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Conserved domains on  [gi|502827580|ref|WP_013062556|]
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acetyl-CoA carboxylase carboxyltransferase subunit alpha [Salinibacter ruber]

Protein Classification

AccA family protein( domain architecture ID 10002787)

AccA family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 6-326 0e+00

Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase alpha subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis


:

Pssm-ID: 440587 [Multi-domain]  Cd Length: 315  Bit Score: 577.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   6 HLLDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDF 85
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  86 TELRGDRKFGDDRSIVGGLAQFtgsrfgyRDRTVMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMAAKFGKPVVV 165
Cdd:COG0825   81 IELHGDRAFGDDPAIVGGLARF-------DGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIIT 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 166 LLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDRILMLENAWYSVIAPESCSQILWR 245
Cdd:COG0825  154 FIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWK 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 246 SWDHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADALDELEDLDPQALLDQRLEKFDALGAY 325
Cdd:COG0825  234 DASKAPEAAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGRF 313


                 .
gi 502827580 326 E 326
Cdd:COG0825  314 L 314
 
Name Accession Description Interval E-value
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 6-326 0e+00

Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase alpha subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440587 [Multi-domain]  Cd Length: 315  Bit Score: 577.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   6 HLLDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDF 85
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  86 TELRGDRKFGDDRSIVGGLAQFtgsrfgyRDRTVMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMAAKFGKPVVV 165
Cdd:COG0825   81 IELHGDRAFGDDPAIVGGLARF-------DGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIIT 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 166 LLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDRILMLENAWYSVIAPESCSQILWR 245
Cdd:COG0825  154 FIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWK 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 246 SWDHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADALDELEDLDPQALLDQRLEKFDALGAY 325
Cdd:COG0825  234 DASKAPEAAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGRF 313


                 .
gi 502827580 326 E 326
Cdd:COG0825  314 L 314
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 6-328 0e+00

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 558.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   6 HLLDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDF 85
Cdd:PRK05724   4 NYLDFEKPIAELEAKIEELRAVAEDSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIELLFTDF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  86 TELRGDRKFGDDRSIVGGLAQFtgsrfgyRDRTVMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMAAKFGKPVVV 165
Cdd:PRK05724  84 TELHGDRAFADDKAIVGGLARL-------NGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIIT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 166 LLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDRILMLENAWYSVIAPESCSQILWR 245
Cdd:PRK05724 157 FIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 246 SWDHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADALDELEDLDPQALLDQRLEKFDALGAY 325
Cdd:PRK05724 237 DASKAPEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGRF 316


                 ...
gi 502827580 326 ESA 328
Cdd:PRK05724 317 LES 319
AccA_sub NF041504
carboxyltransferase subunit alpha;
60-323 3.31e-150

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 422.63  E-value: 3.31e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  60 WQRVQIARHPERPYTLDHIEALTEDFTELRGDRKFGDDRSIVGGLAQFTGsrfgyrdRTVMIMGHQKGRDTKERKYRRFG 139
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRG-------RPVTVIGQEKGSDTEERLRHNFG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 140 MPNPEGYRKAERLMKMAAKFGKPVVVLLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGL 219
Cdd:NF041504  74 MARPEGYRKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALAN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 220 GDRILMLENAWYSVIAPESCSQILWRSWDHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADA 299
Cdd:NF041504 154 ANRVLMLEHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEA 233

                        250       260
                 ....*....|....*....|....
gi 502827580 300 LDELEDLDPQALLDQRLEKFDALG 323
Cdd:NF041504 234 LAELAGLSADELIAQRREKFLAMG 257
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 7-323 1.85e-146

acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the alpha chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273113 [Multi-domain]  Cd Length: 316  Bit Score: 415.36  E-value: 1.85e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580    7 LLDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDFT 86
Cdd:TIGR00513   5 YLDFEKPIAELEAKIESLRARSRDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIELIFDDFF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   87 ELRGDRKFGDDRSIVGGLAQFTGsrfgyrdRTVMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMAAKFGKPVVVL 166
Cdd:TIGR00513  85 ELAGDRAYADDKAIVGGIARLDG-------RPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  167 LDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDRILMLENAWYSVIAPESCSQILWRS 246
Cdd:TIGR00513 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502827580  247 WDHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADALDELEDLDPQALLDQRLEKFDALG 323
Cdd:TIGR00513 238 ASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLG 314
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 7-156 1.93e-88

Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A carboxylase carboxyltransferase is composed of an alpha and beta subunit.


