NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|501626018|ref|WP_012603955|]
View 

MULTISPECIES: fructosamine kinase family protein [Vibrio]

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

show extra options »

Show site features     Horizontal zoom: ×

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 ...
1-287 4.66e-180

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: 497.15  E-value: 4.66e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018    1 MWQAISQQLSDTLLFNFQITERTKVSGGDINDCYMISDGNERYFVKVNQREFLPKFEIEAENLRLLRETSTVYVPELVLI 80
Cdd:pfam03881   1 MWQAIAQQLSEQTGKPFEITEREPVGGGDINQAYRLSDGEQRYFVKLNQREQLAMFEAEAEGLEALAETQTIRVPKVIAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018   81 GKTKECSFIILNYLPTKPlETSNNSYDFGVQLAQLHQWGEQKEFGCDQDNYIGSTLQPNPWHKKWGRFFSEQRIGFQLQL 160
Cdd:pfam03881  81 GSSRDHSFLVLEYLELGP-DNRGSAYELGQQLAKLHRWSGQKQFGFDFDNTIGSTPQPNTWQSSWADFFAEQRIGWQLQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  161 LKEKGIEFGDIDDIVDVVNMRLAGHNPRPSLLHGDLWNGNVANSAFG-PICYDPACYWGDHECDLALTELFEGFSKEFYE 239
Cdd:pfam03881 160 AKEKGGNFGNIDRLVERVADLLAGHQPQPSLLHGDLWSGNAAFTADGePVIFDPACYYGDRECDLAMTELFGGFPPSFYE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 501626018  240 GYQSVNPLDVGYTDRKDIYNLYHLLNHCNQFGGEYLAQTEACIQKIQA 287
Cdd:pfam03881 240 GYQSVWPLDEGYEDRKPLYQLYHLLNHLNLFGGGYLSQAQQLIDKLLA 287
 
Name Accession Description Interval E-value
Fructosamin_kin pfam03881
Fructosamine kinase; This family includes eukaryotic fructosamine-3-kinase enzymes. The family ...
1-287 4.66e-180

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: 497.15  E-value: 4.66e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018    1 MWQAISQQLSDTLLFNFQITERTKVSGGDINDCYMISDGNERYFVKVNQREFLPKFEIEAENLRLLRETSTVYVPELVLI 80
Cdd:pfam03881   1 MWQAIAQQLSEQTGKPFEITEREPVGGGDINQAYRLSDGEQRYFVKLNQREQLAMFEAEAEGLEALAETQTIRVPKVIAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018   81 GKTKECSFIILNYLPTKPlETSNNSYDFGVQLAQLHQWGEQKEFGCDQDNYIGSTLQPNPWHKKWGRFFSEQRIGFQLQL 160
Cdd:pfam03881  81 GSSRDHSFLVLEYLELGP-DNRGSAYELGQQLAKLHRWSGQKQFGFDFDNTIGSTPQPNTWQSSWADFFAEQRIGWQLQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  161 LKEKGIEFGDIDDIVDVVNMRLAGHNPRPSLLHGDLWNGNVANSAFG-PICYDPACYWGDHECDLALTELFEGFSKEFYE 239
Cdd:pfam03881 160 AKEKGGNFGNIDRLVERVADLLAGHQPQPSLLHGDLWSGNAAFTADGePVIFDPACYYGDRECDLAMTELFGGFPPSFYE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 501626018  240 GYQSVNPLDVGYTDRKDIYNLYHLLNHCNQFGGEYLAQTEACIQKIQA 287
Cdd:pfam03881 240 GYQSVWPLDEGYEDRKPLYQLYHLLNHLNLFGGGYLSQAQQLIDKLLA 287
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
3-285 1.08e-145

