NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|518600412|ref|WP_019770619|]
View 

acetyl-CoA carboxylase carboxyl transferase subunit alpha [Streptococcus sobrinus]

Protein Classification

acetyl-CoA carboxylase carboxyltransferase subunit alpha( domain architecture ID 10013922)

acetyl-CoA carboxylase carboxyltransferase subunit alpha (AccA) is a component of the acetyl coenzyme A carboxylase (ACC) complex that catalyzes the carboxylation of acetyl-CoA to form malonyl-CoA

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 1-256 0e+00

acetyl-CoA carboxylase subunit alpha; Provisional


:

Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 496.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   1 MSDVARILKEARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPN 80
Cdd:PRK12319   1 MTDVARILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  81 PDGYRKALRLMKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADK 160
Cdd:PRK12319  81 PEGYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 161 VWMLEHTIYAILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPEHGYFTSEIVENIKTSLIEELAQLSKL 240
Cdd:PRK12319 161 VWMLENTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPEHGYFSSEIIDMIKKNLIEELAQLSQK 240

                        250
                 ....*....|....*.
gi 518600412 241 PLDQLLENRYQRFRKY 256
Cdd:PRK12319 241 PLEQLLEERYQRFRKY 256
 
Name Accession Description Interval E-value
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 1-256 0e+00

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 496.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   1 MSDVARILKEARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPN 80
Cdd:PRK12319   1 MTDVARILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  81 PDGYRKALRLMKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADK 160
Cdd:PRK12319  81 PEGYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 161 VWMLEHTIYAILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPEHGYFTSEIVENIKTSLIEELAQLSKL 240
Cdd:PRK12319 161 VWMLENTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPEHGYFSSEIIDMIKKNLIEELAQLSQK 240

                        250
                 ....*....|....*.
gi 518600412 241 PLDQLLENRYQRFRKY 256
Cdd:PRK12319 241 PLEQLLEERYQRFRKY 256
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 11-256 1.90e-139

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: 394.02  E-value: 1.90e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  11 ARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRKALRL 90
Cdd:COG0825   61 ARHPQRPYTLDYIEAIFTDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  91 MKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPiiaiiigeggsggALALAVADKVWMLEHTIYA 170
Cdd:COG0825  141 MKLAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPiisvvigeggsggALAIGVGDRVLMLEHSIYS 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 171 ILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPE-----HgYFTSEIVENIKTSLIEELAQLSKLPLDQL 245
Cdd:COG0825  221 VISPEGCASILWKDASKAPEAAEALKITAQDLKELGIIDEIIPEplggaH-RDPEAAAENLKEALLKALKELKGLSPEEL 299

                        250
                 ....*....|.
gi 518600412 246 LENRYQRFRKY 256
Cdd:COG0825  300 LEQRYEKFRAI 310
AccA_sub NF041504
carboxyltransferase subunit alpha;
8-255 3.42e-127

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 361.00  E-value: 3.42e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   8 LKEARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRKA 87
Cdd:NF041504   4 VQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGYRKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  88 LRLMKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADKVWMLEHT 167
Cdd:NF041504  84 LRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLMLEHA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 168 IYAILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPEHGYFTS----EIVENIKTSLIEELAQLSKLPLD 243
Cdd:NF041504 164 IYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHrdpaALIAALGDAIEEALAELAGLSAD 243

                        250
                 ....*....|..
gi 518600412 244 QLLENRYQRFRK 255
Cdd:NF041504 244 ELIAQRREKFLA 255
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 7-256 4.61e-105

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: 307.12  E-value: 4.61e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412    7 ILKEARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRK 86
Cdd:TIGR00513  60 RLQLARHPDRPYTLDYIELIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRK 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   87 ALRLMKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADKVWMLEH 166
Cdd:TIGR00513 140 ALRLMKMAERFKMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEY 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  167 TIYAILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPE------HGYFtsEIVENIKTSLIEELAQLSKL 240
Cdd:TIGR00513 220 STYSVISPEGCAAILWKDASKAPKAAEAMKITAPDLKELGLIDSIIPEplggahRNPL--AAAASLKEQLLADLATLDQL 297

