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Conserved domains on  [gi|2787114717|ref|WP_370264006|]
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phosphotransferase family protein [Limnobacter sp.]

Protein Classification

phosphotransferase family protein( domain architecture ID 10142358)

phosphotransferase family protein may catalyze the phosphorylation of aminoglycosides and confer aminoglycoside antibiotic resistance

CATH:  1.10.510.10
EC:  2.7.1.-
Gene Ontology:  GO:0016301|GO:0016310|GO:0005524
PubMed:  16244704

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
26-276 2.71e-73

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: 227.11  E-value: 2.71e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  26 QLVPLSGGAIQENWRLVLEVDGGPHHgtvlCVLRCDSATAGVASSHSRAQEFALLATAFNAGVRVPEPLLLCTDPQVLGR 105
Cdd:cd05154     2 AVRRLSGGASNETYLVDAGGDGGGRR----LVLRRPPPGGLLPSAHDLEREYRVLRALAGTGVPVPRVLALCEDPSVLGA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 106 PFFLMKCVPGTAAAHVIVKDMRYAPDRAELAHALGRELATIHSIVPPVPALNFLPLPEGnPALLKVQQHRAYLDTLPNAY 185
Cdd:cd05154    78 PFYVMERVDGRVLPDPLPRPDLSPEERRALARSLVDALAALHSVDPAALGLADLGRPEG-YLERQVDRWRRQLEAAATDP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 186 -PALEWGLRWLERHAPRNLQLALCHGDYRTGNYMVDEHG-LSGILDWEFAQWGNPLQDLGWFCARCWRFGQHE-----LE 258
Cdd:cd05154   157 pPALEEALRWLRANLPADGRPVLVHGDFRLGNLLFDPDGrVTAVLDWELATLGDPLEDLAWLLARWWRPGDPPglaapTR 236
                         250
                  ....*....|....*...
gi 2787114717 259 AGGIGLREHFYAGYEEVS 276
Cdd:cd05154   237 LPGFPSREELLARYEEAS 254
 
Name Accession Description Interval E-value
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
26-276 2.71e-73

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: 227.11  E-value: 2.71e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  26 QLVPLSGGAIQENWRLVLEVDGGPHHgtvlCVLRCDSATAGVASSHSRAQEFALLATAFNAGVRVPEPLLLCTDPQVLGR 105
Cdd:cd05154     2 AVRRLSGGASNETYLVDAGGDGGGRR----LVLRRPPPGGLLPSAHDLEREYRVLRALAGTGVPVPRVLALCEDPSVLGA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 106 PFFLMKCVPGTAAAHVIVKDMRYAPDRAELAHALGRELATIHSIVPPVPALNFLPLPEGnPALLKVQQHRAYLDTLPNAY 185
Cdd:cd05154    78 PFYVMERVDGRVLPDPLPRPDLSPEERRALARSLVDALAALHSVDPAALGLADLGRPEG-YLERQVDRWRRQLEAAATDP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 186 -PALEWGLRWLERHAPRNLQLALCHGDYRTGNYMVDEHG-LSGILDWEFAQWGNPLQDLGWFCARCWRFGQHE-----LE 258
Cdd:cd05154   157 pPALEEALRWLRANLPADGRPVLVHGDFRLGNLLFDPDGrVTAVLDWELATLGDPLEDLAWLLARWWRPGDPPglaapTR 236
                         250
                  ....*....|....*...
gi 2787114717 259 AGGIGLREHFYAGYEEVS 276
Cdd:cd05154   237 LPGFPSREELLARYEEAS 254
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
6-289 7.40e-46

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 157.58  E-value: 7.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717   6 QQALARHIAAQWnARRVRIEQLVPLSGGAIQENWRLVLEVDggphhgtvlCVLRCDSAtaGVASSHSRAQEFALLAT-AF 84
Cdd:COG3173     5 EAALRALLAAQL-PGLAGLPEVEPLSGGWSNLTYRLDTGDR---------LVLRRPPR--GLASAHDVRREARVLRAlAP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  85 NAGVRVPEPLLLCTDPQVLGRPFFLMKCVPGTAAAHVIVKDmrYAPDRAELAHALGRELATIHSIVPPVPALNFLPlPEG 164
Cdd:COG3173    73 RLGVPVPRPLALGEDGEVIGAPFYVMEWVEGETLEDALPDL--SPAERRALARALGEFLAALHAVDPAAAGLADGR-PEG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 165 NPALLKV--QQHRAYLDTLPNAYPALEWGLRWLERHAPRNLQLALCHGDYRTGNYMVDEHG--LSGILDWEFAQWGNPLQ 240
Cdd:COG3173   150 LERQLARwrAQLRRALARTDDLPALRERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDPDDgrLTAVIDWELATLGDPAA 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2787114717 241 DLGWFCArCWRFGQHELeaggiGLREHFYAGYEEVSPTPidrAEVAYWE 289
Cdd:COG3173   230 DLAYLLL-YWRLPDDLL-----GPRAAFLAAYEEATGDL---DDLTWWA 269
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
27-277 3.89e-27

