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Conserved domains on  [gi|446118842|ref|WP_000196697|]
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MULTISPECIES: Mph(C) family macrolide 2'-phosphotransferase [Bacillales]

Protein Classification

macrolide 2'-phosphotransferase( domain architecture ID 10142354)

macrolide 2'-phosphotransferase is an aminoglycoside phosphotransferase family protein that 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 8-283 8.52e-154

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: 430.90  E-value: 8.52e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842   8 IKCAEKYQLHIQPQTISLNESGLDFQVAFGKDKHGVEWVLRLPRRPDVYKRTKPEKQTVDFLQKNVSFEIPKWKVHAKDL 87
Cdd:cd05152    1 LALAAKHGLDLKPATLRLNESGLDFQVAFARDTEGRRWVLRIPRRPDVSERLEAEKKVLDLVTPHLPFAVPDWRIHTPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  88 IAYPKLTGKPAATIDPEIQNYVWEIEHKPLPENFINTLAETLVDLHNIPEENINVQHINIKTIQEIKNDFQRRMNKVKET 167
Cdd:cd05152   81 IAYPLLPGVPAATIDPEIQNYVWNWDPLAPPPVFARSLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKET 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842 168 YGVSDELWNRWKQWLENDELWPRHATMIHGDLHPGHIMVDNQANVTGLIDWTEATHSDPSMDFIGHHRVFDDEGLEQLIT 247
Cdd:cd05152  161 FGVPPALLARWQAWLADDSLWPFHTVLVHGDLHPGHILVDEDGRVTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLD 240

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446118842 248 AYGKAGGEIWPRMKEHIIELNAVFPMFIAEFAMESG 283
Cdd:cd05152  241 AYEKAGGEVWPRMLEHIIELAAAYPLTIALFALDSG 276
 
Name Accession Description Interval E-value
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 8-283 8.52e-154

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: 430.90  E-value: 8.52e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842   8 IKCAEKYQLHIQPQTISLNESGLDFQVAFGKDKHGVEWVLRLPRRPDVYKRTKPEKQTVDFLQKNVSFEIPKWKVHAKDL 87
Cdd:cd05152    1 LALAAKHGLDLKPATLRLNESGLDFQVAFARDTEGRRWVLRIPRRPDVSERLEAEKKVLDLVTPHLPFAVPDWRIHTPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  88 IAYPKLTGKPAATIDPEIQNYVWEIEHKPLPENFINTLAETLVDLHNIPEENINVQHINIKTIQEIKNDFQRRMNKVKET 167
Cdd:cd05152   81 IAYPLLPGVPAATIDPEIQNYVWNWDPLAPPPVFARSLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKET 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842 168 YGVSDELWNRWKQWLENDELWPRHATMIHGDLHPGHIMVDNQANVTGLIDWTEATHSDPSMDFIGHHRVFDDEGLEQLIT 247
Cdd:cd05152  161 FGVPPALLARWQAWLADDSLWPFHTVLVHGDLHPGHILVDEDGRVTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLD 240

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446118842 248 AYGKAGGEIWPRMKEHIIELNAVFPMFIAEFAMESG 283
Cdd:cd05152  241 AYEKAGGEVWPRMLEHIIELAAAYPLTIALFALDSG 276
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 22-263 1.04e-30

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: 115.29  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842   22 TISLNESGLDFQVAFGKDKHGvEWVLRLPRRPDVYKRTKPEKQTVDFLQKNVSFEIPKwkVHAKDLIAYPKLTGKPAATI 101
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDG-RYVLRLPPPGRAAEELRRELALLRHLAAAGVPPVPR--VLAGCTDAELLGLPFLLMEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  102 DPEIQNYVWEIEHKPlpENFINTLAETLVDLHNIPEENINVQHINIKTIQEIKNDFQRRMNKVKETYGVS-DELWNRWKQ 180
Cdd:pfam01636  78 LPGEVLARPLLPEER--GALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRlEELEERLLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  181 WLenDELWPRHATM--IHGDLHPGHIMVDNQANVTGLIDWTEATHSDPSMDFIGHHRVFDDEGLEQLITAYGKAGGEI-W 257
Cdd:pfam01636 156 AL--LALLPAELPPvlVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFgY 233


                  ....*.
gi 446118842  258 PRMKEH 263
Cdd:pfam01636 234 ARLREL 239
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 41-256 2.32e-25

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 102.12  E-value: 2.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  41 HGVEWVLRL-PRRPDVYKRTKPEKQTVDFLQKNVSFEIPKwkvhakdliayPKLTGKPAATIDPEIQNYVW---EIEHKP 116
Cdd:COG3173   41 TGDRLVLRRpPRGLASAHDVRREARVLRALAPRLGVPVPR-----------PLALGEDGEVIGAPFYVMEWvegETLEDA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842 117 LPEN-------FINTLAETLVDLHNIPEENINVQHINIKTIQEIKNDFQRRMNKVKETYGVSDELWNRWKQWLENDELWP 189
Cdd:COG3173  110 LPDLspaerraLARALGEFLAALHAVDPAAAGLADGRPEGLERQLARWRAQLRRALARTDDLPALRERLAAWLAANLPEW 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446118842 190 RHATMIHGDLHPGHIMVD-NQANVTGLIDWTEATHSDPSMDF---IGHHRVFDD--EGLEQLITAYGKAGGEI 256
Cdd:COG3173  190 GPPVLVHGDLRPGNLLVDpDDGRLTAVIDWELATLGDPAADLaylLLYWRLPDDllGPRAAFLAAYEEATGDL 262
 