                         250
                  ....*....|....*.
gi 518600412  241 PLDQLLENRYQRFRKY 256
Cdd:TIGR00513 298 STEELKNRRYQKLMSL 313
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 11-95 8.64e-48

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: 155.26  E-value: 8.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   11 ARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRKALRL 90
Cdd:pfam03255  60 ARHPERPYTLDYIEALFDDFIELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRL 139


                  ....*
gi 518600412   91 MKQAE 95
Cdd:pfam03255 140 MKLAE 144
 
Name Accession Description Interval E-value
PRK12319 PRK12319
acetyl-CoA carboxylase subunit alpha; Provisional
 1-256 0e+00

acetyl-CoA carboxylase subunit alpha; Provisional


Pssm-ID: 183435 [Multi-domain]  Cd Length: 256  Bit Score: 496.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   1 MSDVARILKEARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPN 80
Cdd:PRK12319   1 MTDVARILKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  81 PDGYRKALRLMKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADK 160
Cdd:PRK12319  81 PEGYRKALRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 161 VWMLEHTIYAILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPEHGYFTSEIVENIKTSLIEELAQLSKL 240
Cdd:PRK12319 161 VWMLENTMYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPEHGYFSSEIIDMIKKNLIEELAQLSQK 240

                        250
                 ....*....|....*.
gi 518600412 241 PLDQLLENRYQRFRKY 256
Cdd:PRK12319 241 PLEQLLEERYQRFRKY 256
AccA COG0825
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ...
 11-256 1.90e-139

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: 394.02  E-value: 1.90e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  11 ARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRKALRL 90
Cdd:COG0825   61 ARHPQRPYTLDYIEAIFTDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEGYRKALRL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  91 MKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPiiaiiigeggsggALALAVADKVWMLEHTIYA 170
Cdd:COG0825  141 MKLAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPiisvvigeggsggALAIGVGDRVLMLEHSIYS 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 171 ILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPE-----HgYFTSEIVENIKTSLIEELAQLSKLPLDQL 245
Cdd:COG0825  221 VISPEGCASILWKDASKAPEAAEALKITAQDLKELGIIDEIIPEplggaH-RDPEAAAENLKEALLKALKELKGLSPEEL 299

                        250
                 ....*....|.
gi 518600412 246 LENRYQRFRKY 256
Cdd:COG0825  300 LEQRYEKFRAI 310
PRK05724 PRK05724
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
 11-256 3.69e-131

acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated


Pssm-ID: 235580 [Multi-domain]  Cd Length: 319  Bit Score: 373.32  E-value: 3.69e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  11 ARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRKALRL 90
Cdd:PRK05724  64 ARHPQRPYTLDYIELLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPEGYRKALRL 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  91 MKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADKVWMLEHTIYA 170
Cdd:PRK05724 144 MKMAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVLMLEYSTYS 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 171 ILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPE-----HgYFTSEIVENIKTSLIEELAQLSKLPLDQL 245
Cdd:PRK05724 224 VISPEGCASILWKDASKAPEAAEAMKITAQDLKELGIIDEIIPEplggaH-RDPEAAAAALKEALLEALAELKGLSPEEL 302

                        250
                 ....*....|.
gi 518600412 246 LENRYQRFRKY 256
Cdd:PRK05724 303 LERRYEKFMSI 313
AccA_sub NF041504
carboxyltransferase subunit alpha;
8-255 3.42e-127

carboxyltransferase subunit alpha;


Pssm-ID: 469391 [Multi-domain]  Cd Length: 257  Bit Score: 361.00  E-value: 3.42e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   8 LKEARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRKA 87
Cdd:NF041504   4 VQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGYRKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  88 LRLMKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADKVWMLEHT 167
Cdd:NF041504  84 LRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLMLEHA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 168 IYAILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPEHGYFTS----EIVENIKTSLIEELAQLSKLPLD 243
Cdd:NF041504 164 IYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLGGAHrdpaALIAALGDAIEEALAELAGLSAD 243

