|
Name |
Accession |
Description |
Interval |
E-value |
| AccA |
COG0825 |
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
9-266 |
3.94e-157 |
|
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: 439.47 E-value: 3.94e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 9 AWTTVQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPEG 88
Cdd:COG0825 54 PWQKVQLARHPQRPYTLDYIEAIFTDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 89 YRKSQRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATV-----------LGeggsgga 157
Cdd:COG0825 134 YRKALRLMKLAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVigeggsggalaIG------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 158 lgigVADRVIMLSHSIYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDEGE-GAHLDPERVMQNLKV 236
Cdd:COG0825 207 ----VGDRVLMLEHSIYSVISPEGCASILWKDASKAPEAAEALKITAQDLKELGIIDEIIPEPLgGAHRDPEAAAENLKE 282
|
250 260 270
....*....|....*....|....*....|
gi 446633057 237 VLKQALDELLPMDANERCEARYQRLMKFGS 266
Cdd:COG0825 283 ALLKALKELKGLSPEELLEQRYEKFRAIGR 312
|
|
| PRK05724 |
PRK05724 |
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated |
8-266 |
6.93e-150 |
|
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
Pssm-ID: 235580 [Multi-domain] Cd Length: 319 Bit Score: 421.47 E-value: 6.93e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 8 KAWTTVQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPE 87
Cdd:PRK05724 56 TPWQKVQLARHPQRPYTLDYIELLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 88 GYRKSQRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVLGEGGSGGALGIGVADRVI 167
Cdd:PRK05724 136 GYRKALRLMKMAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 168 MLSHSIYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDE--GeGAHLDPERVMQNLKVVLKQALDEL 245
Cdd:PRK05724 216 MLEYSTYSVISPEGCASILWKDASKAPEAAEAMKITAQDLKELGIIDEIIPEplG-GAHRDPEAAAAALKEALLEALAEL 294
|
250 260
....*....|....*....|.
gi 446633057 246 LPMDANERCEARYQRLMKFGS 266
Cdd:PRK05724 295 KGLSPEELLERRYEKFMSIGR 315
|
|
| AccA_sub |
NF041504 |
carboxyltransferase subunit alpha; |
10-265 |
3.44e-134 |
|
carboxyltransferase subunit alpha;
Pssm-ID: 469391 [Multi-domain] Cd Length: 257 Bit Score: 379.49 E-value: 3.44e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 10 WTTVQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPEGY 89
Cdd:NF041504 1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 90 RKSQRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVLGEGGSGGALGIGVADRVIML 169
Cdd:NF041504 81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 170 SHSIYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDEGE-GAHLDPERVMQNLKVVLKQALDELLPM 248
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLgGAHRDPAALIAALGDAIEEALAELAGL 240
|
250
....*....|....*..
gi 446633057 249 DANERCEARYQRLMKFG 265
Cdd:NF041504 241 SADELIAQRREKFLAMG 257
|
|
| accA |
TIGR00513 |
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ... |
8-266 |
5.42e-115 |
|
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: 332.93 E-value: 5.42e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 8 KAWTTVQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPE 87
Cdd:TIGR00513 56 GAWQRLQLARHPDRPYTLDYIELIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 88 GYRKSQRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVLGEGGSGGALGIGVADRVI 167
Cdd:TIGR00513 136 GYRKALRLMKMAERFKMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 168 MLSHSIYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDEGE-GAHLDPERVMQNLKVVLKQALDELL 246
Cdd:TIGR00513 216 MLEYSTYSVISPEGCAAILWKDASKAPKAAEAMKITAPDLKELGLIDSIIPEPLgGAHRNPLAAAASLKEQLLADLATLD 295
|
250 260
....*....|....*....|
gi 446633057 247 PMDANERCEARYQRLMKFGS 266
Cdd:TIGR00513 296 QLSTEELKNRRYQKLMSLGY 315
|
|
| ACCA |
pfam03255 |
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ... |
9-100 |
3.73e-60 |
|
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: 187.23 E-value: 3.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 9 AWTTVQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPEG 88
Cdd:pfam03255 53 PWQKVQLARHPERPYTLDYIEALFDDFIELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEG 132
|
90
....*....|..
gi 446633057 89 YRKSQRLLDMAE 100
Cdd:pfam03255 133 YRKALRLMKLAE 144
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| AccA |
COG0825 |
Acetyl-CoA carboxylase alpha subunit [Lipid transport and metabolism]; Acetyl-CoA carboxylase ... |
9-266 |
3.94e-157 |
|
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: 439.47 E-value: 3.94e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 9 AWTTVQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPEG 88
Cdd:COG0825 54 PWQKVQLARHPQRPYTLDYIEAIFTDFIELHGDRAFGDDPAIVGGLARFDGRPVMVIGHQKGRDTKERIKRNFGMPHPEG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 89 YRKSQRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATV-----------LGeggsgga 157
Cdd:COG0825 134 YRKALRLMKLAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIISVVigeggsggalaIG------- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 158 lgigVADRVIMLSHSIYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDEGE-GAHLDPERVMQNLKV 236
Cdd:COG0825 207 ----VGDRVLMLEHSIYSVISPEGCASILWKDASKAPEAAEALKITAQDLKELGIIDEIIPEPLgGAHRDPEAAAENLKE 282
|
250 260 270
....*....|....*....|....*....|
gi 446633057 237 VLKQALDELLPMDANERCEARYQRLMKFGS 266
Cdd:COG0825 283 ALLKALKELKGLSPEELLEQRYEKFRAIGR 312
|
|
| PRK05724 |
PRK05724 |
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated |
8-266 |
6.93e-150 |
|
acetyl-CoA carboxylase carboxyltransferase subunit alpha; Validated
Pssm-ID: 235580 [Multi-domain] Cd Length: 319 Bit Score: 421.47 E-value: 6.93e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 8 KAWTTVQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPE 87
Cdd:PRK05724 56 TPWQKVQLARHPQRPYTLDYIELLFTDFTELHGDRAFADDKAIVGGLARLNGRPVMVIGHQKGRDTKEKIRRNFGMPRPE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 88 GYRKSQRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVLGEGGSGGALGIGVADRVI 167
Cdd:PRK05724 136 GYRKALRLMKMAEKFGLPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLKVPIICTVIGEGGSGGALAIGVGDRVL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 168 MLSHSIYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDE--GeGAHLDPERVMQNLKVVLKQALDEL 245
Cdd:PRK05724 216 MLEYSTYSVISPEGCASILWKDASKAPEAAEAMKITAQDLKELGIIDEIIPEplG-GAHRDPEAAAAALKEALLEALAEL 294
|
250 260
....*....|....*....|.
gi 446633057 246 LPMDANERCEARYQRLMKFGS 266
Cdd:PRK05724 295 KGLSPEELLERRYEKFMSIGR 315
|
|
| AccA_sub |
NF041504 |
carboxyltransferase subunit alpha; |
10-265 |
3.44e-134 |
|
carboxyltransferase subunit alpha;
Pssm-ID: 469391 [Multi-domain] Cd Length: 257 Bit Score: 379.49 E-value: 3.44e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 10 WTTVQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPEGY 89
Cdd:NF041504 1 WQKVQVARHPDRPHALDYIAALFTDFTELHGDRLFGDDPAIVGGLGRFRGRPVTVIGQEKGSDTEERLRHNFGMARPEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 90 RKSQRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVLGEGGSGGALGIGVADRVIML 169
Cdd:NF041504 81 RKALRLMELAEKFGRPVITLIDTPGAYPGVGAEERGQAEAIARSIEAMLQLTVPNIAVIIGEGGSGGALALANANRVLML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 170 SHSIYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDEGE-GAHLDPERVMQNLKVVLKQALDELLPM 248
Cdd:NF041504 161 EHAIYSVISPEGCASILWRDASRAQEAAEALKLTAQDLLKLGLIDQIIPEPLgGAHRDPAALIAALGDAIEEALAELAGL 240
|
250
....*....|....*..