Pssm-ID: 427221 [Multi-domain]  Cd Length: 144  Bit Score: 261.57  E-value: 1.93e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580    7 LLDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDFT 86
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELRKLAEESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFDDFI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   87 ELRGDRKFGDDRSIVGGLAQFtgsrfgyRDRTVMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMA 156
Cdd:pfam03255  81 ELHGDRLFGDDPAIVGGLARF-------DGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLA 143
 
Name Accession Description Interval E-value
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 6-326 0e+00

Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase alpha subunit is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440587 [Multi-domain]  Cd Length: 315  Bit Score: 577.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   6 HLLDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDF 85
Cdd:COG0825    1 NYLDFEKPIAELEAKIEELRALAEESGVDISEEIARLEKKLEKLLKEIYSNLTPWQKVQLARHPQRPYTLDYIEAIFTDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  86 TELRGDRKFGDDRSIVGGLAQFtgsrfgyRDRTVMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMAAKFGKPVVV 165
Cdd:COG0825   81 IELHGDRAFGDDPAIVGGLARF-------DGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRLMKLAEKFGLPIIT 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 166 LLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDRILMLENAWYSVIAPESCSQILWR 245
Cdd:COG0825  154 FIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVIGEGGSGGALAIGVGDRVLMLEHSIYSVISPEGCASILWK 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 246 SWDHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADALDELEDLDPQALLDQRLEKFDALGAY 325
Cdd:COG0825  234 DASKAPEAAEALKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAENLKEALLKALKELKGLSPEELLEQRYEKFRAIGRF 313


                 .
gi 502827580 326 E 326
Cdd:COG0825  314 L 314
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 6-328 0e+00

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 558.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   6 HLLDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDF 85
Cdd:PRK05724   4 NYLDFEKPIAELEAKIEELRAVAEDSDVDLSEEIERLEKKLEELTKKIYSNLTPWQKVQLARHPQRPYTLDYIELLFTDF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  86 TELRGDRKFGDDRSIVGGLAQFtgsrfgyRDRTVMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMAAKFGKPVVV 165
Cdd:PRK05724  84 TELHGDRAFADDKAIVGGLARL-------NGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRLMKMAEKFGLPIIT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 166 LLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDRILMLENAWYSVIAPESCSQILWR 245
Cdd:PRK05724 157 FIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYSVISPEGCASILWK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 246 SWDHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADALDELEDLDPQALLDQRLEKFDALGAY 325
Cdd:PRK05724 237 DASKAPEAAEAMKITAQDLKELGIIDEIIPEPLGGAHRDPEAAAAALKEALLEALAELKGLSPEELLERRYEKFMSIGRF 316


                 ...
gi 502827580 326 ESA 328
Cdd:PRK05724 317 LES 319
AccA_sub NF041504
carboxyltransferase subunit alpha;
60-323 3.31e-150

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 422.63  E-value: 3.31e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  60 WQRVQIARHPERPYTLDHIEALTEDFTELRGDRKFGDDRSIVGGLAQFTGsrfgyrdRTVMIMGHQKGRDTKERKYRRFG 139
Cdd:NF041504   1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRG-------RPVTVIGQEKGSDTEERLRHNFG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 140 MPNPEGYRKAERLMKMAAKFGKPVVVLLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGL 219
Cdd:NF041504  74 MARPEGYRKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALAN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 220 GDRILMLENAWYSVIAPESCSQILWRSWDHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADA 299
Cdd:NF041504 154 ANRVLMLEHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHRDPAALIAALGDAIEEA 233

                        250       260
                 ....*....|....*....|....
gi 502827580 300 LDELEDLDPQALLDQRLEKFDALG 323
Cdd:NF041504 234 LAELAGLSADELIAQRREKFLAMG 257
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 7-323 1.85e-146

acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase contains a biotin carboxyl carrier protein or domain, a biotin carboxylase, and a carboxyl transferase. This model represents the alpha chain of the carboxyl transferase for cases in which the architecture of the protein is as in E. coli, in which the carboxyltransferase portion consists of two non-identical subnits, alpha and beta. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 273113 [Multi-domain]  Cd Length: 316  Bit Score: 415.36  E-value: 1.85e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580    7 LLDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDFT 86
Cdd:TIGR00513   5 YLDFEKPIAELEAKIESLRARSRDEDVDLSEEIERLEKRSVELTKKIFSNLGAWQRLQLARHPDRPYTLDYIELIFDDFF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   87 ELRGDRKFGDDRSIVGGLAQFTGsrfgyrdRTVMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMAAKFGKPVVVL 166
Cdd:TIGR00513  85 ELAGDRAYADDKAIVGGIARLDG-------RPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRKALRLMKMAERFKMPIITF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  167 LDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDRILMLENAWYSVIAPESCSQILWRS 246
Cdd:TIGR00513 158 IDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEYSTYSVISPEGCAAILWKD 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502827580  247 WDHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADALDELEDLDPQALLDQRLEKFDALG 323
Cdd:TIGR00513 238 ASKAPKAAEAMKITAPDLKELGLIDSIIPEPLGGAHRNPLAAAASLKEQLLADLATLDQLSTEELKNRRYQKLMSLG 314
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 8-326 6.82e-121

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 354.63  E-value: 6.82e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   8 LDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDFTE 87
Cdd:PLN03230  76 LPFEKPIVDLENRIDEVRELANKTGVDFSAQIAELEERYDQVRRELYSRLTPVQRLSVARHPNRPTFLDHVLNMTDKWVE 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  88 LRGDRKFGDDRSIVGGLAQFTGSRFgyrdrtvMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMAAKFGKPVVVLL 167
Cdd:PLN03230 156 LHGDRAGFDDPAIVCGIGSMEGMSF-------MFIGHQKGRNTKENIYRNFAMPQPNGYRKALRFMRHAEKFGFPILTFV 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 168 DTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDRILMLENAWYSVIAPESCSQILWRSW 247
Cdd:PLN03230 229 DTPGAYAGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGNRMLMMENAVYYVASPEACAAILWKSA 308

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502827580 248 DHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADALDELEDLDPQALLDQRLEKFDALGAYE 326
Cdd:PLN03230 309 AAAPKAAEALRITAAELVKLGVVDEIVPEPLGGAHSDPLQASKNIKEVILRHMKELMKMDPEELLQDRAAKFRKIGEFD 387
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 6-325 7.20e-121

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 350.65  E-value: 7.20e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   6 HLLDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDF 85
Cdd:CHL00198   7 HVPDFMKPLAELESQVEELSKLAPKNDKVINNKLKSFQRKLRILKKEIFYSLTPLQRLHLVRQSERPTTLDYIPYILDEW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  86 TELRGDRKFGDDRSIVGGLAQFTGsrfgyrdRTVMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMAAKFGKPVVV 165
Cdd:CHL00198  87 IELHGDRGGSDDPALVGGIGKING-------RTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKALRLMKHANKFGLPILT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 166 LLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDRILMLENAWYSVIAPESCSQILWR 245
Cdd:CHL00198 160 FIDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYAVYTVATPEACAAILWK 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 246 SWDHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADALDELEDLDPQALLDQRLEKFDALGAY 325
Cdd:CHL00198 240 DSKKSLDAAEALKITSEDLKVLGIIDEIIPEPIGGAQADPASASKILKKKLIRQLDFLKILSPSELKAHRYEKFRKLGAF 319
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 8-331 4.01e-112

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 342.60  E-value: 4.01e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   8 LDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDFTE 87
Cdd:PLN03229  97 LDFEKPLVDLEKKIVDVRKMANETGLDFSDQIISLESKYQQALKDLYTHLTPIQRVNIARHPNRPTFLDHIFNITDKFVE 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  88 LRGDRKFGDDRSIVGGLAQFTGSRFgyrdrtvMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMAAKFGKPVVVLL 167
Cdd:PLN03229 177 LHGDRAGYDDPAIVTGIGTIDGKRY-------MFIGHQKGRNTKENIMRNFGMPTPHGYRKALRMMYYADHHGFPIVTFI 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 168 DTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDRILMLENAWYSVIAPESCSQILWRSW 247
Cdd:PLN03229 250 DTPGAYADLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKLLMLENAVFYVASPEACAAILWKSA 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 248 DHKEDAAQALKLTATDLTEVGIVDEIVPEPVGGAHRDPQRTYQAVGAAVADALDELEDLDPQALLDQRLEKFDALGAYES 327
Cdd:PLN03229 330 KAAPKAAEKLRITAQELCRLQIADGIIPEPLGGAHADPSWTSQQIKIAINENMDELGKMDTEELLKHRMLKFRKIGGFQE 409


                 ....
gi 502827580 328 AEPM 331
Cdd:PLN03229 410 GVPV 413
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 7-156 1.93e-88

Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A carboxylase carboxyltransferase is composed of an alpha and beta subunit.


Pssm-ID: 427221 [Multi-domain]  Cd Length: 144  Bit Score: 261.57  E-value: 1.93e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580    7 LLDFEKPLVELEDKLTEMRELNAETQDDLSNEIEALEERVEQLRTSIYRNLTRWQRVQIARHPERPYTLDHIEALTEDFT 86
Cdd:pfam03255   1 YLDFEKPIAELEAKIEELRKLAEESGVDLSEEIEKLEEKLEKLRKEIYSNLTPWQKVQLARHPERPYTLDYIEALFDDFI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   87 ELRGDRKFGDDRSIVGGLAQFtgsrfgyRDRTVMIMGHQKGRDTKERKYRRFGMPNPEGYRKAERLMKMA 156
Cdd:pfam03255  81 ELHGDRLFGDDPAIVGGLARF-------DGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRLMKLA 143
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 63-319 7.87e-83

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 251.62  E-value: 7.87e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  63 VQIARHPERPYTLDHIEALTEDFTELRGDRKFGDDRSIVGGLAQFTGsrfgyrdRTVMIMGHQKGRDTKERKYRRFGMPN 142
Cdd:PRK12319   8 LKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAG-------QPVTVVGIQKGKNLQDNLKRNFGQPH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 143 PEGYRKAERLMKMAAKFGKPVVVLLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVGLGDR 222
Cdd:PRK12319  81 PEGYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 223 ILMLENAWYSVIAPESCSQILWRSWDHKEDAAQALKLTATDLTEVGIVDEIVPEpvggAHRDPQRTYQAVGAAVADALDE 302
Cdd:PRK12319 161 VWMLENTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPE----HGYFSSEIIDMIKKNLIEELAQ 236

                        250
                 ....*....|....*..
gi 502827580 303 LEDLDPQALLDQRLEKF 319
Cdd:PRK12319 237 LSQKPLEQLLEERYQRF 253
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 143-288 1.37e-09

Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.


Pssm-ID: 426008 [Multi-domain]  Cd Length: 491  Bit Score: 59.19  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  143 PEGYRKAERLMKMAAKFGKPVVVLLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGEGASGGALGVG---L 219
Cdd:pfam01039 310 PDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDskiN 389

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502827580  220 GDRIL-MLENAWYSVIAPESCSQILWRSWDHKED-------AAQALKLTATDLTEVGIVDEIVPEPVgGAHRDPQRT 288
Cdd:pfam01039 390 GADINfAWPTARIAVMGPEGAVEIKFRKEKAAAEmrgkdlaATRKQKIAEYEEELSPPYVAAARGFA-DAVIDPGRT 465
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 83-229 3.05e-05

Carboxyl transferase domain; All of the members in this family are biotin dependent carboxylases. The carboxyl transferase domain carries out the following reaction; transcarboxylation from biotin to an acceptor molecule. There are two recognized types of carboxyl transferase. One of them uses acyl-CoA and the other uses 2-oxoacid as the acceptor molecule of carbon dioxide. All of the members in this family utilize acyl-CoA as the acceptor molecule.