                        250
                 ....*....|..
gi 518600412 244 QLLENRYQRFRK 255
Cdd:NF041504 244 ELIAQRREKFLA 255
accA TIGR00513
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ...
 7-256 4.61e-105

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: 307.12  E-value: 4.61e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412    7 ILKEARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRK 86
Cdd:TIGR00513  60 RLQLARHPDRPYTLDYIELIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPEGYRK 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   87 ALRLMKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADKVWMLEH 166
Cdd:TIGR00513 140 ALRLMKMAERFKMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVNMLEY 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  167 TIYAILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPE------HGYFtsEIVENIKTSLIEELAQLSKL 240
Cdd:TIGR00513 220 STYSVISPEGCAAILWKDASKAPKAAEAMKITAPDLKELGLIDSIIPEplggahRNPL--AAAASLKEQLLADLATLDQL 297

                         250
                  ....*....|....*.
gi 518600412  241 PLDQLLENRYQRFRKY 256
Cdd:TIGR00513 298 STEELKNRRYQKLMSL 313
accA CHL00198
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
 8-255 2.82e-85

acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional


Pssm-ID: 214393 [Multi-domain]  Cd Length: 322  Bit Score: 257.05  E-value: 2.82e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   8 LKEARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRKA 87
Cdd:CHL00198  64 LHLVRQSERPTTLDYIPYILDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKA 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  88 LRLMKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADKVWMLEHT 167
Cdd:CHL00198 144 LRLMKHANKFGLPILTFIDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYA 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 168 IYAILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPE-----HGYfTSEIVENIKTSLIEELAQLSKLPL 242
Cdd:CHL00198 224 VYTVATPEACAAILWKDSKKSLDAAEALKITSEDLKVLGIIDEIIPEpiggaQAD-PASASKILKKKLIRQLDFLKILSP 302

                        250
                 ....*....|...
gi 518600412 243 DQLLENRYQRFRK 255
Cdd:CHL00198 303 SELKAHRYEKFRK 315
PLN03230 PLN03230
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
 8-255 1.24e-74

acetyl-coenzyme A carboxylase carboxyl transferase; Provisional


Pssm-ID: 178769 [Multi-domain]  Cd Length: 431  Bit Score: 233.30  E-value: 1.24e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   8 LKEARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRKA 87
Cdd:PLN03230 131 LSVARHPNRPTFLDHVLNMTDKWVELHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMPQPNGYRKA 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  88 LRLMKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADKVWMLEHT 167
Cdd:PLN03230 211 LRFMRHAEKFGFPILTFVDTPGAYAGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGNRMLMMENA 290

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 168 IYAILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPEH-GYFTSEIVE---NIKTSLIEELAQLSKLPLD 243
Cdd:PLN03230 291 VYYVASPEACAAILWKSAAAAPKAAEALRITAAELVKLGVVDEIVPEPlGGAHSDPLQaskNIKEVILRHMKELMKMDPE 370

                        250
                 ....*....|..
gi 518600412 244 QLLENRYQRFRK 255
Cdd:PLN03230 371 ELLQDRAAKFRK 382
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 11-255 6.82e-68

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 223.19  E-value: 6.82e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  11 ARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRKALRL 90
Cdd:PLN03229 155 ARHPNRPTFLDHIFNITDKFVELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKALRM 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  91 MKQAEKFGRPVVTFINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALAVADKVWMLEHTIYA 170
Cdd:PLN03229 235 MYYADHHGFPIVTFIDTPGAYADLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKLLMLENAVFY 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412 171 ILSPEGFASILWKDGSRATEAAELMKLTAGELYNMEVIDKVIPE-----HG--YFTSeivENIKTSLIEELAQLSKLPLD 243
Cdd:PLN03229 315 VASPEACAAILWKSAKAAPKAAEKLRITAQELCRLQIADGIIPEplggaHAdpSWTS---QQIKIAINENMDELGKMDTE 391

