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Conserved domains on  [gi|1372384683|gb|PSU49405|]
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hypothetical protein C9J12_07895 [Photobacterium frigidiphilum]

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 ...
1-284 0e+00

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: 509.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683   1 MWQAISHQLSDILGKPFKISEREALEGGDVNQCYCVGDGDERFFIKINDKEQLAMFKSEAESLRILNEANCVQVPQLLHL 80
Cdd:pfam03881   1 MWQAIAQQLSEQTGKPFEITEREPVGGGDINQAYRLSDGEQRYFVKLNQREQLAMFEAEAEGLEALAETQTIRVPKVIAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  81 GTCREKSFLILNYLPTKTVDSDSAFKLGQQLAELHQWGEQAEYGFDFDNYVGITPQPNKWRRRWCRFFAEQRIAWQLQLC 160
Cdd:pfam03881  81 GSSRDHSFLVLEYLELGPDNRGSAYELGQQLAKLHRWSGQKQFGFDFDNTIGSTPQPNTWQSSWADFFAEQRIGWQLQLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 161 EEKGIQFGNIDTITGNVISLLMHHQPTPSLLHGDLWHGNTALTVTG-PIIFDPATYWGDRECDIAMTELFGGFPASFYEG 239
Cdd:pfam03881 161 KEKGGNFGNIDRLVERVADLLAGHQPQPSLLHGDLWSGNAAFTADGePVIFDPACYYGDRECDLAMTELFGGFPPSFYEG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1372384683 240 YQSIFPLDDGYQERRDLYNLYHILNHCNLFGGEYLAQAEHIIEKL 284
Cdd:pfam03881 241 YQSVWPLDEGYEDRKPLYQLYHLLNHLNLFGGGYLSQAQQLIDKL 285
 
Name Accession Description Interval E-value
Fructosamin_kin pfam03881
Fructosamine kinase; This family includes eukaryotic fructosamine-3-kinase enzymes. The family ...
1-284 0e+00

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: 509.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683   1 MWQAISHQLSDILGKPFKISEREALEGGDVNQCYCVGDGDERFFIKINDKEQLAMFKSEAESLRILNEANCVQVPQLLHL 80
Cdd:pfam03881   1 MWQAIAQQLSEQTGKPFEITEREPVGGGDINQAYRLSDGEQRYFVKLNQREQLAMFEAEAEGLEALAETQTIRVPKVIAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  81 GTCREKSFLILNYLPTKTVDSDSAFKLGQQLAELHQWGEQAEYGFDFDNYVGITPQPNKWRRRWCRFFAEQRIAWQLQLC 160
Cdd:pfam03881  81 GSSRDHSFLVLEYLELGPDNRGSAYELGQQLAKLHRWSGQKQFGFDFDNTIGSTPQPNTWQSSWADFFAEQRIGWQLQLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 161 EEKGIQFGNIDTITGNVISLLMHHQPTPSLLHGDLWHGNTALTVTG-PIIFDPATYWGDRECDIAMTELFGGFPASFYEG 239
Cdd:pfam03881 161 KEKGGNFGNIDRLVERVADLLAGHQPQPSLLHGDLWSGNAAFTADGePVIFDPACYYGDRECDLAMTELFGGFPPSFYEG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1372384683 240 YQSIFPLDDGYQERRDLYNLYHILNHCNLFGGEYLAQAEHIIEKL 284
Cdd:pfam03881 241 YQSVWPLDEGYEDRKPLYQLYHLLNHLNLFGGGYLSQAQQLIDKL 285
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
3-284 8.31e-155

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


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 433.47  E-value: 8.31e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683   3 QAISHQLSDILGKPFKISEREALEGGDVNQCYCVGDGDERFFIKINDKEQLAMFKSEAESLRILNEANCVQVPQLLHLGT 82
Cdd:COG3001     1 QAIAEALSEALGPPFEITSVRPVSGGDINQAYRVTTDGRRVFVKLNPASPLGMFEAEAAGLRALAATGTIRVPEVIGVGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  83 CREKSFLILNYLPTKTVDSDSAFKLGQQLAELHQWGeQAEYGFDFDNYVGITPQPNKWRRRWCRFFAEQRIAWQLQLCEE 162
Cdd:COG3001    81 TGDHAFLVLEYLELGPPTAGAWERLGRQLAALHQAT-APRFGWDRDNFIGSTPQPNTWTDDWAEFFAEQRLGPQLQLAAE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 163 KGIQFG----NIDTITGNVISLLMHHQPTPSLLHGDLWHGNTALTVTG-PIIFDPATYWGDRECDIAMTELFGGFPASFY 237
Cdd:COG3001   160 KGLLFAadreRIERLVERLPELLAPHEPQPSLLHGDLWSGNVLFTADGePVLIDPAVYYGDREVDLAMTELFGGFPDAFY 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1372384683 238 EGYQSIFPLDDGYQERRDLYNLYHILNHCNLFGGEYLAQAEHIIEKL 284
Cdd:COG3001   240 DAYQEVWPLDPGYEERKPLYQLYHLLNHLNLFGGSYLSQAERILDRL 286
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
6-248 8.14e-06

