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Conserved domains on  [gi|693585953|gb|AIS39738|]
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hygromycin resistance protein [Cloning vector pNLCoI4[luc2-P2A-NlucP/PGK/Hygro]]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 27-238 6.83e-12

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd05120:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 158  Bit Score: 62.71  E-value: 6.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  27 QLSEGEESRAFSFDVGGRgYVLRV--NSCADGFYKDRYVYRHFAS-AALPIPEVLDIGEfSESLTYCISRRAQGVTLQDl 103
Cdd:cd05120    5 LIKEGGDNKVYLLGDPRE-YVLKIgpPRLKKDLEKEAAMLQLLAGkLSLPVPKVYGFGE-SDGWEYLLMERIEGETLSE- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953 104 petelpavlqpvaeamdaiaaadlsqtsgfgpfgpqgigqyttwrdficaiadphVYHWQTVMDDTV-SASVAQALDELm 182
Cdd:cd05120   82 -------------------------------------------------------VWPRLSEEEKEKiADQLAEILAAL- 105

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 693585953 183 lwaEDCPeVRHLVHADFGSNNVLTDN-GRITAVIDWSEAMFGDSQYEVANIFFWRPW 238
Cdd:cd05120  106 ---HRID-SSVLTHGDLHPGNILVKPdGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
 
Name Accession Description Interval E-value
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 27-238 6.83e-12

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: 62.71  E-value: 6.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  27 QLSEGEESRAFSFDVGGRgYVLRV--NSCADGFYKDRYVYRHFAS-AALPIPEVLDIGEfSESLTYCISRRAQGVTLQDl 103
Cdd:cd05120    5 LIKEGGDNKVYLLGDPRE-YVLKIgpPRLKKDLEKEAAMLQLLAGkLSLPVPKVYGFGE-SDGWEYLLMERIEGETLSE- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953 104 petelpavlqpvaeamdaiaaadlsqtsgfgpfgpqgigqyttwrdficaiadphVYHWQTVMDDTV-SASVAQALDELm 182
Cdd:cd05120   82 -------------------------------------------------------VWPRLSEEEKEKiADQLAEILAAL- 105

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 693585953 183 lwaEDCPeVRHLVHADFGSNNVLTDN-GRITAVIDWSEAMFGDSQYEVANIFFWRPW 238
Cdd:cd05120  106 ---HRID-SSVLTHGDLHPGNILVKPdGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 4-251 2.51e-11

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 63.60  E-value: 2.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953   4 PELTATSVEKFLIEKF---DSVSDLMQLSEGEESRAFSFDVGGRgYVLRVN----SCADGFYKDRYVYRHFAS-AALPIP 75
Cdd:COG3173    1 EELDEAALRALLAAQLpglAGLPEVEPLSGGWSNLTYRLDTGDR-LVLRRPprglASAHDVRREARVLRALAPrLGVPVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  76 EVLDIGEFSESL--TYCISRRAQGVTLQDLPETELPAVLQPVAEamdaiaaaDL-----------SQTSGFGPFGPQGIG 142
Cdd:COG3173   80 RPLALGEDGEVIgaPFYVMEWVEGETLEDALPDLSPAERRALAR--------ALgeflaalhavdPAAAGLADGRPEGLE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953 143 -QYTTWRDficaiadphvyHWQTVMDDTvsASVAQALDELMLW-AEDCPEVRH--LVHADFGSNNVLTD--NGRITAVID 216
Cdd:COG3173  152 rQLARWRA-----------QLRRALART--DDLPALRERLAAWlAANLPEWGPpvLVHGDLRPGNLLVDpdDGRLTAVID 218

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 693585953 217 WSEAMFGDSQYEVANI-FFWRPWLACMEQQTRYFER 251
Cdd:COG3173  219 WELATLGDPAADLAYLlLYWRLPDDLLGPRAAFLAA 254
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 24-265 3.99e-11

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: 62.13  E-value: 3.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953   24 DLMQLSEGEESRAFSFDVGGRGYVLRVNSC---ADGFYKDRYVYRHFASA-ALPIPEVLDIGEfSESLTYCISRRAQGVT 99
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDGRYVLRLPPPgraAEELRRELALLRHLAAAgVPPVPRVLAGCT-DAELLGLPFLLMEYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  100 LQDLpETELPAVLQPVAEAMDAIAAADLSQTSgFGPFGPQGIGQYTTWRD-FICAIADPHVYHWQTVMDDTVSASVAQAL 178
Cdd:pfam01636  80 GEVL-ARPLLPEERGALLEALGRALARLHAVD-PAALPLAGRLARLLELLrQLEAALARLLAAELLDRLEELEERLLAAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  179 DELmlWAEDCPEVrhLVHADFGSNNVL-TDNGRITAVIDWSEAMFGDSQYEVANIFfwrpWLACMEQQTRYFER--RHPE 255
Cdd:pfam01636 158 LAL--LPAELPPV--LVHGDLHPGNLLvDPGGRVSGVIDFEDAGLGDPAYDLAILL----NSWGRELGAELLAAylAAYG 229