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: 106.82  E-value: 3.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  27 LVPLSGGAIQENWRLVLEvdggphHGTVlcVLRCDSATAGVASSHSRAQEFALLATAfnAGVRVPEPLLLCTDPQVLGRP 106
Cdd:pfam01636   2 LRPISSGASNRTYLVTTG------DGRY--VLRLPPPGRAAEELRRELALLRHLAAA--GVPPVPRVLAGCTDAELLGLP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 107 FFLMKCVPGTAAAHVIVKDMRYapdraELAHALGRELATIHSIVPPVPALNFLPLPEGNPALLKVQQHRAYLD--TLPNA 184
Cdd:pfam01636  72 FLLMEYLPGEVLARPLLPEERG-----ALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAaeLLDRL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 185 YPALEWGLRWLERHAPRNLQLALCHGDYRTGNYMVDEHG-LSGILDWEFAQWGNPLQDLGWFCARcWRFGQHELEAGGIg 263
Cdd:pfam01636 147 EELEERLLAALLALLPAELPPVLVHGDLHPGNLLVDPGGrVSGVIDFEDAGLGDPAYDLAILLNS-WGRELGAELLAAY- 224
                         250
                  ....*....|....
gi 2787114717 264 LREHFYAGYEEVSP 277
Cdd:pfam01636 225 LAAYGAFGYARLRE 238
PLN02876 PLN02876
acyl-CoA dehydrogenase
57-246 7.55e-10

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 60.19  E-value: 7.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  57 VLRCDSATAGVASSHSRAQEFALL-ATAFNAGVRVPEPLLLCTDPQVLGRPFFLMKCVPGTAAAHVIVKDMryAPD-RAE 134
Cdd:PLN02876   69 VLRKKPPGKLLQSAHAVEREYQVLrALGEHTDVPVPKVYCLCTDASVIGTAFYIMEYLEGRIFVDPKLPGV--APErRRA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 135 LAHALGRELATIHSIvpPVPALNFLPL-PEGNPALLKVQQ-HRAYL----DTLPNAYPALEWGLRWLERHAP----RNLQ 204
Cdd:PLN02876  147 IYRATAKVLAALHSA--DVDAIGLGKYgRRDNYCKRQVERwAKQYLastgEGKPPRNPKMLELIDWLRENIPaedsTGAG 224
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2787114717 205 LALCHGDYRTGNYMVD--EHGLSGILDWEFAQWGNPLQDLGWFC 246
Cdd:PLN02876  225 TGIVHGDFRIDNLVFHptEDRVIGILDWELSTLGNQMCDVAYSC 268
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
207-245 4.85e-04

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


Pssm-ID: 214734  Cd Length: 196  Bit Score: 40.78  E-value: 4.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2787114717  207 LCHGDYRTGNYMV--DEHG---LSGILDWEFAQWGNPLQDLGWF 245
Cdd:smart00587 122 LNHGDLWANNIMFkyDDEGkpeDVALIDFQLSHYGSPAEDLHYF 165
 
Name Accession Description Interval E-value
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
26-276 2.71e-73