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: 46.48  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683   6 SHQLSDILgKPFKISEREALEG---GDVNQCYCVGDGDERFFIKINdkEQLAMFKSEAESLRILNE--ANCVQVPQLL-- 78
Cdd:cd05153     1 DEELAEFL-AHYDLGELLSFEGiaaGIENTNYFVTTTDGRYVLTLF--EKRRSAAELPFELELLDHlaQAGLPVPRPLad 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  79 ----HLGTCREKSFLILNYLPTKTVDSDSA---FKLGQQLAELHQWGEqaeyGFDFdnyvgitPQPNKWRRRWCRFFAEQ 151
Cdd:cd05153    78 kdgeLLGELNGKPAALFPFLPGESLTTPTPeqcRAIGAALARLHLALA----GFPP-------PRPNPRGLAWWKPLAER 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 152 riAWQLQLCEEKGIQfgniDTITgNVISLLMHHQPTP---SLLHGDLWHGNT---ALTVTGPIIFDPAtYWGDRECDIAM 225
Cdd:cd05153   147 --LKARLDLLAADDR----ALLE-DELARLQALAPSDlprGVIHADLFRDNVlfdGDRLSGIIDFYDA-CYDPLLYDLAI 218
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1372384683 226 TELFGGFPASFY----------EGYQSIFPLDD 248
Cdd:cd05153   219 ALNDWCFDDDGKldperakallAGYQSVRPLTE 251
 
Name Accession Description Interval E-value
Fructosamin_kin pfam03881
Fructosamine kinase; This family includes eukaryotic fructosamine-3-kinase enzymes. The family ...
1-284 0e+00

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: 509.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683   1 MWQAISHQLSDILGKPFKISEREALEGGDVNQCYCVGDGDERFFIKINDKEQLAMFKSEAESLRILNEANCVQVPQLLHL 80
Cdd:pfam03881   1 MWQAIAQQLSEQTGKPFEITEREPVGGGDINQAYRLSDGEQRYFVKLNQREQLAMFEAEAEGLEALAETQTIRVPKVIAW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  81 GTCREKSFLILNYLPTKTVDSDSAFKLGQQLAELHQWGEQAEYGFDFDNYVGITPQPNKWRRRWCRFFAEQRIAWQLQLC 160
Cdd:pfam03881  81 GSSRDHSFLVLEYLELGPDNRGSAYELGQQLAKLHRWSGQKQFGFDFDNTIGSTPQPNTWQSSWADFFAEQRIGWQLQLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 161 EEKGIQFGNIDTITGNVISLLMHHQPTPSLLHGDLWHGNTALTVTG-PIIFDPATYWGDRECDIAMTELFGGFPASFYEG 239
Cdd:pfam03881 161 KEKGGNFGNIDRLVERVADLLAGHQPQPSLLHGDLWSGNAAFTADGePVIFDPACYYGDRECDLAMTELFGGFPPSFYEG 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1372384683 240 YQSIFPLDDGYQERRDLYNLYHILNHCNLFGGEYLAQAEHIIEKL 284
Cdd:pfam03881 241 YQSVWPLDEGYEDRKPLYQLYHLLNHLNLFGGGYLSQAQQLIDKL 285
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
3-284 8.31e-155

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


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 433.47  E-value: 8.31e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683   3 QAISHQLSDILGKPFKISEREALEGGDVNQCYCVGDGDERFFIKINDKEQLAMFKSEAESLRILNEANCVQVPQLLHLGT 82
Cdd:COG3001     1 QAIAEALSEALGPPFEITSVRPVSGGDINQAYRVTTDGRRVFVKLNPASPLGMFEAEAAGLRALAATGTIRVPEVIGVGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  83 CREKSFLILNYLPTKTVDSDSAFKLGQQLAELHQWGeQAEYGFDFDNYVGITPQPNKWRRRWCRFFAEQRIAWQLQLCEE 162
Cdd:COG3001    81 TGDHAFLVLEYLELGPPTAGAWERLGRQLAALHQAT-APRFGWDRDNFIGSTPQPNTWTDDWAEFFAEQRLGPQLQLAAE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 163 KGIQFG----NIDTITGNVISLLMHHQPTPSLLHGDLWHGNTALTVTG-PIIFDPATYWGDRECDIAMTELFGGFPASFY 237
Cdd:COG3001   160 KGLLFAadreRIERLVERLPELLAPHEPQPSLLHGDLWSGNVLFTADGePVLIDPAVYYGDREVDLAMTELFGGFPDAFY 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1372384683 238 EGYQSIFPLDDGYQERRDLYNLYHILNHCNLFGGEYLAQAEHIIEKL 284
Cdd:COG3001   240 DAYQEVWPLDPGYEERKPLYQLYHLLNHLNLFGGSYLSQAERILDRL 286
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
23-256 3.44e-15

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: 73.30  E-value: 3.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  23 EALEGGDVNQCYCVGDGDERFFIKINDKEQLAM-FKSEAESLRILNEANCVQVPQLLHLGTCREKS---FLILNYLPTKT 98
Cdd:pfam01636   3 RPISSGASNRTYLVTTGDGRYVLRLPPPGRAAEeLRRELALLRHLAAAGVPPVPRVLAGCTDAELLglpFLLMEYLPGEV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  99 VDSDS--------AFKLGQQLAELHQwgeqaeygfdfdnyVGITPQPNKWRRRWCRFFAEQRIAWQLQLCEEKGIQFgnI 170
Cdd:pfam01636  83 LARPLlpeergalLEALGRALARLHA--------------VDPAALPLAGRLARLLELLRQLEAALARLLAAELLDR--L 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 171 DTITGNVISLLMHHQPT---PSLLHGDLWHGNTALTVTGPII----FDPATyWGDRECDIAMT--ELFGGFPASFYEGYQ 241
Cdd:pfam01636 147 EELEERLLAALLALLPAelpPVLVHGDLHPGNLLVDPGGRVSgvidFEDAG-LGDPAYDLAILlnSWGRELGAELLAAYL 225
                         250
                  ....*....|....*
gi 1372384683 242 sIFPLDDGYQERRDL 256
Cdd:pfam01636 226 -AAYGAFGYARLREL 239
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
3-254 1.09e-13

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 69.76  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683   3 QAISHQLSDILGKPfkisEREALEGGDVNQCYCVGDGDeRFFIKIN---DKEQLAMFKsEAESLRILNEANCVQVPQLLH 79
Cdd:COG3173    10 ALLAAQLPGLAGLP----EVEPLSGGWSNLTYRLDTGD-RLVLRRPprgLASAHDVRR-EARVLRALAPRLGVPVPRPLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  80 LGTCRE---KSFLILNYLP----TKTVDSDS-------AFKLGQQLAELHQWgEQAEYGFDFDNYVGITPQPNKWRRRWC 145
Cdd:COG3173    84 LGEDGEvigAPFYVMEWVEgetlEDALPDLSpaerralARALGEFLAALHAV-DPAAAGLADGRPEGLERQLARWRAQLR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 146 RFFAEQRiawqlqlceekgiqfgNIDTITGNVISLLMHHQP---TPSLLHGDLWHGNTALTVTGP----II-FDPATyWG 217
Cdd:COG3173   163 RALARTD----------------DLPALRERLAAWLAANLPewgPPVLVHGDLRPGNLLVDPDDGrltaVIdWELAT-LG 225
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1372384683 218 DRECDIAMTELFGGFPASFYEGYQSIFpldDGYQERR 254
Cdd:COG3173   226 DPAADLAYLLLYWRLPDDLLGPRAAFL---AAYEEAT 259
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
8-248 3.06e-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: 50.69  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683   8 QLSDILgKPFKISEREALEG--GDVNQCYCVGDGD-ERFFIKIN-----DKEQLAMFkseaesLRILNE--ANCVQVPQL 77
Cdd:COG2334     2 ELAAAL-ERYGLGPLSSLKPlnSGENRNYRVETEDgRRYVLKLYrpgrwSPEEIPFE------LALLAHlaAAGLPVPAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  78 LH------LGTCREKSFLILNYLPTKTVDSDSA---FKLGQQLAELHQWGEqaeygfDFdnyvgitPQPN----KWRRRW 144
Cdd:COG2334    75 VPtrdgetLLELEGRPAALFPFLPGRSPEEPSPeqlEELGRLLARLHRALA------DF-------PRPNardlAWWDEL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 145 CRFFAEQRI--AWQLQLCEEKgiqfgnIDTITGNVISLLmHHQPTpSLLHGDLWHGN--------TAL-----TVTGPII 209
Cdd:COG2334   142 LERLLGPLLpdPEDRALLEEL------LDRLEARLAPLL-GALPR-GVIHGDLHPDNvlfdgdgvSGLidfddAGYGPRL 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1372384683 210 FDPAT---YWGDRECDIAMTelfggfpASFYEGYQSIFPLDD 248
Cdd:COG2334   214 YDLAIalnGWADGPLDPARL-------AALLEGYRAVRPLTE 248
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
6-248 8.14e-06

