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Conserved domains on  [gi|1863079477|ref|WP_176547200|]
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aminoglycoside phosphotransferase family protein [Bacillus sp. AFS053548]

Protein Classification

aminoglycoside phosphotransferase family protein( domain architecture ID 12025366)

aminoglycoside phosphotransferase family protein may catalyze the phosphorylation of small molecules such as aminoglycosides and confer aminoglycoside antibiotic resistance; similar to Streptomyces coelicolor 3-hydroxyasparagine phosphotransferase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
8-242 2.23e-13

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: 68.30  E-value: 2.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477   8 EANFLGKGQEAEVY---SYDQKRVLKLYkPTAYSKLEILK--QFYESMNSSDAnFELPKIHEIIKEKDV---VLTIEKRI 79
Cdd:pfam01636   1 TLRPISSGASNRTYlvtTGDGRYVLRLP-PPGRAAEELRRelALLRHLAAAGV-PPVPRVLAGCTDAELlglPFLLMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477  80 EGRNIQKDLsnyDEQELDLFFENYLSTILSIQRIELEKQFkgikllsdyDEISSKDWNDFLKQSLLRKNTEVDHYLRRDV 159
Cdd:pfam01636  79 PGEVLARPL---LPEERGALLEALGRALARLHAVDPAALP---------LAGRLARLLELLRQLEAALARLLAAELLDRL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477 160 LDYEVKLKRLMDAfSVGYEGEYALVHGDYYPSNLLVNADGQINGVIDFGLMTlYGDPLFDVAlsWILFDLYDELGETKLE 239
Cdd:pfam01636 147 EELEERLLAALLA-LLPAELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAG-LGDPAYDLA--ILLNSWGRELGAELLA 222

                  ...
gi 1863079477 240 KYL 242
Cdd:pfam01636 223 AYL 225
 
Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
8-242 2.23e-13

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: 68.30  E-value: 2.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477   8 EANFLGKGQEAEVY---SYDQKRVLKLYkPTAYSKLEILK--QFYESMNSSDAnFELPKIHEIIKEKDV---VLTIEKRI 79
Cdd:pfam01636   1 TLRPISSGASNRTYlvtTGDGRYVLRLP-PPGRAAEELRRelALLRHLAAAGV-PPVPRVLAGCTDAELlglPFLLMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477  80 EGRNIQKDLsnyDEQELDLFFENYLSTILSIQRIELEKQFkgikllsdyDEISSKDWNDFLKQSLLRKNTEVDHYLRRDV 159
Cdd:pfam01636  79 PGEVLARPL---LPEERGALLEALGRALARLHAVDPAALP---------LAGRLARLLELLRQLEAALARLLAAELLDRL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477 160 LDYEVKLKRLMDAfSVGYEGEYALVHGDYYPSNLLVNADGQINGVIDFGLMTlYGDPLFDVAlsWILFDLYDELGETKLE 239
Cdd:pfam01636 147 EELEERLLAALLA-LLPAELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAG-LGDPAYDLA--ILLNSWGRELGAELLA 222

                  ...
gi 1863079477 240 KYL 242
Cdd:pfam01636 223 AYL 225
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
12-235 3.07e-12

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 65.52  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477  12 LGKGQEAEVY--SYDQKRVLKLYKPTAYSKLEILKQfYESMN--SSDANFELPKIHEIIKEKDVV---LTIEKRIEGRNI 84
Cdd:COG3173    28 LSGGWSNLTYrlDTGDRLVLRRPPRGLASAHDVRRE-ARVLRalAPRLGVPVPRPLALGEDGEVIgapFYVMEWVEGETL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477  85 QKDLSNYDEQELDLFFENYLSTILSIQRIELEKQfkgikLLSDYD----EISSKDWNDFLKQSLLRKNTEVDhyLRRDVL 160
Cdd:COG3173   107 EDALPDLSPAERRALARALGEFLAALHAVDPAAA-----GLADGRpeglERQLARWRAQLRRALARTDDLPA--LRERLA 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863079477 161 DYevkLKRLMDAfsvgyEGEYALVHGDYYPSNLLVN-ADGQINGVIDFGLMTLyGDPLFDVALSWILFDLYDELGE 235
Cdd:COG3173   180 AW---LAANLPE-----WGPPVLVHGDLRPGNLLVDpDDGRLTAVIDWELATL-GDPAADLAYLLLYWRLPDDLLG 246
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
184-228 1.66e-10