                         250
                  ....*....|
gi 693585953  256 LAGSPRLRAY 265
Cdd:pfam01636 230 AFGYARLREL 239
 
Name Accession Description Interval E-value
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 27-238 6.83e-12

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: 62.71  E-value: 6.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  27 QLSEGEESRAFSFDVGGRgYVLRV--NSCADGFYKDRYVYRHFAS-AALPIPEVLDIGEfSESLTYCISRRAQGVTLQDl 103
Cdd:cd05120    5 LIKEGGDNKVYLLGDPRE-YVLKIgpPRLKKDLEKEAAMLQLLAGkLSLPVPKVYGFGE-SDGWEYLLMERIEGETLSE- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953 104 petelpavlqpvaeamdaiaaadlsqtsgfgpfgpqgigqyttwrdficaiadphVYHWQTVMDDTV-SASVAQALDELm 182
Cdd:cd05120   82 -------------------------------------------------------VWPRLSEEEKEKiADQLAEILAAL- 105

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 693585953 183 lwaEDCPeVRHLVHADFGSNNVLTDN-GRITAVIDWSEAMFGDSQYEVANIFFWRPW 238
Cdd:cd05120  106 ---HRID-SSVLTHGDLHPGNILVKPdGKLSGIIDWEFAGYGPPAFDYAAALRDWTE 158
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 4-251 2.51e-11

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 63.60  E-value: 2.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953   4 PELTATSVEKFLIEKF---DSVSDLMQLSEGEESRAFSFDVGGRgYVLRVN----SCADGFYKDRYVYRHFAS-AALPIP 75
Cdd:COG3173    1 EELDEAALRALLAAQLpglAGLPEVEPLSGGWSNLTYRLDTGDR-LVLRRPprglASAHDVRREARVLRALAPrLGVPVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  76 EVLDIGEFSESL--TYCISRRAQGVTLQDLPETELPAVLQPVAEamdaiaaaDL-----------SQTSGFGPFGPQGIG 142
Cdd:COG3173   80 RPLALGEDGEVIgaPFYVMEWVEGETLEDALPDLSPAERRALAR--------ALgeflaalhavdPAAAGLADGRPEGLE 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953 143 -QYTTWRDficaiadphvyHWQTVMDDTvsASVAQALDELMLW-AEDCPEVRH--LVHADFGSNNVLTD--NGRITAVID 216
Cdd:COG3173  152 rQLARWRA-----------QLRRALART--DDLPALRERLAAWlAANLPEWGPpvLVHGDLRPGNLLVDpdDGRLTAVID 218

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 693585953 217 WSEAMFGDSQYEVANI-FFWRPWLACMEQQTRYFER 251
Cdd:COG3173  219 WELATLGDPAADLAYLlLYWRLPDDLLGPRAAFLAA 254
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 24-265 3.99e-11

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: 62.13  E-value: 3.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953   24 DLMQLSEGEESRAFSFDVGGRGYVLRVNSC---ADGFYKDRYVYRHFASA-ALPIPEVLDIGEfSESLTYCISRRAQGVT 99
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDGRYVLRLPPPgraAEELRRELALLRHLAAAgVPPVPRVLAGCT-DAELLGLPFLLMEYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  100 LQDLpETELPAVLQPVAEAMDAIAAADLSQTSgFGPFGPQGIGQYTTWRD-FICAIADPHVYHWQTVMDDTVSASVAQAL 178
Cdd:pfam01636  80 GEVL-ARPLLPEERGALLEALGRALARLHAVD-PAALPLAGRLARLLELLrQLEAALARLLAAELLDRLEELEERLLAAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  179 DELmlWAEDCPEVrhLVHADFGSNNVL-TDNGRITAVIDWSEAMFGDSQYEVANIFfwrpWLACMEQQTRYFER--RHPE 255
Cdd:pfam01636 158 LAL--LPAELPPV--LVHGDLHPGNLLvDPGGRVSGVIDFEDAGLGDPAYDLAILL----NSWGRELGAELLAAylAAYG 229

                         250
                  ....*....|
gi 693585953  256 LAGSPRLRAY 265
Cdd:pfam01636 230 AFGYARLREL 239
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
174-271 2.78e-05

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 43.62  E-value: 2.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953 174 VAQALDELMLWAEDCPEVRHLVHADFGSNNVL-TDNGRITaVIDWSEAMFGDSQYEVANIFFWRPWLACMEQQ--TRYFE 250
Cdd:COG0510   31 LLRRLEELERALAARPLPLVLCHGDLHPGNFLvTDDGRLY-LIDWEYAGLGDPAFDLAALLVEYGLSPEQAEEllEAYGF 109

                         90       100
                 ....*....|....*....|.
gi 693585953 251 RRhPELAGSPRLRAYMLRIGL 271
Cdd:COG0510  110 GR-PTEELLRRLRAYRALADL 129
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 23-238 5.64e-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: 44.14  E-value: 5.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  23 SDLMQLSEGEESRAFSFDVG----GRGYVLRVNSCADGFYKDR-----Y-VYRHFASAALPIPEVLDIGEfSESLT---Y 89
Cdd:cd05154    1 LAVRRLSGGASNETYLVDAGgdggGRRLVLRRPPPGGLLPSAHdlereYrVLRALAGTGVPVPRVLALCE-DPSVLgapF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953  90 CISRRAQGVTL-QDLPETELPAVLQPVAEAMDAIAAADLS----QTSGFGPFGPQGIG---QYTTWRDficaiadphVYH 161
Cdd:cd05154   80 YVMERVDGRVLpDPLPRPDLSPEERRALARSLVDALAALHsvdpAALGLADLGRPEGYlerQVDRWRR---------QLE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953 162 WQTVMDDtvsasvaQALDELMLWAED-CPEVRH--LVHADFGSNNVL-TDNGRITAVIDWSEAMFGDSQYEVANI--FFW 235
Cdd:cd05154  151 AAATDPP-------PALEEALRWLRAnLPADGRpvLVHGDFRLGNLLfDPDGRVTAVLDWELATLGDPLEDLAWLlaRWW 223


                 ...
gi 693585953 236 RPW 238
Cdd:cd05154  224 RPG 226
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 176-224 5.73e-05

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: 44.16  E-value: 5.73e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 693585953 176 QALDELMLWaedcPEVRHLVHADFGSNNVLTD-NGRITAVIDWSEAMFGD 224
Cdd:cd05152  173 AWLADDSLW----PFHTVLVHGDLHPGHILVDeDGRVTGLIDWTEAKVGD 218
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 148-230 1.40e-04

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: 43.02  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953 148 RDFICAIADPHVYHW--------QTVMDDTVSASVAQALDEL----MLWAEDCPEVrhLVHADFGSNNVLTDNGRITAVI 215
Cdd:cd05153  125 AGFPPPRPNPRGLAWwkplaerlKARLDLLAADDRALLEDELarlqALAPSDLPRG--VIHADLFRDNVLFDGDRLSGII 202

                         90
                 ....*....|....*
gi 693585953 216 DWSEAMFGDSQYEVA 230
Cdd:cd05153  203 DFYDACYDPLLYDLA 217
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 162-276 6.18e-04

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: 41.06  E-value: 6.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693585953 162 WQTVMDDTVSASVAQALDELM-LWAEDCPEVRH-LVHADFGSNNVLTDNGRITAVIDWSEAMFGDSQYEVANIFFWRPWL 239
Cdd:COG2334  147 GPLLPDPEDRALLEELLDRLEaRLAPLLGALPRgVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLYDLAIALNGWADG 226

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 693585953 240 ACMEQQTRYF----ERRHP----ELAGSPRLRAY-MLRIGLDQLYQ 276
Cdd:COG2334  227 PLDPARLAALlegyRAVRPlteaELAALPPLLRLrALRFLAWRLRR 272
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
 173-217 2.12e-03

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: 39.10  E-value: 2.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 693585953 173 SVAQALDELmlwAEDCPEVRHLV--HADFGSNNVLTDNGRITAVIDW 217
Cdd:cd05150  145 TAEELLAEL---EATRPAEEDLVvtHGDACLPNIILDPGRFSGFIDL 188
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 195-224 2.31e-03

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include 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). These proteins 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-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: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 39.14  E-value: 2.31e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 693585953 195 VHADFGSNNVLTDNGRITAVIDWSEAMFGD 224
Cdd:cd05155  166 LHGDLHPGNLLVRDGRLSAVIDFGDLGVGD 195
 
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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