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: 227.11  E-value: 2.71e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  26 QLVPLSGGAIQENWRLVLEVDGGPHHgtvlCVLRCDSATAGVASSHSRAQEFALLATAFNAGVRVPEPLLLCTDPQVLGR 105
Cdd:cd05154     2 AVRRLSGGASNETYLVDAGGDGGGRR----LVLRRPPPGGLLPSAHDLEREYRVLRALAGTGVPVPRVLALCEDPSVLGA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 106 PFFLMKCVPGTAAAHVIVKDMRYAPDRAELAHALGRELATIHSIVPPVPALNFLPLPEGnPALLKVQQHRAYLDTLPNAY 185
Cdd:cd05154    78 PFYVMERVDGRVLPDPLPRPDLSPEERRALARSLVDALAALHSVDPAALGLADLGRPEG-YLERQVDRWRRQLEAAATDP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 186 -PALEWGLRWLERHAPRNLQLALCHGDYRTGNYMVDEHG-LSGILDWEFAQWGNPLQDLGWFCARCWRFGQHE-----LE 258
Cdd:cd05154   157 pPALEEALRWLRANLPADGRPVLVHGDFRLGNLLFDPDGrVTAVLDWELATLGDPLEDLAWLLARWWRPGDPPglaapTR 236
                         250
                  ....*....|....*...
gi 2787114717 259 AGGIGLREHFYAGYEEVS 276
Cdd:cd05154   237 LPGFPSREELLARYEEAS 254
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
6-289 7.40e-46

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 157.58  E-value: 7.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717   6 QQALARHIAAQWnARRVRIEQLVPLSGGAIQENWRLVLEVDggphhgtvlCVLRCDSAtaGVASSHSRAQEFALLAT-AF 84
Cdd:COG3173     5 EAALRALLAAQL-PGLAGLPEVEPLSGGWSNLTYRLDTGDR---------LVLRRPPR--GLASAHDVRREARVLRAlAP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  85 NAGVRVPEPLLLCTDPQVLGRPFFLMKCVPGTAAAHVIVKDmrYAPDRAELAHALGRELATIHSIVPPVPALNFLPlPEG 164
Cdd:COG3173    73 RLGVPVPRPLALGEDGEVIGAPFYVMEWVEGETLEDALPDL--SPAERRALARALGEFLAALHAVDPAAAGLADGR-PEG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 165 NPALLKV--QQHRAYLDTLPNAYPALEWGLRWLERHAPRNLQLALCHGDYRTGNYMVDEHG--LSGILDWEFAQWGNPLQ 240
Cdd:COG3173   150 LERQLARwrAQLRRALARTDDLPALRERLAAWLAANLPEWGPPVLVHGDLRPGNLLVDPDDgrLTAVIDWELATLGDPAA 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2787114717 241 DLGWFCArCWRFGQHELeaggiGLREHFYAGYEEVSPTPidrAEVAYWE 289
Cdd:COG3173   230 DLAYLLL-YWRLPDDLL-----GPRAAFLAAYEEATGDL---DDLTWWA 269
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
27-277 3.89e-27

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: 106.82  E-value: 3.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  27 LVPLSGGAIQENWRLVLEvdggphHGTVlcVLRCDSATAGVASSHSRAQEFALLATAfnAGVRVPEPLLLCTDPQVLGRP 106
Cdd:pfam01636   2 LRPISSGASNRTYLVTTG------DGRY--VLRLPPPGRAAEELRRELALLRHLAAA--GVPPVPRVLAGCTDAELLGLP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 107 FFLMKCVPGTAAAHVIVKDMRYapdraELAHALGRELATIHSIVPPVPALNFLPLPEGNPALLKVQQHRAYLD--TLPNA 184
Cdd:pfam01636  72 FLLMEYLPGEVLARPLLPEERG-----ALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAaeLLDRL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 185 YPALEWGLRWLERHAPRNLQLALCHGDYRTGNYMVDEHG-LSGILDWEFAQWGNPLQDLGWFCARcWRFGQHELEAGGIg 263
Cdd:pfam01636 147 EELEERLLAALLALLPAELPPVLVHGDLHPGNLLVDPGGrVSGVIDFEDAGLGDPAYDLAILLNS-WGRELGAELLAAY- 224
                         250
                  ....*....|....
gi 2787114717 264 LREHFYAGYEEVSP 277
Cdd:pfam01636 225 LAAYGAFGYARLRE 238
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
8-292 1.06e-19

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: 87.67  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717   8 ALARHIAAQWNARRVRieQLVPLSGGaIQENWRLVLEvDGGPhhgtvlCVLRCdsATAGVASSHSRAQEFALLATAFNAG 87
Cdd:COG2334     1 DELAAALERYGLGPLS--SLKPLNSG-ENRNYRVETE-DGRR------YVLKL--YRPGRWSPEEIPFELALLAHLAAAG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  88 VRVPEPLLLcTDPQVL----GRPFFLMKCVPGTAaahvivkdmrYAPDRAELAHALGRELATIHSIVPPVPALNFLPLPE 163
Cdd:COG2334    69 LPVPAPVPT-RDGETLleleGRPAALFPFLPGRS----------PEEPSPEQLEELGRLLARLHRALADFPRPNARDLAW 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 164 GNPALLKVQQHRAyldTLPNAYPALEWGLRWLERHAPR---NLQLALCHGDYRTGNYMVDEHGLSGILDWEFAQWGNPLQ 240
Cdd:COG2334   138 WDELLERLLGPLL---PDPEDRALLEELLDRLEARLAPllgALPRGVIHGDLHPDNVLFDGDGVSGLIDFDDAGYGPRLY 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2787114717 241 DLgWFCARCWRFGQHELEaggigLREHFYAGYEEVSptPIDRAEVAYWEVMA 292
Cdd:COG2334   215 DL-AIALNGWADGPLDPA-----RLAALLEGYRAVR--PLTEAELAALPPLL 258
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
76-291 1.53e-15

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: 75.76  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  76 EFALLATAFNAGVRVPEPL------LLCTdpqVLGRPFFLMKCVPGTaaaHVivkdmryAPDRAELAHALGRELATIHSI 149
Cdd:cd05153    57 ELELLDHLAQAGLPVPRPLadkdgeLLGE---LNGKPAALFPFLPGE---SL-------TTPTPEQCRAIGAALARLHLA 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 150 V--PPVPALNFLPlPEGNPALLkvQQHRAYLDTLPNAYPA-LEWGLRWLERHAPRNLQLALCHGDYRTGNYMVDEHGLSG 226
Cdd:cd05153   124 LagFPPPRPNPRG-LAWWKPLA--ERLKARLDLLAADDRAlLEDELARLQALAPSDLPRGVIHADLFRDNVLFDGDRLSG 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2787114717 227 ILDWEFAQWGNPLQDLGWFCARcWRFG-QHELEaggIGLREHFYAGYEEVspTPIDRAEVAYWEVM 291
Cdd:cd05153   201 IIDFYDACYDPLLYDLAIALND-WCFDdDGKLD---PERAKALLAGYQSV--RPLTEEEKAALPLL 260
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
175-317 2.34e-13

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 66.73  E-value: 2.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 175 RAYLDTLPNAYPALEWGLRWLERH-APRNLQLALCHGDYRTGNYMVDEHGLSGILDWEFAQWGNPLQDLGwFCARCWRFG 253
Cdd:COG0510    18 ERYLALGPRDLPELLRRLEELERAlAARPLPLVLCHGDLHPGNFLVTDDGRLYLIDWEYAGLGDPAFDLA-ALLVEYGLS 96
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2787114717 254 QHEleaggiglREHFYAGYEEVSPTPIDRAEVAYWEVMAHVTWAVIALQQAQRHCSGQERSLLL 317
Cdd:COG0510    97 PEQ--------AEELLEAYGFGRPTEELLRRLRAYRALADLLWALWALVRAAQEANGDLLKYLL 152
PLN02876 PLN02876
acyl-CoA dehydrogenase
57-246 7.55e-10

acyl-CoA dehydrogenase


Pssm-ID: 215473 [Multi-domain]  Cd Length: 822  Bit Score: 60.19  E-value: 7.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  57 VLRCDSATAGVASSHSRAQEFALL-ATAFNAGVRVPEPLLLCTDPQVLGRPFFLMKCVPGTAAAHVIVKDMryAPD-RAE 134
Cdd:PLN02876   69 VLRKKPPGKLLQSAHAVEREYQVLrALGEHTDVPVPKVYCLCTDASVIGTAFYIMEYLEGRIFVDPKLPGV--APErRRA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 135 LAHALGRELATIHSIvpPVPALNFLPL-PEGNPALLKVQQ-HRAYL----DTLPNAYPALEWGLRWLERHAP----RNLQ 204
Cdd:PLN02876  147 IYRATAKVLAALHSA--DVDAIGLGKYgRRDNYCKRQVERwAKQYLastgEGKPPRNPKMLELIDWLRENIPaedsTGAG 224
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2787114717 205 LALCHGDYRTGNYMVD--EHGLSGILDWEFAQWGNPLQDLGWFC 246
Cdd:PLN02876  225 TGIVHGDFRIDNLVFHptEDRVIGILDWELSTLGNQMCDVAYSC 268
APH cd05150
Aminoglycoside 3'-phosphotransferase; APH catalyzes the transfer of the gamma-phosphoryl group ...
100-288 2.77e-09

