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Conserved domains on  [gi|495776083|ref|WP_008500662|]
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MULTISPECIES: fructosamine kinase family protein [Enterobacteriaceae]

Protein Classification

fructosamine kinase family protein( domain architecture ID 10511147)

fructosamine kinase family protein such as protein-ribulosamine 3-kinase, which catalyzes the phosphorylation of protein-bound ribulosamines that become unstable as a consequence and detach from proteins

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Fructosamin_kin pfam03881
Fructosamine kinase; This family includes eukaryotic fructosamine-3-kinase enzymes. The family ...
1-285 1.98e-167

Fructosamine kinase; This family includes eukaryotic fructosamine-3-kinase enzymes. The family also includes bacterial members that have not been characterized but probably have a similar or identical function.


:

Pssm-ID: 427564 [Multi-domain]  Cd Length: 288  Bit Score: 465.18  E-value: 1.98e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083    1 MWQAISHLLSEQLGEG-EIELRNELPGGEIHAAWHLRYAGRDLFVKCDERELLPIFTAEADQLELLSRSKTVTVPQVLAV 79
Cdd:pfam03881   1 MWQAIAQQLSEQTGKPfEITEREPVGGGDINQAYRLSDGEQRYFVKLNQREQLAMFEAEAEGLEALAETQTIRVPKVIAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083   80 GSDRDYSFLVMEYLPARPLDAHNAFILGQQLARLHQWSDQPQFGLDFDNDLSTTPQPNAWQRRWSTFFAEQRIGWQLELA 159
Cdd:pfam03881  81 GSSRDHSFLVLEYLELGPDNRGSAYELGQQLAKLHRWSGQKQFGFDFDNTIGSTPQPNTWQSSWADFFAEQRIGWQLQLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  160 AEKGLEFGNIDAIVEHVQQRLASHQPQASLLHGDLWSDNCALGPNG-PYIFDPACYWGDRECDLAMLPLHPEQPPQIYDG 238
Cdd:pfam03881 161 KEKGGNFGNIDRLVERVADLLAGHQPQPSLLHGDLWSGNAAFTADGePVIFDPACYYGDRECDLAMTELFGGFPPSFYEG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 495776083  239 YQSVSPLPPGFLDRQPVYQLYTLMNRAILFGGEHLVNAQRALERMLA 285
Cdd:pfam03881 241 YQSVWPLDEGYEDRKPLYQLYHLLNHLNLFGGGYLSQAQQLIDKLLA 287
 
Name Accession Description Interval E-value
Fructosamin_kin pfam03881
Fructosamine kinase; This family includes eukaryotic fructosamine-3-kinase enzymes. The family ...
1-285 1.98e-167

Fructosamine kinase; This family includes eukaryotic fructosamine-3-kinase enzymes. The family also includes bacterial members that have not been characterized but probably have a similar or identical function.


Pssm-ID: 427564 [Multi-domain]  Cd Length: 288  Bit Score: 465.18  E-value: 1.98e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083    1 MWQAISHLLSEQLGEG-EIELRNELPGGEIHAAWHLRYAGRDLFVKCDERELLPIFTAEADQLELLSRSKTVTVPQVLAV 79
Cdd:pfam03881   1 MWQAIAQQLSEQTGKPfEITEREPVGGGDINQAYRLSDGEQRYFVKLNQREQLAMFEAEAEGLEALAETQTIRVPKVIAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083   80 GSDRDYSFLVMEYLPARPLDAHNAFILGQQLARLHQWSDQPQFGLDFDNDLSTTPQPNAWQRRWSTFFAEQRIGWQLELA 159
Cdd:pfam03881  81 GSSRDHSFLVLEYLELGPDNRGSAYELGQQLAKLHRWSGQKQFGFDFDNTIGSTPQPNTWQSSWADFFAEQRIGWQLQLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  160 AEKGLEFGNIDAIVEHVQQRLASHQPQASLLHGDLWSDNCALGPNG-PYIFDPACYWGDRECDLAMLPLHPEQPPQIYDG 238
Cdd:pfam03881 161 KEKGGNFGNIDRLVERVADLLAGHQPQPSLLHGDLWSGNAAFTADGePVIFDPACYYGDRECDLAMTELFGGFPPSFYEG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 495776083  239 YQSVSPLPPGFLDRQPVYQLYTLMNRAILFGGEHLVNAQRALERMLA 285
Cdd:pfam03881 241 YQSVWPLDEGYEDRKPLYQLYHLLNHLNLFGGGYLSQAQQLIDKLLA 287
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
3-284 1.70e-136

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


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 386.86  E-value: 1.70e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083   3 QAISHLLSEQLGEG-EIELRNELPGGEIHAAWHLRYAGRDLFVKCDERELLPIFTAEADQLELLSRSKTVTVPQVLAVGS 81
Cdd:COG3001    1 QAIAEALSEALGPPfEITSVRPVSGGDINQAYRVTTDGRRVFVKLNPASPLGMFEAEAAGLRALAATGTIRVPEVIGVGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  82 DRDYSFLVMEYLPARPLDAHNAFILGQQLARLHQWSdQPQFGLDFDNDLSTTPQPNAWQRRWSTFFAEQRIGWQLELAAE 161
Cdd:COG3001   81 TGDHAFLVLEYLELGPPTAGAWERLGRQLAALHQAT-APRFGWDRDNFIGSTPQPNTWTDDWAEFFAEQRLGPQLQLAAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083 162 KGLEFG----NIDAIVEHVQQRLASHQPQASLLHGDLWSDNCALGPNG-PYIFDPACYWGDRECDLAMLPLHPEQPPQIY 236
Cdd:COG3001  160 KGLLFAadreRIERLVERLPELLAPHEPQPSLLHGDLWSGNVLFTADGePVLIDPAVYYGDREVDLAMTELFGGFPDAFY 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 495776083 237 DGYQSVSPLPPGFLDRQPVYQLYTLMNRAILFGGEHLVNAQRALERML 284
Cdd:COG3001  240 DAYQEVWPLDPGYEERKPLYQLYHLLNHLNLFGGSYLSQAERILDRLL 287
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
24-259 3.73e-10

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: 59.17  E-value: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  24 LPGGEIHAAWHLRYA----GRDLFVKCD-ERELLPIFTA---EADQLELLSRSkTVTVPQVLAVGSDRDY---SFLVMEY 92
Cdd:cd05154    6 LSGGASNETYLVDAGgdggGRRLVLRRPpPGGLLPSAHDlerEYRVLRALAGT-GVPVPRVLALCEDPSVlgaPFYVMER 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  93 LPARPLDAHN-------------AFILGQQLARLHQWsDQPQFGLDfdnDLSTTPQPNAWQ-RRWStffaeqrigWQLEL 158
Cdd:cd05154   85 VDGRVLPDPLprpdlspeerralARSLVDALAALHSV-DPAALGLA---DLGRPEGYLERQvDRWR---------RQLEA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083 159 AAEKGlefgniDAIVEHVQQRLASHQPQ---ASLLHGDLWSDNCalgpngpyIFDPA-----------CYWGDRECDLAM 224
Cdd:cd05154  152 AATDP------PPALEEALRWLRANLPAdgrPVLVHGDFRLGNL--------LFDPDgrvtavldwelATLGDPLEDLAW 217
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 495776083 225 LpLHPEQPPQIYDGYQSVSPLpPGFLDRQPVYQLY 259
Cdd:cd05154  218 L-LARWWRPGDPPGLAAPTRL-PGFPSREELLARY 250
 
Name Accession Description Interval E-value
Fructosamin_kin pfam03881
Fructosamine kinase; This family includes eukaryotic fructosamine-3-kinase enzymes. The family ...
1-285 1.98e-167

Fructosamine kinase; This family includes eukaryotic fructosamine-3-kinase enzymes. The family also includes bacterial members that have not been characterized but probably have a similar or identical function.