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: 46.48  E-value: 8.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683   6 SHQLSDILgKPFKISEREALEG---GDVNQCYCVGDGDERFFIKINdkEQLAMFKSEAESLRILNE--ANCVQVPQLL-- 78
Cdd:cd05153     1 DEELAEFL-AHYDLGELLSFEGiaaGIENTNYFVTTTDGRYVLTLF--EKRRSAAELPFELELLDHlaQAGLPVPRPLad 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  79 ----HLGTCREKSFLILNYLPTKTVDSDSA---FKLGQQLAELHQWGEqaeyGFDFdnyvgitPQPNKWRRRWCRFFAEQ 151
Cdd:cd05153    78 kdgeLLGELNGKPAALFPFLPGESLTTPTPeqcRAIGAALARLHLALA----GFPP-------PRPNPRGLAWWKPLAER 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 152 riAWQLQLCEEKGIQfgniDTITgNVISLLMHHQPTP---SLLHGDLWHGNT---ALTVTGPIIFDPAtYWGDRECDIAM 225
Cdd:cd05153   147 --LKARLDLLAADDR----ALLE-DELARLQALAPSDlprGVIHADLFRDNVlfdGDRLSGIIDFYDA-CYDPLLYDLAI 218
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1372384683 226 TELFGGFPASFY----------EGYQSIFPLDD 248
Cdd:cd05153   219 ALNDWCFDDDGKldperakallAGYQSVRPLTE 251
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
20-116 2.14e-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: 43.83  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  20 SEREALEGGDVNQCYCVGDgDERFFIKINDKEQLAMFKSEAESLRILNEANCVQVPQLLHLGTCREKSFLILNYLPTKTV 99
Cdd:cd05120     1 ISVKLIKEGGDNKVYLLGD-PREYVLKIGPPRLKKDLEKEAAMLQLLAGKLSLPVPKVYGFGESDGWEYLLMERIEGETL 79
                          90       100
                  ....*....|....*....|....*...
gi 1372384683 100 DSDS-----------AFKLGQQLAELHQ 116
Cdd:cd05120    80 SEVWprlseeekekiADQLAEILAALHR 107
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
59-260 8.25e-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: 42.99  E-value: 8.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  59 EAESLRILNEANcVQVPQLLHLgtCREKS-----FLILNYLPTKTVDSDS-------------AFKLGQQLAELHQWgEQ 120
Cdd:cd05154    48 EYRVLRALAGTG-VPVPRVLAL--CEDPSvlgapFYVMERVDGRVLPDPLprpdlspeerralARSLVDALAALHSV-DP 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683 121 AEYGFDF----DNYVGItpQPNKWRRRWcrffaEQRIAWQLQLCEEkgiqfgnidtitgnVISLLMHHQPT---PSLLHG 193
Cdd:cd05154   124 AALGLADlgrpEGYLER--QVDRWRRQL-----EAAATDPPPALEE--------------ALRWLRANLPAdgrPVLVHG 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1372384683 194 DLWHGNtaltvtgpIIFDPA-----------TYWGDRECDIAMTELFGGFPaSFYEGYQSIFPLdDGYQERRDLYNLY 260
Cdd:cd05154   183 DFRLGN--------LLFDPDgrvtavldwelATLGDPLEDLAWLLARWWRP-GDPPGLAAPTRL-PGFPSREELLARY 250
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
23-116 1.28e-03

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 38.30  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372384683  23 EALEGGDVNQCYCVGDGDERFFIKI--NDKEQLAMFKSEAESLRILNEANcvqV-PQLLHLgtcREKS-FLILNYLPTKT 98
Cdd:cd05151     4 EPLKGGLTNKNYLVEVAGKKYVLRIpgAGTELLIDRENEKANSKAAAELG---IaPEVIYF---DPETgVKITEFIEGAT 77
                          90       100
                  ....*....|....*....|....
gi 1372384683  99 V------DSDSAFKLGQQLAELHQ 116
Cdd:cd05151    78 LltndfsDPENLERIAALLRKLHS 101
 
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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