gi 446633057 249 DANERCEARYQRLMKFG 265
Cdd:NF041504 241 SADELIAQRREKFLAMG 257
|
|
| accA |
TIGR00513 |
acetyl-CoA carboxylase, carboxyl transferase, alpha subunit; The enzyme acetyl-CoA carboxylase ... |
8-266 |
5.42e-115 |
|
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: 332.93 E-value: 5.42e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 8 KAWTTVQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPE 87
Cdd:TIGR00513 56 GAWQRLQLARHPDRPYTLDYIELIFDDFFELAGDRAYADDKAIVGGIARLDGRPVVVIGHQKGRDTKEKLRRNFGMPAPE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 88 GYRKSQRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVLGEGGSGGALGIGVADRVI 167
Cdd:TIGR00513 136 GYRKALRLMKMAERFKMPIITFIDTPGAYPGIGAEERGQSEAIARNLREMARLGVPVICTVIGEGGSGGALAIGVGDKVN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 168 MLSHSIYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDEGE-GAHLDPERVMQNLKVVLKQALDELL 246
Cdd:TIGR00513 216 MLEYSTYSVISPEGCAAILWKDASKAPKAAEAMKITAPDLKELGLIDSIIPEPLgGAHRNPLAAAASLKEQLLADLATLD 295
|
250 260
....*....|....*....|
gi 446633057 247 PMDANERCEARYQRLMKFGS 266
Cdd:TIGR00513 296 QLSTEELKNRRYQKLMSLGY 315
|
|
| PRK12319 |
PRK12319 |
acetyl-CoA carboxylase subunit alpha; Provisional |
13-264 |
2.06e-85 |
|
acetyl-CoA carboxylase subunit alpha; Provisional
Pssm-ID: 183435 [Multi-domain] Cd Length: 256 Bit Score: 255.86 E-value: 2.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 13 VQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPEGYRKS 92
Cdd:PRK12319 8 LKEARDQGRLTTLDYATLIFDDFMELHGDRHFRDDGAVVGGIGYLAGQPVTVVGIQKGKNLQDNLKRNFGQPHPEGYRKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 93 QRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVLGEGGSGGALGIGVADRVIMLSHS 172
Cdd:PRK12319 88 LRLMKQAEKFGRPVVTFINTAGAYPGVGAEERGQGEAIARNLMEMSDLKVPIIAIIIGEGGSGGALALAVADQVWMLENT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 173 IYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDEgegAHLDPERVMQNLKVVLKQALDELLPMDANE 252
Cdd:PRK12319 168 MYAVLSPEGFASILWKDGSRATEAAELMKITAGELLEMGVVDKVIPE---HGYFSSEIIDMIKKNLIEELAQLSQKPLEQ 244
|
250
....*....|..
gi 446633057 253 RCEARYQRLMKF 264
Cdd:PRK12319 245 LLEERYQRFRKY 256
|
|
| accA |
CHL00198 |
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional |
13-265 |
7.69e-83 |
|
acetyl-CoA carboxylase carboxyltransferase alpha subunit; Provisional
Pssm-ID: 214393 [Multi-domain] Cd Length: 322 Bit Score: 251.27 E-value: 7.69e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 13 VQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPEGYRKS 92
Cdd:CHL00198 64 LHLVRQSERPTTLDYIPYILDEWIELHGDRGGSDDPALVGGIGKINGRTIVFLGHQRGRNTKENVLRNFGMPSPGGYRKA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 93 QRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVLGEGGSGGALGIGVADRVIMLSHS 172
Cdd:CHL00198 144 LRLMKHANKFGLPILTFIDTPGAWAGVKAEKLGQGEAIAVNLREMFSFEVPIICTIIGEGGSGGALGIGIGDSIMMLEYA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 173 IYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDEGEG-AHLDPERVMQNLKVVLKQALDELLPMDAN 251
Cdd:CHL00198 224 VYTVATPEACAAILWKDSKKSLDAAEALKITSEDLKVLGIIDEIIPEPIGgAQADPASASKILKKKLIRQLDFLKILSPS 303
|
250
....*....|....
gi 446633057 252 ERCEARYQRLMKFG 265
Cdd:CHL00198 304 ELKAHRYEKFRKLG 317
|
|
| PLN03230 |
PLN03230 |
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional |
13-265 |
2.19e-78 |
|
acetyl-coenzyme A carboxylase carboxyl transferase; Provisional
Pssm-ID: 178769 [Multi-domain] Cd Length: 431 Bit Score: 243.70 E-value: 2.19e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 13 VQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPEGYRKS 92
Cdd:PLN03230 131 LSVARHPNRPTFLDHVLNMTDKWVELHGDRAGFDDPAIVCGIGSMEGMSFMFIGHQKGRNTKENIYRNFAMPQPNGYRKA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 93 QRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVLGEGGSGGALGIGVADRVIMLSHS 172
Cdd:PLN03230 211 LRFMRHAEKFGFPILTFVDTPGAYAGIKAEELGQGEAIAFNLREMFGLRVPIIATVIGEGGSGGALAIGCGNRMLMMENA 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 173 IYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDEG-EGAHLDPERVMQNLKVVLKQALDELLPMDAN 251
Cdd:PLN03230 291 VYYVASPEACAAILWKSAAAAPKAAEALRITAAELVKLGVVDEIVPEPlGGAHSDPLQASKNIKEVILRHMKELMKMDPE 370
|
250
....*....|....
gi 446633057 252 ERCEARYQRLMKFG 265
Cdd:PLN03230 371 ELLQDRAAKFRKIG 384
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
13-265 |
3.80e-66 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 219.34 E-value: 3.80e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 13 VQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPEGYRKS 92
Cdd:PLN03229 152 VNIARHPNRPTFLDHIFNITDKFVELHGDRAGYDDPAIVTGIGTIDGKRYMFIGHQKGRNTKENIMRNFGMPTPHGYRKA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 93 QRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVLGEGGSGGALGIGVADRVIMLSHS 172
Cdd:PLN03229 232 LRMMYYADHHGFPIVTFIDTPGAYADLKSEELGQGEAIAHNLRTMFGLKVPIVSIVIGEGGSGGALAIGCANKLLMLENA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 173 IYSVISPEGCASILWKTAEKAAQASEALGLTADKLQSLGIVEYVVDEG-EGAHLDPERVMQNLKVVLKQALDELLPMDAN 251
Cdd:PLN03229 312 VFYVASPEACAAILWKSAKAAPKAAEKLRITAQELCRLQIADGIIPEPlGGAHADPSWTSQQIKIAINENMDELGKMDTE 391
|
250
....*....|....
gi 446633057 252 ERCEARYQRLMKFG 265
Cdd:PLN03229 392 ELLKHRMLKFRKIG 405
|
|
| ACCA |
pfam03255 |
Acetyl co-enzyme A carboxylase carboxyltransferase alpha subunit; Acetyl co-enzyme A ... |
9-100 |
3.73e-60 |
|
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: 187.23 E-value: 3.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 9 AWTTVQIARHPERPQFLDYVGEIFTEFDALHGDRLFGDDGAMVGGLARFDGQPVMVIGQHRGRSTREKLKHNFGMCNPEG 88
Cdd:pfam03255 53 PWQKVQLARHPERPYTLDYIEALFDDFIELHGDRLFGDDPAIVGGLARFDGQPVMVIGHQKGRDTKENIKRNFGMPHPEG 132
|
90
....*....|..