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


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 410.36  E-value: 1.08e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018   3 QAISQQLSDTLLFNFQITERTKVSGGDINDCYMISDGNERYFVKVNQREFLPKFEIEAENLRLLRETSTVYVPELVLIGK 82
Cdd:COG3001    1 QAIAEALSEALGPPFEITSVRPVSGGDINQAYRVTTDGRRVFVKLNPASPLGMFEAEAAGLRALAATGTIRVPEVIGVGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  83 TKECSFIILNYLPTKPLeTSNNSYDFGVQLAQLHQWGeQKEFGCDQDNYIGSTLQPNPWHKKWGRFFSEQRIGFQLQLLK 162
Cdd:COG3001   81 TGDHAFLVLEYLELGPP-TAGAWERLGRQLAALHQAT-APRFGWDRDNFIGSTPQPNTWTDDWAEFFAEQRLGPQLQLAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018 163 EKGIEFG----DIDDIVDVVNMRLAGHNPRPSLLHGDLWNGNVANSAFG-PICYDPACYWGDHECDLALTELFEGFSKEF 237
Cdd:COG3001  159 EKGLLFAadreRIERLVERLPELLAPHEPQPSLLHGDLWSGNVLFTADGePVLIDPAVYYGDREVDLAMTELFGGFPDAF 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 501626018 238 YEGYQSVNPLDVGYTDRKDIYNLYHLLNHCNQFGGEYLAQTEACIQKI 285
Cdd:COG3001  239 YDAYQEVWPLDPGYEERKPLYQLYHLLNHLNLFGGSYLSQAERILDRL 286
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
28-247 7.25e-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: 43.40  E-value: 7.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  28 GDINDCYMISDG--NERYFVKVNQREF-------LPKFEIEAENLRLLRETSTVYVP----------ELVLIGKTKECsf 88
Cdd:cd05153   14 GELLSFEGIAAGieNTNYFVTTTDGRYvltlfekRRSAAELPFELELLDHLAQAGLPvprpladkdgELLGELNGKPA-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  89 IILNYLPTKPLETSN--NSYDFGVQLAQLHQWGEQKEFGCDQDnyigstLQPNPWHKKWGRF--FSEQRIGFQLQLLKEK 164
Cdd:cd05153   92 ALFPFLPGESLTTPTpeQCRAIGAALARLHLALAGFPPPRPNP------RGLAWWKPLAERLkaRLDLLAADDRALLEDE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018 165 giefgdIDDIvdvvnMRLAGHNPRPSLLHGDLWNGNV---ANSAFGPICYDPACYwGDHECDLALT----------ELFE 231
Cdd:cd05153  166 ------LARL-----QALAPSDLPRGVIHADLFRDNVlfdGDRLSGIIDFYDACY-DPLLYDLAIAlndwcfdddgKLDP 233
                        250
                 ....*....|....*.
gi 501626018 232 GFSKEFYEGYQSVNPL 247
Cdd:cd05153  234 ERAKALLAGYQSVRPL 249
 
Name Accession Description Interval E-value
Fructosamin_kin pfam03881
Fructosamine kinase; This family includes eukaryotic fructosamine-3-kinase enzymes. The family ...
1-287 4.66e-180

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: 497.15  E-value: 4.66e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018    1 MWQAISQQLSDTLLFNFQITERTKVSGGDINDCYMISDGNERYFVKVNQREFLPKFEIEAENLRLLRETSTVYVPELVLI 80
Cdd:pfam03881   1 MWQAIAQQLSEQTGKPFEITEREPVGGGDINQAYRLSDGEQRYFVKLNQREQLAMFEAEAEGLEALAETQTIRVPKVIAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018   81 GKTKECSFIILNYLPTKPlETSNNSYDFGVQLAQLHQWGEQKEFGCDQDNYIGSTLQPNPWHKKWGRFFSEQRIGFQLQL 160
Cdd:pfam03881  81 GSSRDHSFLVLEYLELGP-DNRGSAYELGQQLAKLHRWSGQKQFGFDFDNTIGSTPQPNTWQSSWADFFAEQRIGWQLQL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  161 LKEKGIEFGDIDDIVDVVNMRLAGHNPRPSLLHGDLWNGNVANSAFG-PICYDPACYWGDHECDLALTELFEGFSKEFYE 239
Cdd:pfam03881 160 AKEKGGNFGNIDRLVERVADLLAGHQPQPSLLHGDLWSGNAAFTADGePVIFDPACYYGDRECDLAMTELFGGFPPSFYE 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 501626018  240 GYQSVNPLDVGYTDRKDIYNLYHLLNHCNQFGGEYLAQTEACIQKIQA 287
Cdd:pfam03881 240 GYQSVWPLDEGYEDRKPLYQLYHLLNHLNLFGGGYLSQAQQLIDKLLA 287
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
3-285 1.08e-145