Pssm-ID: 427564 [Multi-domain]  Cd Length: 288  Bit Score: 465.18  E-value: 1.98e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083    1 MWQAISHLLSEQLGEG-EIELRNELPGGEIHAAWHLRYAGRDLFVKCDERELLPIFTAEADQLELLSRSKTVTVPQVLAV 79
Cdd:pfam03881   1 MWQAIAQQLSEQTGKPfEITEREPVGGGDINQAYRLSDGEQRYFVKLNQREQLAMFEAEAEGLEALAETQTIRVPKVIAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083   80 GSDRDYSFLVMEYLPARPLDAHNAFILGQQLARLHQWSDQPQFGLDFDNDLSTTPQPNAWQRRWSTFFAEQRIGWQLELA 159
Cdd:pfam03881  81 GSSRDHSFLVLEYLELGPDNRGSAYELGQQLAKLHRWSGQKQFGFDFDNTIGSTPQPNTWQSSWADFFAEQRIGWQLQLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  160 AEKGLEFGNIDAIVEHVQQRLASHQPQASLLHGDLWSDNCALGPNG-PYIFDPACYWGDRECDLAMLPLHPEQPPQIYDG 238
Cdd:pfam03881 161 KEKGGNFGNIDRLVERVADLLAGHQPQPSLLHGDLWSGNAAFTADGePVIFDPACYYGDRECDLAMTELFGGFPPSFYEG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 495776083  239 YQSVSPLPPGFLDRQPVYQLYTLMNRAILFGGEHLVNAQRALERMLA 285
Cdd:pfam03881 241 YQSVWPLDEGYEDRKPLYQLYHLLNHLNLFGGGYLSQAQQLIDKLLA 287
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
3-284 1.70e-136

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


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 386.86  E-value: 1.70e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083   3 QAISHLLSEQLGEG-EIELRNELPGGEIHAAWHLRYAGRDLFVKCDERELLPIFTAEADQLELLSRSKTVTVPQVLAVGS 81
Cdd:COG3001    1 QAIAEALSEALGPPfEITSVRPVSGGDINQAYRVTTDGRRVFVKLNPASPLGMFEAEAAGLRALAATGTIRVPEVIGVGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  82 DRDYSFLVMEYLPARPLDAHNAFILGQQLARLHQWSdQPQFGLDFDNDLSTTPQPNAWQRRWSTFFAEQRIGWQLELAAE 161
Cdd:COG3001   81 TGDHAFLVLEYLELGPPTAGAWERLGRQLAALHQAT-APRFGWDRDNFIGSTPQPNTWTDDWAEFFAEQRLGPQLQLAAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083 162 KGLEFG----NIDAIVEHVQQRLASHQPQASLLHGDLWSDNCALGPNG-PYIFDPACYWGDRECDLAMLPLHPEQPPQIY 236
Cdd:COG3001  160 KGLLFAadreRIERLVERLPELLAPHEPQPSLLHGDLWSGNVLFTADGePVLIDPAVYYGDREVDLAMTELFGGFPDAFY 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 495776083 237 DGYQSVSPLPPGFLDRQPVYQLYTLMNRAILFGGEHLVNAQRALERML 284
Cdd:COG3001  240 DAYQEVWPLDPGYEERKPLYQLYHLLNHLNLFGGSYLSQAERILDRLL 287
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
3-238 3.28e-20

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 87.86  E-value: 3.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083   3 QAISHLLSEQLGE--GEIELRnELPGGEIHAAWHLRyAGRDLFVKCDERELLPI--FTAEADQLELLSRSKTVTVPQVLA 78
Cdd:COG3173    6 AALRALLAAQLPGlaGLPEVE-PLSGGWSNLTYRLD-TGDRLVLRRPPRGLASAhdVRREARVLRALAPRLGVPVPRPLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  79 VGSDRD---YSFLVMEYLPARPLD-----------AHNAFILGQQLARLHQwSDQPQFGLDFDNDLSTTPQPNAWQRRWS 144
Cdd:COG3173   84 LGEDGEvigAPFYVMEWVEGETLEdalpdlspaerRALARALGEFLAALHA-VDPAAAGLADGRPEGLERQLARWRAQLR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083 145 TFFAEQRigwqlelaaekglefgNIDAIVEHVQQRLASHQP---QASLLHGDLWSDNCALGPNGPYI-----FDPACyWG 216
Cdd:COG3173  163 RALARTD----------------DLPALRERLAAWLAANLPewgPPVLVHGDLRPGNLLVDPDDGRLtavidWELAT-LG 225
                        250       260
                 ....*....|....*....|..
gi 495776083 217 DRECDLAMLPLHPEQPPQIYDG 238
Cdd:COG3173  226 DPAADLAYLLLYWRLPDDLLGP 247
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
23-225 3.78e-17