Pssm-ID: 426008 [Multi-domain]  Cd Length: 491  Bit Score: 45.33  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580   83 EDFTELRGDrKFGDDRSIVGGLAQFTGSRFGyrdRTVMIMGHQKgrdTKerkyrrFGMP-NPEGYRKAERLMKMAAKFGK 161
Cdd:pfam01039  27 EDLFFHRAT-EFGRKRIPRDGVVTGSGAVIG---RAVEVVAQDF---TV------FGGSlGPAKGEKILRAMEIAIKTGL 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502827580  162 PVVVLLDTPGAYPGMGAEERGQAEAIAHNLFEMARlETPVVIVVIGEGASGGALGVGLGDRILMLENA 229
Cdd:pfam01039  94 PLIGINDSGGARIQEGVENLRGSGKIFGRNSLASG-VIPQISLIMGPCAGGGAYLPALGDFVIMVEGT 160
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
16-228 7.93e-05

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 44.25  E-value: 7.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  16 ELEDKLTEMRELNAETQDdlsneiEALEERVEQLRTsiyRN-LTrwqrvqiARhpERpytldhIEALTED--FTE---LR 89
Cdd:COG4799    1 AMRALLAELRARREEALL------GGGEKAIERQHA---RGkLT-------AR--ER------IDLLLDPgsFLElgaLA 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  90 GDRKFGDDRS-----IVGGLAQFTGsrfgyrdRTVMIMGHQ---KGrdtkerkyrrfGMPNPEGYRKAERLMKMAAKFGK 161
Cdd:COG4799   57 GHRMYDDDDRvpgdgVVTGIGTVDG-------RPVVVVANDftvKG-----------GSLGPMTAKKILRAQDIALENGL 118

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502827580 162 PVVVLLDTPGAYPGMGAEERGQAEAIAHNLFEMARLeTPVVIVVIGEGASGGALGVGLGDRILMLEN 228
Cdd:COG4799  119 PVIYLVDSGGARLQEGVESFAGYGRIFYRNARSSGG-IPQISVIMGPCAAGGAYSPALSDFVIMVKG 184
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
143-301 6.08e-04

Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 41.55  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 143 PEGYRKAERLMKMAAKFGKPVVVLLDTPGAYPGMGAEERGQAEAIAHNLFEMARLETPVVIVVIGeGASGGALGV----G 218
Cdd:COG4799  332 IDAADKAARFIRLCDAFNIPLVFLVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVILR-KAYGAGYYAmcgkA 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580 219 LG-DRILMLENAWYSVIAPESCSQILWR----SWDHKEDAAQAL------KLTATDLTEVGIVDEIVpepvggahrDPQR 287
Cdd:COG4799  411 LGpDFLFAWPTAEIAVMGGEGAANVLYRrelaAAEDPEALRAELiaeyeeQANPYYAAARGWIDDVI---------DPRD 481

                        170
                 ....*....|....
gi 502827580 288 TYQAVGAAVADALD 301
Cdd:COG4799  482 TRRVLARALEAAAN 495
MdcE pfam06833
Malonate decarboxylase gamma subunit (MdcE); This family consists of several bacterial ...
 161-264 7.07e-04

Malonate decarboxylase gamma subunit (MdcE); This family consists of several bacterial malonate decarboxylase gamma subunit proteins. Malonate decarboxylase of Klebsiella pneumoniae consists of four different subunits and catalyzes the conversion of malonate plus H+ to acetate and CO2. The catalysis proceeds via acetyl and malonyl thioester residues with the phosphribosyl-dephospho-CoA prosthetic group of the acyl carrier protein (ACP) subunit. MdcD and E together probably function as malonyl-S-ACP decarboxylase.


Pssm-ID: 399666  Cd Length: 232  Bit Score: 40.56  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502827580  161 KPVVVLLDTPGAYPGMGAEERGQAEAIAH--NLFEMARLE-TPVVIVVIGEGASGGALGVGL-GDRILMLENAWYSVIAP 236
Cdd:pfam06833  65 RPILALVDVPSQRYGRRDELLGIHQALAHlaKALALARLAgHPTIGLLYGKSMSGAFLAHGLqANRLIALPGAMVHVMDL 144

                          90       100
                  ....*....|....*....|....*...
gi 502827580  237 ESCSQILWRSWDHKEDAAQALKLTATDL 264
Cdd:pfam06833 145 ASMARVTKRSVEALEALAASTPVFAPGL 172
 
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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