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: 59.94  E-value: 1.66e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1863079477 184 VHGDYYPSNLLVnADGQINGVIDFGLMTLyGDPLFDVALSWILFD 228
Cdd:cd05155   166 LHGDLHPGNLLV-RDGRLSAVIDFGDLGV-GDPACDLAIAWTLFD 208
 
Name Accession Description Interval E-value
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
8-242 2.23e-13

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: 68.30  E-value: 2.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477   8 EANFLGKGQEAEVY---SYDQKRVLKLYkPTAYSKLEILK--QFYESMNSSDAnFELPKIHEIIKEKDV---VLTIEKRI 79
Cdd:pfam01636   1 TLRPISSGASNRTYlvtTGDGRYVLRLP-PPGRAAEELRRelALLRHLAAAGV-PPVPRVLAGCTDAELlglPFLLMEYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477  80 EGRNIQKDLsnyDEQELDLFFENYLSTILSIQRIELEKQFkgikllsdyDEISSKDWNDFLKQSLLRKNTEVDHYLRRDV 159
Cdd:pfam01636  79 PGEVLARPL---LPEERGALLEALGRALARLHAVDPAALP---------LAGRLARLLELLRQLEAALARLLAAELLDRL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477 160 LDYEVKLKRLMDAfSVGYEGEYALVHGDYYPSNLLVNADGQINGVIDFGLMTlYGDPLFDVAlsWILFDLYDELGETKLE 239
Cdd:pfam01636 147 EELEERLLAALLA-LLPAELPPVLVHGDLHPGNLLVDPGGRVSGVIDFEDAG-LGDPAYDLA--ILLNSWGRELGAELLA 222

                  ...
gi 1863079477 240 KYL 242
Cdd:pfam01636 223 AYL 225
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
12-235 3.07e-12

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 65.52  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477  12 LGKGQEAEVY--SYDQKRVLKLYKPTAYSKLEILKQfYESMN--SSDANFELPKIHEIIKEKDVV---LTIEKRIEGRNI 84
Cdd:COG3173    28 LSGGWSNLTYrlDTGDRLVLRRPPRGLASAHDVRRE-ARVLRalAPRLGVPVPRPLALGEDGEVIgapFYVMEWVEGETL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477  85 QKDLSNYDEQELDLFFENYLSTILSIQRIELEKQfkgikLLSDYD----EISSKDWNDFLKQSLLRKNTEVDhyLRRDVL 160
Cdd:COG3173   107 EDALPDLSPAERRALARALGEFLAALHAVDPAAA-----GLADGRpeglERQLARWRAQLRRALARTDDLPA--LRERLA 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1863079477 161 DYevkLKRLMDAfsvgyEGEYALVHGDYYPSNLLVN-ADGQINGVIDFGLMTLyGDPLFDVALSWILFDLYDELGE 235
Cdd:COG3173   180 AW---LAANLPE-----WGPPVLVHGDLRPGNLLVDpDDGRLTAVIDWELATL-GDPAADLAYLLLYWRLPDDLLG 246
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
184-228 1.66e-10

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: 59.94  E-value: 1.66e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1863079477 184 VHGDYYPSNLLVnADGQINGVIDFGLMTLyGDPLFDVALSWILFD 228
Cdd:cd05155   166 LHGDLHPGNLLV-RDGRLSAVIDFGDLGV-GDPACDLAIAWTLFD 208
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
178-227 1.55e-09

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: 57.24  E-value: 1.55e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1863079477 178 EGEYALVHGDYYPSNLLVNADGQINGVIDFGLMTLyGDPLFDVAlsWILF 227
Cdd:cd05154   174 DGRPVLVHGDFRLGNLLFDPDGRVTAVLDWELATL-GDPLEDLA--WLLA 220
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
150-269 1.76e-07