Name Accession Description Interval E-value
MPH2' cd05152
Macrolide 2'-Phosphotransferase; MPH2' catalyzes the transfer of the gamma-phosphoryl group ...
 8-283 8.52e-154

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: 430.90  E-value: 8.52e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842   8 IKCAEKYQLHIQPQTISLNESGLDFQVAFGKDKHGVEWVLRLPRRPDVYKRTKPEKQTVDFLQKNVSFEIPKWKVHAKDL 87
Cdd:cd05152    1 LALAAKHGLDLKPATLRLNESGLDFQVAFARDTEGRRWVLRIPRRPDVSERLEAEKKVLDLVTPHLPFAVPDWRIHTPEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  88 IAYPKLTGKPAATIDPEIQNYVWEIEHKPLPENFINTLAETLVDLHNIPEENINVQHINIKTIQEIKNDFQRRMNKVKET 167
Cdd:cd05152   81 IAYPLLPGVPAATIDPEIQNYVWNWDPLAPPPVFARSLGKALAALHSIPADLAAAAGLPVYTAEEVRARMAARMDRVKET 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842 168 YGVSDELWNRWKQWLENDELWPRHATMIHGDLHPGHIMVDNQANVTGLIDWTEATHSDPSMDFIGHHRVFDDEGLEQLIT 247
Cdd:cd05152  161 FGVPPALLARWQAWLADDSLWPFHTVLVHGDLHPGHILVDEDGRVTGLIDWTEAKVGDPADDFAWHYAAFGEEALERLLD 240

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446118842 248 AYGKAGGEIWPRMKEHIIELNAVFPMFIAEFAMESG 283
Cdd:cd05152  241 AYEKAGGEVWPRMLEHIIELAAAYPLTIALFALDSG 276
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
 22-263 1.04e-30

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: 115.29  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842   22 TISLNESGLDFQVAFGKDKHGvEWVLRLPRRPDVYKRTKPEKQTVDFLQKNVSFEIPKwkVHAKDLIAYPKLTGKPAATI 101
Cdd:pfam01636   1 TLRPISSGASNRTYLVTTGDG-RYVLRLPPPGRAAEELRRELALLRHLAAAGVPPVPR--VLAGCTDAELLGLPFLLMEY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  102 DPEIQNYVWEIEHKPlpENFINTLAETLVDLHNIPEENINVQHINIKTIQEIKNDFQRRMNKVKETYGVS-DELWNRWKQ 180
Cdd:pfam01636  78 LPGEVLARPLLPEER--GALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDRlEELEERLLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  181 WLenDELWPRHATM--IHGDLHPGHIMVDNQANVTGLIDWTEATHSDPSMDFIGHHRVFDDEGLEQLITAYGKAGGEI-W 257
Cdd:pfam01636 156 AL--LALLPAELPPvlVHGDLHPGNLLVDPGGRVSGVIDFEDAGLGDPAYDLAILLNSWGRELGAELLAAYLAAYGAFgY 233


                  ....*.
gi 446118842  258 PRMKEH 263
Cdd:pfam01636 234 ARLREL 239
YcbJ COG3173
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ...
 41-256 2.32e-25

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


Pssm-ID: 442406 [Multi-domain]  Cd Length: 284  Bit Score: 102.12  E-value: 2.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  41 HGVEWVLRL-PRRPDVYKRTKPEKQTVDFLQKNVSFEIPKwkvhakdliayPKLTGKPAATIDPEIQNYVW---EIEHKP 116
Cdd:COG3173   41 TGDRLVLRRpPRGLASAHDVRREARVLRALAPRLGVPVPR-----------PLALGEDGEVIGAPFYVMEWvegETLEDA 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842 117 LPEN-------FINTLAETLVDLHNIPEENINVQHINIKTIQEIKNDFQRRMNKVKETYGVSDELWNRWKQWLENDELWP 189
Cdd:COG3173  110 LPDLspaerraLARALGEFLAALHAVDPAAAGLADGRPEGLERQLARWRAQLRRALARTDDLPALRERLAAWLAANLPEW 189

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446118842 190 RHATMIHGDLHPGHIMVD-NQANVTGLIDWTEATHSDPSMDF---IGHHRVFDD--EGLEQLITAYGKAGGEI 256
Cdd:COG3173  190 GPPVLVHGDLRPGNLLVDpDDGRLTAVIDWELATLGDPAADLaylLLYWRLPDDllGPRAAFLAAYEEATGDL 262
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
 44-237 3.72e-10

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: 57.31  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  44 EWVLRLPRRPDVYKRTKpEKQTVDFLQKNVSFEIPK----WKVHAKDLIAYPKLTGKPAATIDPEIQnyvweIEHKplpE 119
Cdd:cd05120   22 EYVLKIGPPRLKKDLEK-EAAMLQLLAGKLSLPVPKvygfGESDGWEYLLMERIEGETLSEVWPRLS-----EEEK---E 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842 120 NFINTLAETLVDLHNIPEEninvqhiniktiqeikndfqrrmnkvketygvsdelwnrwkqwlendelwprhaTMIHGDL 199
Cdd:cd05120   93 KIADQLAEILAALHRIDSS------------------------------------------------------VLTHGDL 118

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446118842 200 HPGHIMVDNQANVTGLIDWTEATHSDPSMDFIGHHRVF 237
Cdd:cd05120  119 HPGNILVKPDGKLSGIIDWEFAGYGPPAFDYAAALRDW 156
APH_ChoK_like_1 cd05155
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ...
 188-259 7.79e-08

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: 52.24  E-value: 7.79e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446118842 188 WPRHATMIHGDLHPGHIMVDNQaNVTGLIDWTEATHSDPSMDFIGHHRVFDDEGLEQLITAYGkAGGEIWPR 259
Cdd:cd05155  159 WAGPPVWLHGDLHPGNLLVRDG-RLSAVIDFGDLGVGDPACDLAIAWTLFDAAARAAFRAALG-VDDATWAR 228
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
171-265 1.22e-07

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


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 50.16  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842 171 SDELWNRWKQWLENDELWPRHATMIHGDLHPGHIMVDNQANVTgLIDWTEATHSDPSMD---FIGHHRvFDDEGLEQLIT 247
Cdd:COG0510   28 LPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDGRLY-LIDWEYAGLGDPAFDlaaLLVEYG-LSPEQAEELLE 105

                         90       100
                 ....*....|....*....|
gi 446118842 248 AYGKAGG--EIWPRMKEHII 265
Cdd:COG0510  106 AYGFGRPteELLRRLRAYRA 125
ACAD10_11_N-like cd05154
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ...
 125-259 1.26e-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: 45.68  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842 125 LAETLVDLHNIPeeninVQHINIKTIQEIKNDFQR---RMNKVKETYGVSD-ELWNRWKQWLEndELWP--RHATMIHGD 198
Cdd:cd05154  111 LVDALAALHSVD-----PAALGLADLGRPEGYLERqvdRWRRQLEAAATDPpPALEEALRWLR--ANLPadGRPVLVHGD 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446118842 199 LHPGHIMVDNQANVTGLIDWtEATH-SDPSMDfIGHHRVFDDEGLEQLITAYGKAGGEIWPR 259
Cdd:cd05154  184 FRLGNLLFDPDGRVTAVLDW-ELATlGDPLED-LAWLLARWWRPGDPPGLAAPTRLPGFPSR 243
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
 90-229 2.15e-04

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 42.25  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842  90 YPKLTGKPAATIDPEIqnyvweiehkplpenfINTLAETLVDLHNI------PEENINVQHINIKTIQEIKNDFQRRMNK 163
Cdd:cd05153   94 FPFLPGESLTTPTPEQ----------------CRAIGAALARLHLAlagfppPRPNPRGLAWWKPLAERLKARLDLLAAD 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446118842 164 VKETygVSDELwNRWKQWLENDElwPRhaTMIHGDLHPGHIMVDNQaNVTGLIDWTEATHSDPSMD 229
Cdd:cd05153  158 DRAL--LEDEL-ARLQALAPSDL--PR--GVIHADLFRDNVLFDGD-RLSGIIDFYDACYDPLLYD 215
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
 172-266 7.72e-04

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: 40.29  E-value: 7.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842 172 DELWNRWKQWLENdelWPRHAtmIHGDLHPGHIMVDNqANVTGLIDWteathsdpsmDFIGH-HRVFDdegleqL-ITAY 249
Cdd:COG2334  164 DRLEARLAPLLGA---LPRGV--IHGDLHPDNVLFDG-DGVSGLIDF----------DDAGYgPRLYD------LaIALN 221

                         90
                 ....*....|....*..
gi 446118842 250 GKAGGEIWPRMKEHIIE 266
Cdd:COG2334  222 GWADGPLDPARLAALLE 238
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
 196-271 5.42e-03

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 37.71  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446118842 196 HGDLHPGHIMVDNQANVTGLIDWTEATHSDPSMDF-IGHHRVFDDEGLEQ---LITAYGKAGGEIWPRmkeHIIELNAVF 271
Cdd:cd13993  130 HRDIKPENILLSQDEGTVKLCDFGLATTEKISMDFgVGSEFYMAPECFDEvgrSLKGYPCAAGDIWSL---GIILLNLTF 206
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 195-254 6.82e-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: 6.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446118842 195 IHGDLHPGHIMVDNQAnvTGLIDWTEATHSDP----SMD-------FIGHHRVFDDEGLEQLITAYGKAGG 254
Cdd:COG3642   73 VHGDLTTSNILVDDGG--VYLIDFGLARYSDPledkAVDlavlkrsLESTHPDPAEELWEAFLEGYREVGP 141
 
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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