gi 446633057 89 YRKSQRLLDMAE 100
Cdd:pfam03255 133 YRKALRLMKLAE 144
|
|
| Carboxyl_trans |
pfam01039 |
Carboxyl transferase domain; All of the members in this family are biotin dependent ... |
50-194 |
9.39e-11 |
|
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: 61.51 E-value: 9.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 50 MVGGLARFDGQPVMVIGQHRgrstreklKHNFGMCNPEGYRKSQRLLDMAERFNLPVFTFIDTMGAYPGVGAEERGQAEA 129
Cdd:pfam01039 282 VVTGFARLGGIPVGVVANQP--------RVGAGVLFPDSADKAARFIRDCDAFNLPLVILADVPGFLPGQRQEYGGILKH 353
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 130 IATSLAQLSSLKVPVIaTVLGEGG-----SGGALGIGVADRVIMLSHSIYSVISPEGCASILWKTAEKAA 194
Cdd:pfam01039 354 GAKLLYALAEATVPKI-TVIPRKAyggayVVMDSKINGADINFAWPTARIAVMGPEGAVEIKFRKEKAAA 422
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
32-149 |
6.97e-08 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 53.11 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 32 FTEFDALHGDRLFGDD-----GAMVGGLARFDGQPVMVIGQhrgrstreklkhNF----GMCNPEGYRKSQRLLDMAERF 102
Cdd:COG4799 49 FLELGALAGHRMYDDDdrvpgDGVVTGIGTVDGRPVVVVAN------------DFtvkgGSLGPMTAKKILRAQDIALEN 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446633057 103 NLPVFTFIDTMGAYPGVGAEERGQAEAIATSLAQlSSLKVPVIATVL 149
Cdd:COG4799 117 GLPVIYLVDSGGARLQEGVESFAGYGRIFYRNAR-SSGGIPQISVIM 162
|
|
| MmdA |
COG4799 |
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism]; |
34-149 |
4.22e-05 |
|
Acetyl-CoA carboxylase, carboxyltransferase component [Lipid transport and metabolism];
Pssm-ID: 443827 [Multi-domain] Cd Length: 508 Bit Score: 44.63 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 34 EFDALHgdRLFGDdgAMVGGLARFDGQPVMVIGQHRgrstreklKHNFGMCNPEGYRKSQRLLDMAERFNLPVFTFIDTM 113
Cdd:COG4799 292 SFFEFK--PLYGP--NIVTGFARIDGRPVGIVANQP--------MVLAGVLDIDAADKAARFIRLCDAFNIPLVFLVDVP 359
|
90 100 110
....*....|....*....|....*....|....*.
gi 446633057 114 GAYPGVGAEERGQAEAIATSLAQLSSLKVPVIATVL 149
Cdd:COG4799 360 GFMVGTEQERGGIIRHGAKLLYAVAEATVPKITVIL 395
|
|
| PLN02820 |
PLN02820 |
3-methylcrotonyl-CoA carboxylase, beta chain |
15-149 |
8.73e-04 |
|
3-methylcrotonyl-CoA carboxylase, beta chain
Pssm-ID: 178415 [Multi-domain] Cd Length: 569 Bit Score: 40.56 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446633057 15 IARHPERPQFL-----DYV---GEIFTEFDALHGDRLFGDD---GAMVGGLARFDGQPVMVIGQH---RGrstreklkhn 80
Cdd:PLN02820 73 VKRHRSRNKLLpreriDRLldpGSPFLELSQLAGHELYGEDlpsGGIVTGIGPVHGRLCMFVANDptvKG---------- 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446633057 81 fGMCNPEGYRKSQRLLDMAERFNLPVFTFIDTMGAYPGVGAE---ERGQAEAIATSLAQLSSLKVPVIATVL 149
Cdd:PLN02820 143 -GTYYPITVKKHLRAQEIAAQCRLPCIYLVDSGGANLPRQAEvfpDRDHFGRIFYNQARMSSAGIPQIALVL 213
|
|
|