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 49.78  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477 150 EVDHYLRRDVLDYEV---KLKRLMDAFSvGYEGEYALVHGDYYPSNLLVNADGQInGVIDFGLMTLyGDPLFDVALSWIL 226
Cdd:COG0510    16 RLERYLALGPRDLPEllrRLEELERALA-ARPLPLVLCHGDLHPGNFLVTDDGRL-YLIDWEYAGL-GDPAFDLAALLVE 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1863079477 227 FDLYDELGETKLEKYLnkvVNRLGEEVRITIHLYVLFYSIYSA 269
Cdd:COG0510    93 YGLSPEQAEELLEAYG---FGRPTEELLRRLRAYRALADLLWA 132
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
181-221 2.61e-06

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: 46.53  E-value: 2.61e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1863079477 181 YALVHGDYYPSNLLVNADGQINGVIDFGLMTlYGDPLFDVA 221
Cdd:cd05120   111 SVLTHGDLHPGNILVKPDGKLSGIIDWEFAG-YGPPAFDYA 150
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
156-221 2.01e-05

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: 45.30  E-value: 2.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1863079477 156 RRDVLDYEvkLKRLMDAFSVGYEGE-YALVHGDYYPSNLLVNaDGQINGVIDFGLMtLYGDPLFDVA 221
Cdd:COG2334   155 DRALLEEL--LDRLEARLAPLLGALpRGVIHGDLHPDNVLFD-GDGVSGLIDFDDA-GYGPRLYDLA 217
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
183-225 7.26e-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: 7.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1863079477 183 LVHGDYYPSNLLVNaDGQINGVIDFGLMTlYGDPLFDVA---LSWI 225
Cdd:cd05153   181 VIHADLFRDNVLFD-GDRLSGIIDFYDAC-YDPLLYDLAialNDWC 224
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
182-243 3.68e-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: 41.46  E-value: 3.68e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1863079477 182 ALVHGDYYPSNLLVNADGQINGVIDFGLMTLyGDPLFDVALswilfdLYDELGETKLEKYLN 243
Cdd:cd05152   186 VLVHGDLHPGHILVDEDGRVTGLIDWTEAKV-GDPADDFAW------HYAAFGEEALERLLD 240
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
40-210 1.45e-03

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 39.40  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477  40 LEILKQFYESMNSSDANFELPKIHEIIKEkdVVLTIEK----RIEGRNIQKdlsnydeqeldlFFENY------------ 103
Cdd:cd05121    74 LRILRRLARLLERLSPLLRRLDLVAIVDE--FARSLLEeldfRREARNAER------------FRKNLkdspdvyvpkvy 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477 104 --LST--ILSIQRIElekqfkGIKLlSDYDEISSKDWNdflkqsllrkntevdhylRRDVLdyevklKRLMDAFsvgYEG 179
Cdd:cd05121   140 peLSTrrVLVMEYID------GVKL-TDLEALRAAGID------------------RKELA------RRLVDAY---LKQ 185
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1863079477 180 --EYALVHGDYYPSNLLVNADGQInGVIDFGLM 210
Cdd:cd05121   186 ifEDGFFHADPHPGNILVLPDGRI-ALLDFGMV 217
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
183-251 7.02e-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: 36.48  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1863079477 183 LVHGDYYPSNLLVNaDGQInGVIDFGLMTLYGDP--------LFDVALSWILFDLYDELGETKLEKYL-----NKVVNRL 249
Cdd:COG3642    72 IVHGDLTTSNILVD-DGGV-YLIDFGLARYSDPLedkavdlaVLKRSLESTHPDPAEELWEAFLEGYRevgpaEEVLRRL 149

                  ..
gi 1863079477 250 GE 251
Cdd:COG3642   150 RE 151
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
163-217 7.67e-03

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 37.20  E-value: 7.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1863079477 163 EVK--LKRLMDAfsVGYEGEYALVHGDYYPSNLLVNADGQINgVIDFGLMTLYGDPL 217
Cdd:cd07843   107 EVKclMLQLLSG--VAHLHDNWILHRDLKTSNLLLNNRGILK-ICDFGLAREYGSPL 160
 
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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