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


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 410.36  E-value: 1.08e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018   3 QAISQQLSDTLLFNFQITERTKVSGGDINDCYMISDGNERYFVKVNQREFLPKFEIEAENLRLLRETSTVYVPELVLIGK 82
Cdd:COG3001    1 QAIAEALSEALGPPFEITSVRPVSGGDINQAYRVTTDGRRVFVKLNPASPLGMFEAEAAGLRALAATGTIRVPEVIGVGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  83 TKECSFIILNYLPTKPLeTSNNSYDFGVQLAQLHQWGeQKEFGCDQDNYIGSTLQPNPWHKKWGRFFSEQRIGFQLQLLK 162
Cdd:COG3001   81 TGDHAFLVLEYLELGPP-TAGAWERLGRQLAALHQAT-APRFGWDRDNFIGSTPQPNTWTDDWAEFFAEQRLGPQLQLAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018 163 EKGIEFG----DIDDIVDVVNMRLAGHNPRPSLLHGDLWNGNVANSAFG-PICYDPACYWGDHECDLALTELFEGFSKEF 237
Cdd:COG3001  159 EKGLLFAadreRIERLVERLPELLAPHEPQPSLLHGDLWSGNVLFTADGePVLIDPAVYYGDREVDLAMTELFGGFPDAF 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 501626018 238 YEGYQSVNPLDVGYTDRKDIYNLYHLLNHCNQFGGEYLAQTEACIQKI 285
Cdd:COG3001  239 YDAYQEVWPLDPGYEERKPLYQLYHLLNHLNLFGGSYLSQAERILDRL 286
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
23-241 1.24e-12

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: 65.99  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018   23 TKVSGGDINDCYMISDGNERYFVKV-NQREFLPKFEIEAENLRLLRETSTVYVPELVLIGKT---KECSFIILNYLPTKP 98
Cdd:pfam01636   3 RPISSGASNRTYLVTTGDGRYVLRLpPPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDaelLGLPFLLMEYLPGEV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018   99 LETSNNS-------YDFGVQLAQLHQwgeqkefgcdqdnyIGSTLQPNPWHKKWGRFFSEQRIGFQLQLLKEKgiEFGDI 171
Cdd:pfam01636  83 LARPLLPeergallEALGRALARLHA--------------VDPAALPLAGRLARLLELLRQLEAALARLLAAE--LLDRL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  172 DDIVDVVNMRLAGHNP---RPSLLHGDLWNGNVANSAFGPI-----CYDpaCYWGDHECDLA--LTELFEGFSKEFYEGY 241
Cdd:pfam01636 147 EELEERLLAALLALLPaelPPVLVHGDLHPGNLLVDPGGRVsgvidFED--AGLGDPAYDLAilLNSWGRELGAELLAAY 224
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
23-241 1.96e-11