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: 78.70  E-value: 3.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083   23 ELPGGEIHAAWHLRYAGRDLFVK-CDERELLPIFTAEADQLELLSRSKTVTVPQVLAVGSDRDYS---FLVMEYLPARPL 98
Cdd:pfam01636   4 PISSGASNRTYLVTTGDGRYVLRlPPPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDAELLglpFLLMEYLPGEVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083   99 DAHN--------AFILGQQLARLHQwsdqpqfgldfdndLSTTPQPNAWQRRWSTFFAEQRIGWQLELAAEKGLEFgnID 170
Cdd:pfam01636  84 ARPLlpeergalLEALGRALARLHA--------------VDPAALPLAGRLARLLELLRQLEAALARLLAAELLDR--LE 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495776083  171 AIVEHVQQRLASHQPQAS---LLHGDLWSDNCALGPNGPYI----FDPACyWGDRECDLAML 225
Cdd:pfam01636 148 ELEERLLAALLALLPAELppvLVHGDLHPGNLLVDPGGRVSgvidFEDAG-LGDPAYDLAIL 208
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
24-259 3.73e-10

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: 59.17  E-value: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  24 LPGGEIHAAWHLRYA----GRDLFVKCD-ERELLPIFTA---EADQLELLSRSkTVTVPQVLAVGSDRDY---SFLVMEY 92
Cdd:cd05154    6 LSGGASNETYLVDAGgdggGRRLVLRRPpPGGLLPSAHDlerEYRVLRALAGT-GVPVPRVLALCEDPSVlgaPFYVMER 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  93 LPARPLDAHN-------------AFILGQQLARLHQWsDQPQFGLDfdnDLSTTPQPNAWQ-RRWStffaeqrigWQLEL 158
Cdd:cd05154   85 VDGRVLPDPLprpdlspeerralARSLVDALAALHSV-DPAALGLA---DLGRPEGYLERQvDRWR---------RQLEA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083 159 AAEKGlefgniDAIVEHVQQRLASHQPQ---ASLLHGDLWSDNCalgpngpyIFDPA-----------CYWGDRECDLAM 224
Cdd:cd05154  152 AATDP------PPALEEALRWLRANLPAdgrPVLVHGDFRLGNL--------LFDPDgrvtavldwelATLGDPLEDLAW 217
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 495776083 225 LpLHPEQPPQIYDGYQSVSPLpPGFLDRQPVYQLY 259
Cdd:cd05154  218 L-LARWWRPGDPPGLAAPTRL-PGFPSREELLARY 250
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
61-251 1.68e-09

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: 57.63  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  61 QLELLS--RSKTVTVPQVLA------VGSDRDYSFLVMEYLPARPLDAHNA---FILGQQLARLHQWSDqpqfglDFdnd 129
Cdd:COG2334   57 ELALLAhlAAAGLPVPAPVPtrdgetLLELEGRPAALFPFLPGRSPEEPSPeqlEELGRLLARLHRALA------DF--- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083 130 lsttPQPNAWQRRWSTFFAEQRIGWQLELAAEKGLefgnIDAIVEHVQQRLASHQPQ--ASLLHGDLWSDNCALGPNG-P 206
Cdd:COG2334  128 ----PRPNARDLAWWDELLERLLGPLLPDPEDRAL----LEELLDRLEARLAPLLGAlpRGVIHGDLHPDNVLFDGDGvS 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495776083 207 YI--FDPACYwGDRECDLAML----PLHPEQPPQ---IYDGYQSVSPLPPGFLD 251
Cdd:COG2334  200 GLidFDDAGY-GPRLYDLAIAlngwADGPLDPARlaaLLEGYRAVRPLTEAELA 252
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
33-131 2.76e-07

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: 50.27  E-value: 2.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  33 WHLRYAGRDLFVKCDERELLPIFTAEADQLELLSRskTVTVPQVLAVGSDRDYSFLVMEYLPARPLDAHNAF-------- 104
Cdd:cd05150   16 YRLDGGGPVLYLKTAPAGYAYELAREAERLRWLAG--KLPVPEVLDYGSDDGGDWLLTTALPGRDAASLEPLldperlvd 93
                         90       100
                 ....*....|....*....|....*....
gi 495776083 105 ILGQQLARLHQ--WSDQPqfgldFDNDLS 131
Cdd:cd05150   94 LLAEALRALHSlpIADCP-----FDRRLD 117
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
32-115 4.95e-05

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: 42.68  E-value: 4.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  32 AWHLRyAGRDLFVKCDERELLPIFTAEADQLELLSRSKTVTVPQVLAVGSDRDYSFLVMEYLPARPLD-----------A 100
Cdd:cd05120   14 VYLLG-DPREYVLKIGPPRLKKDLEKEAAMLQLLAGKLSLPVPKVYGFGESDGWEYLLMERIEGETLSevwprlseeekE 92
                         90
                 ....*....|....*
gi 495776083 101 HNAFILGQQLARLHQ 115
Cdd:cd05120   93 KIADQLAEILAALHR 107
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
9-101 1.32e-04

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 43.08  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083   9 LSEQLGEGeielrnelPGGEIHAAWHLRyAGRDLFVKcderELLPIFTAEADQLELLSRSKTVT-------VPQVLAVGS 81
Cdd:COG0515   11 ILRLLGRG--------GMGVVYLARDLR-LGRPVALK----VLRPELAADPEARERFRREARALarlnhpnIVRVYDVGE 77
                         90       100
                 ....*....|....*....|
gi 495776083  82 DRDYSFLVMEYLPARPLDAH 101
Cdd:COG0515   78 EDGRPYLVMEYVEGESLADL 97
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
61-247 5.00e-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: 41.09  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  61 QLELLS--RSKTVTVPQVLAVGSDRDYSFL------VMEYLPARPLDAHNA---FILGQQLARLHqwsdqpQFGLDFdnd 129
Cdd:cd05153   57 ELELLDhlAQAGLPVPRPLADKDGELLGELngkpaaLFPFLPGESLTTPTPeqcRAIGAALARLH------LALAGF--- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083 130 lsTTPQPNAWQRRWSTFFAEQrigwqleLAAEKGLEFGNIDAIVEHVQQRLASHQPQA---SLLHGDLWSDN-------- 198
Cdd:cd05153  128 --PPPRPNPRGLAWWKPLAER-------LKARLDLLAADDRALLEDELARLQALAPSDlprGVIHADLFRDNvlfdgdrl 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083 199 CALgpngpyI-FDPACYwGDRECDLAMLPLH------PEQPPQIY----DGYQSVSPLPP 247
Cdd:cd05153  199 SGI------IdFYDACY-DPLLYDLAIALNDwcfdddGKLDPERAkallAGYQSVRPLTE 251
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
169-246 1.06e-03

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 38.99  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083 169 IDAIVEHVQQRLASHQPQASLLHGDLWSDNCALGPNG-PYIFDP--ACyWGDRECDLAML----PLHPEQPPQIYDGYQS 241
Cdd:COG0510   31 LLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGrLYLIDWeyAG-LGDPAFDLAALlveyGLSPEQAEELLEAYGF 109

                 ....*
gi 495776083 242 VSPLP 246
Cdd:COG0510  110 GRPTE 114
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
57-134 2.74e-03

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: 37.63  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495776083  57 AEADQLELLsRSKTVTVPQVLAVGSDRDYsfLVMEYLPARPL---------DAHNAFILGQQLARLHQ------------ 115
Cdd:COG3642    5 REARLLREL-REAGVPVPKVLDVDPDDAD--LVMEYIEGETLadlleegelPPELLRELGRLLARLHRagivhgdlttsn 81
                         90       100
                 ....*....|....*....|.
gi 495776083 116 --WSDQPQFGLDFDNDLSTTP 134
Cdd:COG3642   82 ilVDDGGVYLIDFGLARYSDP 102
 
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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