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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636  13 PAGGSTGSAFLGVYANQKYFLK------------RNASPFLAALSVEHITPRLLWTRRVSTGDVLtaqEWLDGETLTREQ 80
Cdd:cd05151    6 LKGGLTNKNYLVEVAGKKYVLRipgagtellidrENEKANSKAAAELGIAPEVIYFDPETGVKIT---EFIEGATLLTND 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636  81 MMQPV----VASMLAKVHHSSLLKrmlrqvggqvldpdqlrqsllqnfpenlaaqprveqalaeiqrWVPrvtvqsvCHG 156
Cdd:cd05151   83 FSDPEnlerIAALLRKLHSSPLED-------------------------------------------LVL-------CHN 112

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 896155636 157 DLNHKNWLRANGRLYLVDWEQVALGDPAYDLADVM 191
Cdd:cd05151  113 DLVPGNFLLDDDRLYLIDWEYAGMNDPLFDLAALF 147

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636   12 QPAGGSTGSAFLGVYANQKYFLKRNASP--------------FLAALSVEHItPRLLWTRRVST--GDVLTAQEWLDGET 75
Cdd:pfam01636   4 PISSGASNRTYLVTTGDGRYVLRLPPPGraaeelrrelallrHLAAAGVPPV-PRVLAGCTDAEllGLPFLLMEYLPGEV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636   76 LTREQMMQPV------VASMLAKVHHSSLLKRMLRQVGGQVLDPDQLRQSLLQN--FPENLAAQPR-VEQALAEIQRWVP 146
Cdd:pfam01636  83 LARPLLPEERgalleaLGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARllAAELLDRLEElEERLLAALLALLP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896155636  147 RVTVQSVCHGDLNHKNWL-RANGRL-YLVDWEQVALGDPAYDLADVMAHYGnHDTWPAFLAAYGA 209
Cdd:pfam01636 163 AELPPVLVHGDLHPGNLLvDPGGRVsGVIDFEDAGLGDPAYDLAILLNSWG-RELGAELLAAYLA 226

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636  69 EWLDGE---TLTREQMMQpvVASMLAKVHHSSLlKRMLRQVGGQVLDPDQ-LRQSLLQNFPENLAAQ-PRVEQALAEIQR 143
Cdd:cd05153   95 PFLPGEsltTPTPEQCRA--IGAALARLHLALA-GFPPPRPNPRGLAWWKpLAERLKARLDLLAADDrALLEDELARLQA 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896155636 144 WVPRVTVQSVCHGDLNHKNWLRANGRLY-LVDWEQVALGDPAYDLADVM-------AHYGNHDTWPAFLAAYGA 209
Cdd:cd05153  172 LAPSDLPRGVIHADLFRDNVLFDGDRLSgIIDFYDACYDPLLYDLAIALndwcfddDGKLDPERAKALLAGYQS 245

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636   12 QPAGGSTGSAFLGVYANQKYFLKRNASP--------------FLAALSVEHItPRLLWTRRVST--GDVLTAQEWLDGET 75
Cdd:pfam01636   4 PISSGASNRTYLVTTGDGRYVLRLPPPGraaeelrrelallrHLAAAGVPPV-PRVLAGCTDAEllGLPFLLMEYLPGEV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636   76 LTREQMMQPV------VASMLAKVHHSSLLKRMLRQVGGQVLDPDQLRQSLLQN--FPENLAAQPR-VEQALAEIQRWVP 146
Cdd:pfam01636  83 LARPLLPEERgalleaLGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARllAAELLDRLEElEERLLAALLALLP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896155636  147 RVTVQSVCHGDLNHKNWL-RANGRL-YLVDWEQVALGDPAYDLADVMAHYGnHDTWPAFLAAYGA 209
Cdd:pfam01636 163 AELPPVLVHGDLHPGNLLvDPGGRVsGVIDFEDAGLGDPAYDLAILLNSWG-RELGAELLAAYLA 226

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636  69 EWLDG---ETLTREQMMQpvVASMLAKVHHssLLKRMLRQVGGQVLDPDQLRQSLLQNFPENLAAQPRVEQALAEIQRWV 145
Cdd:COG2334   95 PFLPGrspEEPSPEQLEE--LGRLLARLHR--ALADFPRPNARDLAWWDELLERLLGPLLPDPEDRALLEELLDRLEARL 170