                        250
                 ....*....|..
gi 518600412 244 QLLENRYQRFRK 255
Cdd:PLN03229 392 ELLKHRMLKFRK 403
ACCA pfam03255
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ...
 11-95 8.64e-48

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: 155.26  E-value: 8.64e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   11 ARDQARMTTLDYAKEIFDDFFELHGDRHFADDGAVVGGLATLNGRPATVVGIQKGKNLQDNLNRNFGQPNPDGYRKALRL 90
Cdd:pfam03255  60 ARHPERPYTLDYIEALFDDFIELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEGYRKALRL 139


                  ....*
gi 518600412   91 MKQAE 95
Cdd:pfam03255 140 MKLAE 144
Carboxyl_trans pfam01039
Carboxyl transferase domain; All of the members in this family are biotin dependent ...
 28-196 1.90e-06

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: 48.41  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412   28 DDFFELHGDrhFADDgaVVGGLATLNGRPATVVGIQKGKNLqdnlnrnfGQPNPDGYRKALRLMKQAEKFGRPVVTFINT 107
Cdd:pfam01039 269 GEFFEIKPG--YAKT--VVTGFARLGGIPVGVVANQPRVGA--------GVLFPDSADKAARFIRDCDAFNLPLVILADV 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  108 AGAYPGIGAEERGQGEAIAKNLMEMSDLKVPIIAIIIGEGGSGGALALA----VADKVWMLEHTIYAILSPEGFASILwk 183
Cdd:pfam01039 337 PGFLPGQRQEYGGILKHGAKLLYALAEATVPKITVIPRKAYGGAYVVMDskinGADINFAWPTARIAVMGPEGAVEIK-- 414

                         170
                  ....*....|...
gi 518600412  184 dgSRATEAAELMK 196
Cdd:pfam01039 415 --FRKEKAAAEMR 425
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
26-138 2.43e-05

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 45.02  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  26 IFDD--FFELHgdRHFADdgAVVGGLATLNGRPatvVGIqkgknLQDNLNRNFGQPNPDGYRKALRLMKQAEKFGRPVVT 103
Cdd:COG4799  287 LVDGgsFFEFK--PLYGP--NIVTGFARIDGRP---VGI-----VANQPMVLAGVLDIDAADKAARFIRLCDAFNIPLVF 354

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 518600412 104 FINTAGAYPGIGAEERGQGEAIAKNLMEMSDLKVP 138
Cdd:COG4799  355 LVDVPGFMVGTEQERGGIIRHGAKLLYAVAEATVP 389
MmdA COG4799
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
27-117 1.41e-03

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


Pssm-ID: 443827 [Multi-domain]  Cd Length: 508  Bit Score: 39.63  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518600412  27 FDD--FFEL-----HGDRHFADD---GAVVGGLATLNGRPATVVGiqkgknlQDnlnrnF----GQPNPDGYRKALRLMK 92
Cdd:COG4799   44 LDPgsFLELgalagHRMYDDDDRvpgDGVVTGIGTVDGRPVVVVA-------ND-----FtvkgGSLGPMTAKKILRAQD 111

                         90       100
                 ....*....|....*....|....*
gi 518600412  93 QAEKFGRPVVTFINTAGAYPGIGAE 117
Cdd:COG4799  112 IALENGLPVIYLVDSGGARLQEGVE 136
ADOP TIGR03434
Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, ...
 37-82 5.94e-03

Acidobacterial duplicated orphan permease; Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.


Pssm-ID: 274576 [Multi-domain]  Cd Length: 803  Bit Score: 37.88  E-value: 5.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 518600412   37 RHFADDGAVVGGLATLNGRPATVVGIqkgknlqdnLNRNFGQPNPD 82
Cdd:TIGR03434 155 RRFGGDPAVVGRTIRLNGRPYTVVGV---------MPPGFTFPGRD 191
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH