPAID 192
Cdd:cd14021   113 -------------------------------------------VFCHNDLQENNILLTNDQdGLRLIDFEYSGFNYRGYD 149


                  ....*
gi 1397887290 193 LSLLF 197
Cdd:cd14021   150 IANFF 154
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 155-197 1.80e-03

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: 38.76  E-value: 1.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1397887290 155 KPVVCHCDLNHNNWMITDRGELY-LIDWDNAEIADPAIDLSLLF 197
Cdd:cd05152   184 HTVLVHGDLHPGHILVDEDGRVTgLIDWTEAKVGDPADDFAWHY 227
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
160-220 3.58e-03

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 38.33  E-value: 3.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290 160 HCDLNHNNwMITDRGELYLIDWD----NAEIADPAIDLSLLFK-----RYIPREDWDKWLAFYGEVNDEE 220
Cdd:PRK09605  451 HGDLTTSN-FIVRDDRLYLIDFGlgkySDLIEDKAVDLHVLKQslestHYDFEELWEAFLEGYRETEGAE 519
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
 137-213 5.99e-03

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


Pssm-ID: 214734  Cd Length: 196  Bit Score: 36.92  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1397887290  137 IERALEYMETHLHIVEGIKPVVCHCDLNHNN--WMITDRGEL---YLIDWDNAEIADPAIDLSLLF----KRYIPREDWD 207
Cdd:smart00587 101 LDNLEDLKKEDKEPDEGEFNVLNHGDLWANNimFKYDDEGKPedvALIDFQLSHYGSPAEDLHYFLltslSVEIRREHFD 180


                   ....*.
gi 1397887290  208 KWLAFY 213
Cdd:smart00587 181 ELLKFY 186
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 160-181 9.60e-03

C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain 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), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270695 [Multi-domain]  Cd Length: 183  Bit Score: 36.33  E-value: 9.60e-03
                          10        20
                  ....*....|....*....|..
gi 1397887290 160 HCDLNHNNWMITDRGELYLIDW 181
Cdd:cd05144   133 HGDFSEFNILVDEDEKITVIDF 154
 
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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