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896155636 146 PRVT---VQSVCHGDLNHKNWLRANGRL-YLVDWEQVALGDPAYDLADVMAHYGNHDTWP----AFLAAYGA 209
Cdd:COG2334  171 APLLgalPRGVIHGDLHPDNVLFDGDGVsGLIDFDDAGYGPRLYDLAIALNGWADGPLDParlaALLEGYRA 242

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636  69 EWLDGE---TLTREQMMQpvVASMLAKVHHSSLlKRMLRQVGGQVLDPDQ-LRQSLLQNFPENLAAQ-PRVEQALAEIQR 143
Cdd:cd05153   95 PFLPGEsltTPTPEQCRA--IGAALARLHLALA-GFPPPRPNPRGLAWWKpLAERLKARLDLLAADDrALLEDELARLQA 171

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896155636 144 WVPRVTVQSVCHGDLNHKNWLRANGRLY-LVDWEQVALGDPAYDLADVM-------AHYGNHDTWPAFLAAYGA 209
Cdd:cd05153  172 LAPSDLPRGVIHADLFRDNVLFDGDRLSgIIDFYDACYDPLLYDLAIALndwcfddDGKLDPERAKALLAGYQS 245

class V lanthionine synthetase subunit LxmK;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896155636 119 SLLQNFPENLAAqprVEqALAEIQRWVPRVTVqsvcHGDLNHKNWLRANGRLYLVDWEQVALGDPAYDL 187
Cdd:NF038156 167 RLLQNDAELVAA---LR-RLREREAAAPRVPV----HGDLRLDQFLVADGRLYLTDWEEFRLGDPARDV 227

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636 135 EQALAEIQRWVPRVTVQSVCHGDLNHKNWLRANGRL-YLVDWEQVALGDPAYDLADVM---AHYGNHDTWPA-FLAAYGA 209
Cdd:cd05150  147 EELLAELEATRPAEEDLVVTHGDACLPNIILDPGRFsGFIDLGRLGVADRYQDLALAVrslRENLGGEEYAErFLDAYGI 226

                         90
                 ....*....|...
gi 896155636 210 NMDDhlQHRLYWY 222
Cdd:cd05150  227 DAPD--PERLAYY 237

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636  67 AQEWLDGETLTREQMMQPVVASMLAK---VHHSSLLKRMLRQVGGQVLDP------DQLRQSLLQNFPENLAAQ----PR 133
Cdd:cd05157   71 VEEFLPGRTLTPEDLRDPKISRLIARrlaELHSIVPLGEIEGKKKPILWTtirkwlDLAPEVFEDEKNKEKKLEkvdlER 150

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896155636 134 VEQALAEIQRWVPRVTVQSV--CHGDLNHKN--WLRANGRLYLVDWEQVALGDPAYDLAdvmahygNH 197
Cdd:cd05157  151 LRKELEWLEKWLESLEKSPIvfCHNDLLYGNilYNEDDDSVTFIDFEYAGPNPRAFDIA-------NH 211

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).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636  68 QEWLDGETLTREQMMQPVV----ASMLAKVHhssllKRMLRQVGgqvldpdqlrqsllqnfpenlaaqprveqalaeiqr 143
Cdd:cd14021   75 EEYIDGRPLTTDELRNPSVltsiAKLLAKFH-----KIKTPPVV------------------------------------ 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896155636 144 wvprvtvqsVCHGDLNHKNWLR--ANGRLYLVDWEQVALGDPAYDLADVM--AHYGN-HDTWPAFLAAYganmDDHLQHR 218
Cdd:cd14021  114 ---------FCHNDLQENNILLtnDQDGLRLIDFEYSGFNYRGYDIANFFneSMIDYdHPEPPYFKIYK----ENYISEE 180

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 896155636 219 LYWYSDLHLLSDMK-TAALHQRSDEVAKALRQFEVLQ 254
Cdd:cd14021  181 EKRLFVSVYLSEYLeKNVLPSLDKLVEQFLQEVEIFT 217

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).

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 896155636 155 HGDLNHKNWLRANGRLY-LVDWEQVALGDPAYDLA 188
Cdd:cd05155  167 HGDLHPGNLLVRDGRLSaVIDFGDLGVGDPACDLA 201