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: 56.82  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 100 PQVL------GRPFFLMKCVPGTAAAhvivkDMRYAPDRAELAHALGRELATIHSIvPPVPAlnflPLPEGNPALLKVQQ 173
Cdd:cd05150    55 PEVLdygsddGGDWLLTTALPGRDAA-----SLEPLLDPERLVDLLAEALRALHSL-PIADC----PFDRRLDARLAEAR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 174 HR--AYLDTLPNAYPAlEWG------LRWLERHAPRNLQLALCHGDYRTGNYMVDEHGLSGILDWEFAQWGNPLQDLGWf 245
Cdd:cd05150   125 ARveAGLVDEDDFDEE-RQGrtaeelLAELEATRPAEEDLVVTHGDACLPNIILDPGRFSGFIDLGRLGVADRYQDLAL- 202
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2787114717 246 CARCWRFgqhelEAGGIGLREHFYAGYEEVSPtpiDRAEVAYW 288
Cdd:cd05150   203 AVRSLRE-----NLGGEEYAERFLDAYGIDAP---DPERLAYY 237
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
205-250 1.46e-08

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: 53.08  E-value: 1.46e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2787114717 205 LALCHGDYRTGNYMVDEHG-LSGILDWEFAQWGNPLQDLGWFCARCW 250
Cdd:cd05120   111 SVLTHGDLHPGNILVKPDGkLSGIIDWEFAGYGPPAFDYAAALRDWT 157
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
75-278 2.49e-08

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: 52.65  E-value: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  75 QEFALLATAFNAGVRVPEPLLLCtdpqvLGRPFFLMKCVPGTAAAHVIVKdmryAPDRAELAHALGRELATIHSivppvp 154
Cdd:COG3642     5 REARLLRELREAGVPVPKVLDVD-----PDDADLVMEYIEGETLADLLEE----GELPPELLRELGRLLARLHR------ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 155 alnflplpegnpallkvqqhrayldtlpnaypalewglrwlerhaprnlqLALCHGDYRTGNYMVDEHGLsGILDWEFAQ 234
Cdd:COG3642    70 --------------------------------------------------AGIVHGDLTTSNILVDDGGV-YLIDFGLAR 98
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2787114717 235 WGNPLQDLGWFCARCWRFGQHELEAGGIGLREHFYAGYEEVSPT 278
Cdd:COG3642    99 YSDPLEDKAVDLAVLKRSLESTHPDPAEELWEAFLEGYREVGPA 142
YsxE COG5897
Spore coat protein YsxE, aminoglycoside phosphotransferase family [Cell cycle control, cell ...
187-277 1.35e-05

Spore coat protein YsxE, aminoglycoside phosphotransferase family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444599  Cd Length: 335  Bit Score: 46.14  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 187 ALEWGLRWLERH-APRNLQLALCHGDYRTGNYMVDEHGLSGILDWEFAQWGNPLQDLGWFCARCWRFGqhelEAGGIGLR 265
Cdd:COG5897   183 ADERLERWYEDEkEKKKWRIVLCHGRLSPSHVLFDESGQGYLINFERAGFDTPVRDLALFFRRAFRTA----PTNEEELV 258
                          90
                  ....*....|..
gi 2787114717 266 EHFYAgYEEVSP 277
Cdd:COG5897   259 EWFSA-YEKELP 269
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
204-246 5.17e-05

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: 42.93  E-value: 5.17e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2787114717 204 QLALCHGDYRTGNYMVDEHGLsGILDWEFAQWGNPLQDLGWFC 246
Cdd:cd05151   106 DLVLCHNDLVPGNFLLDDDRL-YLIDWEYAGMNDPLFDLAALF 147
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
117-302 1.94e-04

Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group from ATP to the 2'-hydroxyl of macrolide antibiotics such as erythromycin, clarithromycin, and azithromycin, among others. Macrolides penetrate the bacterial cell and bind to ribosomes, where it interrupts protein elongation, leading ultimately to the demise of the bacterium. Phosphorylation of macrolides leads to their inactivation. Based on substrate specificity and amino acid sequence, MPH2' is divided into types I and II, encoded by mphA and mphB genes, respectively. MPH2'I inactivates 14-membered ring macrolides while MPH2'II inactivates both 14- and 16-membered ring macrolides. Enzymatic inactivation of macrolides has been reported as a mechanism for bacterial resistance in clinical samples. MPH2' is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270701 [Multi-domain]  Cd Length: 276  Bit Score: 42.62  E-value: 1.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 117 AAAHVIVKDMRYAPDRAELAHALGRELATIHSIvpPVPALNFLPLPEGNPALLKvQQHRAYLDTLPNAY---PALE--WG 191
Cdd:cd05152    96 PEIQNYVWNWDPLAPPPVFARSLGKALAALHSI--PADLAAAAGLPVYTAEEVR-ARMAARMDRVKETFgvpPALLarWQ 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 192 lRWLERHA--PRnlQLALCHGDYRTGNYMVDEHG-LSGILDWEFAQWGNPLQDLGWFcARCwrFGQHELEAggigLREHF 268
Cdd:cd05152   173 -AWLADDSlwPF--HTVLVHGDLHPGHILVDEDGrVTGLIDWTEAKVGDPADDFAWH-YAA--FGEEALER----LLDAY 242
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2787114717 269 YAGYEEVSPT-PIDRAEV--AYWevmahVTWAVIALQ 302
Cdd:cd05152   243 EKAGGEVWPRmLEHIIELaaAYP-----LTIALFALD 274
FN3K COG3001
Fructosamine-3-kinase [Carbohydrate transport and metabolism];
7-277 2.39e-04

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


Pssm-ID: 442239 [Multi-domain]  Cd Length: 287  Bit Score: 42.11  E-value: 2.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717   7 QALARHIAAQWNARrVRIEQLVPLSGGAIQENWRLvlEVDGGPhhgtvlCVLRCDSAtAGVASSHSRAQEFALLATAfnA 86
Cdd:COG3001     1 QAIAEALSEALGPP-FEITSVRPVSGGDINQAYRV--TTDGRR------VFVKLNPA-SPLGMFEAEAAGLRALAAT--G 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717  87 GVRVPEPLLLCTDPqvlGRPFFLMKCVPGtaaahvivkdmryAPDRAELAHALGRELATIHSIVPPV---PALNFL-PLP 162
Cdd:COG3001    69 TIRVPEVIGVGTTG---DHAFLVLEYLEL-------------GPPTAGAWERLGRQLAALHQATAPRfgwDRDNFIgSTP 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 163 EGNP---------------ALLKVQQHRAYLDTLPNA-----YPALEwglRWLERHAPRNlqlALCHGDYRTGNYMVDEH 222
Cdd:COG3001   133 QPNTwtddwaeffaeqrlgPQLQLAAEKGLLFAADRErierlVERLP---ELLAPHEPQP---SLLHGDLWSGNVLFTAD 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2787114717 223 GLSGILDwEFAQWGNPLQDLGWfcarCWRFGqheleaggiGLREHFYAGYEEVSP 277
Cdd:COG3001   207 GEPVLID-PAVYYGDREVDLAM----TELFG---------GFPDAFYDAYQEVWP 247
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
113-230 2.46e-04

Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). These proteins catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates, such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides, and macrolides leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270704 [Multi-domain]  Cd Length: 234  Bit Score: 41.84  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2787114717 113 VPGTAAAHVIVkdmryaPDRAELAHALGRELATIHSIVPPVPALNFL--PLPEGNPALLKVQQHRAYLDTLPNAYPALEw 190
Cdd:cd05155    76 LEGETAADAPL------ADPAAAAEDLARFLAALHAIDPAGPPNPGRgnPLRGRDLAVRDAEEALAALAGLLDVAAARA- 148
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2787114717 191 glRWLERHA--PRNLQLALCHGDYRTGNYMVDEHGLSGILDW 230
Cdd:cd05155   149 --LWERALAapAWAGPPVWLHGDLHPGNLLVRDGRLSAVIDF 188
CHK smart00587
ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases
207-245 4.85e-04

ZnF_C4 abd HLH domain containing kinases domain; subfamily of choline kinases


Pssm-ID: 214734  Cd Length: 196  Bit Score: 40.78  E-value: 4.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2787114717  207 LCHGDYRTGNYMV--DEHG---LSGILDWEFAQWGNPLQDLGWF 245
Cdd:smart00587 122 LNHGDLWANNIMFkyDDEGkpeDVALIDFQLSHYGSPAEDLHYF 165
 
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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