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 63.21  E-value: 1.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  23 TKVSGGDINDCYMISDGnERYFVKVNQREFLPKFEI--EAENLRLLRETSTVYVPELVLIGKTKE---CSFIILNYLP-- 95
Cdd:COG3173   26 EPLSGGWSNLTYRLDTG-DRLVLRRPPRGLASAHDVrrEARVLRALAPRLGVPVPRPLALGEDGEvigAPFYVMEWVEge 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  96 --------TKPLETSNNSYDFGVQLAQLHQWgEQKEFGCDQDNYIGSTLQPNPWHKKWGRFFSEQRigfqlqllkekgie 167
Cdd:COG3173  105 tledalpdLSPAERRALARALGEFLAALHAV-DPAAAGLADGRPEGLERQLARWRAQLRRALARTD-------------- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018 168 fgDIDDIVDVVNMRLAGHNP---RPSLLHGDLWNGNVansafgpiCYDPA------------CYWGDHECDLALTEL--- 229
Cdd:COG3173  170 --DLPALRERLAAWLAANLPewgPPVLVHGDLRPGNL--------LVDPDdgrltavidwelATLGDPAADLAYLLLywr 239
                        250
                 ....*....|....*.
gi 501626018 230 ----FEGFSKEFYEGY 241
Cdd:COG3173  240 lpddLLGPRAAFLAAY 255
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
38-248 9.97e-07

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: 49.15  E-value: 9.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  38 DGNERYFVKVNQREFLPKFEIEAEnLRLLRE--TSTVYVPELV------LIGKTKECSFIILNYLPTKPLETSNNS--YD 107
Cdd:COG2334   34 EDGRRYVLKLYRPGRWSPEEIPFE-LALLAHlaAAGLPVPAPVptrdgeTLLELEGRPAALFPFLPGRSPEEPSPEqlEE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018 108 FGVQLAQLHQwgeqkefgcdqdnyIGSTLQPNPWHKKWGRFFSEQRIGFQLQLLKEkgiEFGDIDDIVDVVNMRLAGHNP 187
Cdd:COG2334  113 LGRLLARLHR--------------ALADFPRPNARDLAWWDELLERLLGPLLPDPE---DRALLEELLDRLEARLAPLLG 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501626018 188 --RPSLLHGDLWNGNV---ANSAFGPI-----CYDPACY--------WGDHECDLALTElfegfskEFYEGYQSVNPLD 248
Cdd:COG2334  176 alPRGVIHGDLHPDNVlfdGDGVSGLIdfddaGYGPRLYdlaialngWADGPLDPARLA-------ALLEGYRAVRPLT 247
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
28-247 7.25e-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: 43.40  E-value: 7.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  28 GDINDCYMISDG--NERYFVKVNQREF-------LPKFEIEAENLRLLRETSTVYVP----------ELVLIGKTKECsf 88
Cdd:cd05153   14 GELLSFEGIAAGieNTNYFVTTTDGRYvltlfekRRSAAELPFELELLDHLAQAGLPvprpladkdgELLGELNGKPA-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018  89 IILNYLPTKPLETSN--NSYDFGVQLAQLHQWGEQKEFGCDQDnyigstLQPNPWHKKWGRF--FSEQRIGFQLQLLKEK 164
Cdd:cd05153   92 ALFPFLPGESLTTPTpeQCRAIGAALARLHLALAGFPPPRPNP------RGLAWWKPLAERLkaRLDLLAADDRALLEDE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501626018 165 giefgdIDDIvdvvnMRLAGHNPRPSLLHGDLWNGNV---ANSAFGPICYDPACYwGDHECDLALT----------ELFE 231
Cdd:cd05153  166 ------LARL-----QALAPSDLPRGVIHADLFRDNVlfdGDRLSGIIDFYDACY-DPLLYDLAIAlndwcfdddgKLDP 233
                        250
                 ....*....|....*.
gi 501626018 232 GFSKEFYEGYQSVNPL 247
Cdd:cd05153  234 ERAKALLAGYQSVRPL 249
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
24-101 5.09e-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: 39.59  E-value: 5.09e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501626018  24 KVSGGDINDCYMISDgNERYFVKVNQREFLPKFEIEAENLRLLRETSTVYVPELVLIGKTKECSFIILNYLPTKPLET 101
Cdd:cd05120    5 LIKEGGDNKVYLLGD-PREYVLKIGPPRLKKDLEKEAAMLQLLAGKLSLPVPKVYGFGESDGWEYLLMERIEGETLSE 81
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH